Anti-gal3 antibodies and methods of use

Abstract

To provide anti-Gal3 antibodies and methods of use.SOLUTION: Disclosed herein are antibodies and compositions used for binding to Gal3. Some embodiments allow for disrupting interactions between Gal3 and cell surface markers and / or proteins associated with neurological diseases and / or proteopathies, such as Alzheimer's disease. Additionally, disclosed herein are methods of treatment and uses of antibodies or binding fragments thereof for treatment of fibrosis, liver fibrosis, kidney fibrosis, cardiac fibrosis, pulmonary fibrosis, non-alcoholic fatty liver disease, non-alcoholic steatohepatitis, sepsis, atopic dermatitis, psoriasis, cancer, brain cancer, breast cancer, colorectal cancer, kidney cancer, liver cancer, lung cancer, pancreatic cancer, bladder cancer, stomach cancer, hematological malignancy, neurological diseases and / or proteopathies. Furthermore, some embodiments provided herein can cross the blood-brain barrier and can be conjugated or otherwise associated with one or more payloads for the treatment of a neurological disease.SELECTED DRAWING: Figure 1

Description

[Technical Field]

[0001] CROSS-REFERENCE TO RELATED APPLICATIONS This application claims the benefit of priority to U.S. Provisional Patent Application No. 62 / 960,300, filed January 13, 2020, U.S. Provisional Patent Application No. 63 / 024,327, filed May 13, 2020, U.S. Provisional Patent Application No. 63 / 092,069, filed October 15, 2020, and U.S. Provisional Patent Application No. 63 / 122,409, filed December 7, 2020, each of which is expressly incorporated by reference herein in its entirety, including any appendices filed therewith.

[0002] Sequence Listing Reference This application is submitted with an electronic Sequence Listing, which is provided as a file entitled SeqListingIMMUT027WO.TXT, 875,600 bytes in size, created and last updated on January 12, 2021. The information in the electronic Sequence Listing is incorporated herein by reference in its entirety.

[0003] Field Embodiments of the present disclosure generally relate to antibodies or binding fragments thereof that bind to galectin-3 (Gal3). These antibodies or binding fragments thereof can block or interfere with the interaction of Gal3 with cell surface markers and / or proteins associated with neurological disorders and / or proteopathies. These antibodies or binding fragments thereof can also cross the blood-brain barrier. [Background technology]

[0004] Galectin-3 (Gal3, GAL3) is a lectin, or carbohydrate-binding protein, with specificity for beta-galactosides. In human cells, Gal3 is expressed and can be found in the nucleus, cytoplasm, cell surface, and extracellular space. Gal3 recognizes and interacts with beta-galactose conjugates on various proteins. [Prior art documents] [Patent documents]

[0005] [Patent Document 1] International Publication No. 2019 / 023247 [Patent Document 2] PCT Application International Publication No. 2020 / 160156 [Patent Document 3] U.S. Patent No. 5,985,660 [Patent Document 4] European Patent No. 404,097 [Patent Document 5] International Publication No. 93 / 11161 [Patent Document 6] International Publication No. 00 / 24782 [Patent Document 7] US Patent Application Publication No. 2003 / 0133939 [Patent Document 8] U.S. Patent No. 6,162,963 [Patent Document 9] U.S. Patent No. 6,150,584 [Patent Document 10] U.S. Patent No. 6,174,708 [Patent Document 11] U.S. Patent No. 5,624,659 [Patent Document 12] U.S. Patent No. 6,187,287 [Patent Document 13] European Patent No. 0,329,400 [Patent Document 14] U.S. Patent No. 5,270,202 [Patent Document 15] European Patent No. 699,755 [Patent Document 16] U.S. Patent No. 5,969,108 [Patent Document 17] U.S. Patent No. 5,695,937 [Patent Document 18] U.S. Patent No. 5,405,783 [Patent Document 19] U.S. Patent No. 5,412,087 [Patent Document 20] U.S. Patent No. 5,445,934 [Patent Document 21] U.S. Patent No. 5,208,020 [Patent Document 22] U.S. Patent No. 5,416,064 [Patent Document 23] U.S. Patent No. 7,276,497 [Patent Document 24] U.S. Patent No. 6,716,821 [Patent Document 25] US Patent Application Publication No. 2013 / 029900 [Patent Document 26] US Patent Application Publication No. 2013 / 0323268 [Patent Document 27] U.S. Patent No. 6,884,869 [Patent Document 28] U.S. Patent No. 7,659,241 [Patent Document 29] U.S. Patent No. 7,498,298 [Patent Document 30] U.S. Patent No. 7,964,566 [Patent Document 31] U.S. Patent No. 7,750,116 [Patent Document 32] U.S. Patent No. 8,288,352 [Patent Document 33] U.S. Patent No. 8,703,714 [Patent Document 34] U.S. Patent No. 8,871,720 [Patent Document 35] U.S. Patent No. 8,404,678 [Patent Document 36] U.S. Patent No. 8,163,736 [Patent Document 37] U.S. Patent No. 8,426,402 [Patent Document 38] U.S. Patent No. 8,802,667 [Patent Document 39] U.S. Patent No. 8,809,320 [Patent Document 40] U.S. Patent No. 6,562,806 [Patent Document 41] U.S. Patent No. 6,608,192 [Patent Document 42] U.S. Patent No. 7,704,924 [Patent Document 43] U.S. Patent No. 7,067,511 [Patent Document 44] U.S. Patent No. 7,612,062 [Patent Document 45] U.S. Patent No. 7,244,724 [Patent Document 46] U.S. Patent No. 7,528,126 [Patent Document 47] U.S. Patent No. 7,049,311 [Patent Document 48] U.S. Patent No. 8,633,185 [Patent Document 49] U.S. Patent No. 8,501,934 [Patent Document 50] U.S. Patent No. 8,697,688 [Patent Document 51] US Patent Application Publication No. 2014 / 0294868 [Patent Document 52] U.S. Patent No. 8,697,688 [Patent Document 53] U.S. Patent No. 9,242,013 [Patent Document 54] US Patent Application Publication No. 2014 / 0286970 [Patent Document 55] U.S. Patent No. 8,936,910 [Patent Document 56] International Publication No. 2014 / 140317 [Patent Document 57] U.S. Patent and Trademark Office Publication No. 2015 / 0105539 [License 58] U.S. Patent and Trademark Office Publication No. 2015 / 0105540 [Patent Document 59] U.S. Patent No. 9,089,614 [License 60] International Publication No. 2015 / 038426 [License 61] U.S. Patent No. 6,821,783 [Non-licensed literature]

[0006] [Non-licensed Document 1] Kabat et al., Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, Md., 1991 [Non-licensed Document 2] Chothia and Lesk, J Mol Biol 196(4): 901-917, 1987 [Non-licensed Document 3] Lefranc et al., 2003 Dev Comp Immunol. 27:55-77 [Non-licensed Document 4] Kunik et al., 2012, Nucl Acids Res. W521-4

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[0007] Disclosure Overview Disclosed herein are embodiments relating to anti-Gal3 antibodies, binding fragments thereof, and / or antigen-binding molecules. In some embodiments, any such construct can be used to block the interaction of Gal3 with cell surface markers.

[0008] In some embodiments, these cell surface markers are associated with diseases, such as cancer or fibrosis. In some embodiments, any such structure prevents abnormal protein folding or accumulation. In some embodiments, any such structure can be used to treat neurological disorders, such as, but not limited to, Alzheimer's disease.

[0009] In some embodiments, any such structure may be used to aid in crossing the blood-brain barrier. In some embodiments, these articles may be associated with one or more payloads.

[0010] (1)V H -CDR1, V H -CDR2, and V H a heavy chain variable region comprising CDR3, and (2) a V L -CDR1, V L -CDR2, and V L Disclosed herein are anti-Gal3 antibodies or binding fragments thereof comprising a light chain variable region comprising V-CDR3. H - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 36-44, 588-615. H - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 54-60, 616-643. H - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 70 to 81, 644 to 671. L - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 92-101, 672-699. L - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 111 to 116, 700 to 727. L - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 127 to 135, 728 to 755.

[0011] Also disclosed herein are methods for treating a neurological disorder in a subject in need thereof. In some embodiments, the method comprises administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the neurological disorder in the subject.

[0012] Also disclosed herein are methods for disrupting the binding of Gal3 to APP or Aβ, or both. In some embodiments, the method includes contacting APP or Aβ, or both, with an anti-Gal3 antibody or a binding fragment thereof, thereby disrupting the binding of Gal3 to APP.

[0013] Also disclosed herein are methods for treating a proteopathy in a subject in need thereof. In some embodiments, the method comprises administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the proteopathy in the subject.

[0014] Also disclosed herein are methods of administering an antibody to a subject. In some embodiments, the method comprises administering to a subject an anti-Gal3 antibody or binding fragment thereof.

[0015] Also disclosed herein are methods for promoting neuronal regeneration in a subject in need thereof. In some embodiments, the method comprises administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby promoting neuronal regeneration in the subject.

[0016] Also disclosed herein are methods for disrupting the binding of Gal3 to a cell surface receptor. In some embodiments, the method includes contacting Gal3 with an anti-Gal3 antibody or binding fragment thereof, thereby disrupting the binding of Gal3 to the cell surface receptor.

[0017] Also disclosed herein are methods for treating a disease, such as an inflammatory disease, cancer, and / or fibrosis, in a subject in need thereof. In some embodiments, the disease includes fibrosis, liver fibrosis, kidney fibrosis, cardiac fibrosis, pulmonary fibrosis, non-alcoholic fatty liver disease, non-alcoholic steatohepatitis, sepsis, atopic dermatitis, psoriasis, cancer, brain cancer, breast cancer, colorectal cancer, kidney cancer, liver cancer, lung cancer, pancreatic cancer, bladder cancer, gastric cancer, or hematological malignancies. In some embodiments, the method includes administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the disease in the subject.

[0018] Also disclosed are anti-Gal3 antibodies or binding fragments thereof for use in treating diseases, such as inflammatory diseases, cancer, and / or fibrosis, in a subject in need thereof.

[0019] Also disclosed herein is an anti-Gal3 antibody or binding fragment thereof for use in treating a neurodegenerative disorder in a subject in need thereof.

[0020] Also disclosed herein is an anti-Gal3 antibody or binding fragment thereof for use in treating a proteopathy in a subject in need thereof.

[0021] Also disclosed herein is an anti-Gal3 antibody or binding fragment thereof for use in promoting neuronal regeneration in a subject in need thereof.

[0022] Antibody conjugates are also disclosed herein. In some embodiments, the antibody conjugate comprises an anti-Gal3 antibody or its binding fragment and a payload conjugated to the anti-Gal3 antibody or its binding fragment. In some embodiments, the antibody conjugate can cross the blood-brain barrier. In some embodiments, the barrier is in a subject with a weakened or altered blood-brain barrier due to a disease that affects the blood-brain barrier, for example, that reduces the structural integrity of the barrier.

[0023] Also disclosed herein are multispecific antibodies. In some embodiments, the multispecific antibodies comprise a first binding domain that binds to Gal3 and a second binding domain that binds to a therapeutic target molecule located in the brain of a subject.

[0024] Also disclosed herein is a method for delivering a payload to the central nervous system of a subject in need thereof. In some embodiments, the method comprises administering to the subject an antibody conjugate comprising an anti-Gal3 antibody or a binding fragment thereof and a payload conjugated to the anti-Gal3 antibody or a binding fragment thereof, wherein the antibody conjugate can cross the blood-brain barrier. In some embodiments, the barrier is in a subject with a weakened or altered blood-brain barrier due to a disease that affects the blood-brain barrier, for example, that reduces the structural integrity of the barrier.

[0025] Also disclosed herein are methods for increasing the permeability of a payload across the blood-brain barrier of a subject in need thereof. In some embodiments, the method comprises conjugating an anti-Gal3 antibody or a binding fragment thereof to a payload to form an antibody conjugate. In some embodiments, the barrier is in a subject with a weakened or altered blood-brain barrier due to a disease that affects the blood-brain barrier, for example, that reduces the structural integrity of the barrier.

[0026] Also disclosed herein is the use of an anti-Gal3 antibody or binding fragment thereof to assist a payload in crossing the blood-brain barrier of a subject.

[0027] Also disclosed herein are methods for disrupting the interaction of Gal3 with transforming growth factor beta (TGF-b) receptor.

[0028] Also disclosed herein are methods of treating fibrosis in a subject in need thereof.

[0029] Also disclosed herein are methods of treating non-alcoholic fatty liver disease (NAFLD) or non-alcoholic steatohepatitis (NASH) in a subject in need thereof.

[0030] Also disclosed herein are methods of treating an immune-related disorder in a subject in need thereof.

[0031] Also disclosed herein are methods for disrupting the interaction of Gal3 with tumor cell surface markers.

[0032] Also disclosed herein are methods of treating cancer in a subject in need thereof.

[0033] Also disclosed herein are methods for identifying an antibody or binding fragment thereof as having the ability to interfere with the interaction of Gal3 with a TGF-b receptor, a cell surface marker, or a tumor cell surface marker.

[0034] Pharmaceutical compositions or medicaments are also disclosed herein. In some embodiments, the pharmaceutical composition or medicament comprises any one of the anti-Gal3 antibodies or binding fragments thereof, any one of the antibody conjugates, or any one of the multispecific antibodies disclosed herein, and at least one pharmaceutically acceptable diluent, excipient, or carrier. In some embodiments, the composition or medicament is used to treat fibrosis, liver fibrosis, non-alcoholic fatty liver disease (NAFLD), non-alcoholic steatohepatitis (NASH), kidney fibrosis, cardiac fibrosis, arterial fibrosis, venous thrombosis, or pulmonary fibrosis. In some embodiments, the composition or medicament is used to treat cancer. In some embodiments, the composition or medicament is used to treat immune-related disorders.

[0035] Also disclosed herein are anti-Gal3 antibodies or binding fragments thereof for use in treating fibrosis, liver fibrosis, NAFLD, NASH, kidney fibrosis, cardiac fibrosis, arterial fibrosis, venous thrombosis, or pulmonary fibrosis.

[0036] Also disclosed herein are anti-Gal3 antibodies or binding fragments thereof for use in the treatment of cancer.

[0037] Also disclosed herein are anti-Gal3 antibodies or binding fragments thereof for use in inhibiting tumor cell growth in vitro.

[0038] Also disclosed herein is an anti-Gal3 antibody or binding fragment thereof for use in slowing brain tumor growth.

[0039] Also disclosed herein are antibodies that bind to human Gal3 and compete with anti-Gal3 antibodies or binding fragments thereof for binding to human Gal3. In some embodiments, the antibody competes with any one of the anti-Gal3 antibodies or binding fragments disclosed herein.

[0040] Also disclosed herein are methods for identifying antibodies or binding fragments that have the ability to interfere with the interaction of Gal3 with TGF-b receptor.

[0041] Also disclosed herein are antibodies or binding fragments thereof that bind to the N-terminal domain and / or TRD of Gal3.

[0042] Also disclosed herein are proteins comprising one or more peptide sequences having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 18-27. [Brief explanation of the drawings]

[0043] In addition to the features described above, additional features and variations will be readily apparent from the following description of the drawings and illustrative embodiments. It should be understood that these drawings depict typical embodiments and are not intended to be limiting in scope. [Figure 1]FIG. 1 depicts a graphical representation of the assessment of the relative binding affinity of APP695 to galectin-3 (GAL3) from different sources as measured by enzyme-linked immunosorbent assay (ELISA). [Figure 2] FIG. 2 depicts a graphical representation of the assessment of the relative binding affinities of APP695 and GAL3 after blocking with anti-GAL3 antibodies as measured by ELISA. [Figure 3] FIG. 3 depicts the results of a hippocampus-dependent memory test (Morris water maze) for APPSwe transgenic and wild-type control mice treated with an isotype control or anti-GAL3 antibody (TB001) before and after antibody treatment. [Figure 4] FIG. 4 depicts a graphical representation of the number of crossings during the probe trail phase of the Morris water maze for APPSwe transgenic animals and wild-type controls. [Figure 5A] FIG. 5A depicts the results of an analysis of Aβ protein levels in brain tissue of APPSwe transgenic and wild-type mice as determined by immunoblotting using a monoclonal Aβ-specific sequence-dependent antibody (6E10). [Figure 5B] FIG. 5B depicts a graphical representation of the intensities of the bands in FIG. 5A as determined by Image J software. [Figure 5C] FIG. 5C depicts the results of analysis of mTB001 in brain tissue of APPSwe transgenic and wild-type mice as measured by ELISA. [Figure 6A] FIG. 6A shows the results of the Morris water maze test for Aβ42 fibril-injected mice treated with isotype control or anti-GAL3 antibody (TB001) and wild-type (uninjected) controls prior to antibody treatment. [Figure 6B] FIG. 6B shows the results of the Morris water maze test for Aβ42 fibril-injected mice treated with isotype control or anti-GAL3 antibody (TB001) and wild-type (uninjected) controls after antibody treatment. [Figure 7] FIG. 7 depicts a graphical representation of the number of crossings during the exploration trial phase of the Morris water maze test for Aβ42 fibril-injected mice treated with isotype control or anti-GAL3 antibody (TB001) and wild-type (uninjected) controls. [Figure 8A] FIG. 8A depicts a graphical representation of the results of immunohistochemical staining of the levels of Aβ with 6E10 antibody in mouse brain tissue as quantified by NIH Image J software. [Figure 8B] FIG. 8B depicts a graphical representation of the results of immunohistochemical staining of the levels of NeuN in mouse brain tissue as quantified by NIH Image J software. [Figure 8C] FIG. 8C depicts a graphical representation of the results of immunohistochemical staining of phospho-tau levels in mouse brain tissue as quantified by NIH Image J software. [Figure 8D] FIG. 8D depicts a graphical representation of the results of immunohistochemical staining of the levels of Iba-1 in mouse brain tissue as quantified by NIH Image J software. [Figure 8E] FIG. 8E depicts a graphical representation of the results of immunohistochemical staining of the levels of galectin-3 in mouse brain tissue as quantified by NIH Image J software. [Figure 9] FIG. 9 depicts a graphical representation of immunoblot band intensities of Aβ protein levels in brain tissues of Aβ42 fibril-injected and wild-type mice analyzed by Image J software. [Figure 10A] FIG. 10A depicts a graphical representation of the assessment of the relative binding affinities of Aβ42 peptides from different sources to Gal3 as measured by ELISA. [Figure 10B] FIG. 10B depicts a graphical representation of the assessment of the relative binding affinities of Aβ42 oligomers from different sources to Gal3 as measured by ELISA. [Figure 11A]FIG. 11A depicts a graphical representation of the assessment of the relative binding affinity of Aβ42 peptides after blocking with anti-Gal3 antibodies as measured by ELISA. [Figure 11B] FIG. 11B depicts a graphical representation of the assessment of relative binding affinity of Aβ42 oligomers after blocking with anti-Gal3 antibody as measured by ELISA. [Figure 11C] FIG. 11C depicts a graphical representation of the comparison of the efficacy of blocking the interaction of Aβ42 and Gal3 between anti-Gal3 antibodies (TB001 and TB006) or the small molecule Gal3 inhibitor TD139. [Figure 12A] FIG. 12A depicts a graphical representation of the assessment of the relative binding affinity of TLR4 to Gal3 from different sources as measured by ELISA. [Figure 12B] FIG. 12B depicts a graphical representation of the assessment of the relative binding affinities of TLR4 and Gal3 after blocking with anti-Gal3 antibodies as measured by ELISA. [Figure 13A] FIG. 13A depicts a graphical representation of the assessment of the relative binding affinity of TREM2 to Gal3 from different sources as measured by ELISA. [Figure 13B] FIG. 13B depicts a graphical representation of the assessment of the relative binding affinities of TREM2 and Gal3 after blocking with anti-Gal3 antibodies as measured by ELISA. [Figure 14A] FIG. 14A depicts a graphical representation of the assessment of the relative binding affinities of tau oligomers and Gal3 after blocking with anti-Gal3 antibodies as measured by ELISA. [Figure 14B] FIG. 14B depicts a graphical representation of the assessment of the relative binding affinities of tau oligomers from different sources to Gal3 as measured by ELISA. [Figure 15A] FIG. 15A depicts a graphical representation of the assessment of the relative binding affinities of alpha-synuclein and Gal3 after blocking with anti-Gal3 antibodies as measured by ELISA. [Figure 15B]FIG. 15B depicts a graphical representation of the assessment of the relative binding affinity of alpha-synuclein to Gal3 from different sources as measured by ELISA. [Figure 16-1] Figure 16-1 depicts the protein sequences of Gal3, amyloid-beta precursor protein (APP) isoform c (APP695), amyloid-beta peptide (1-42), and TGF-b receptor. [Figure 16-2] Figure 16-2 depicts the protein sequence of the TGF-b receptor, as well as other designated protein sequences. [Figure 16-3] Figure 16-3 depicts other designated protein sequences. [Figure 16-4] Figure 16-4 depicts other designated protein sequences. [Figure 16-5] Figure 16-5 depicts other designated protein sequences. [Figure 16-6] Figure 16-6 depicts other designated protein sequences. [Figure 16-7] Figure 16-7 depicts other designated protein sequences. [Figure 16-8] Figure 16-8 depicts other designated protein sequences. [Figure 16-9] Figure 16-9 depicts other designated protein sequences. [Figure 17] FIG. 17 depicts the peptide sequence of Gal3 used to generate and analyze antibodies. [Figure 18] 18 depicts an exemplary variable heavy chain complementarity determining region (CDR) 1 of an anti-Gal3 antibody disclosed herein. In some embodiments, any of the compositions or methods provided herein can comprise one or more of the CDRs provided herein. [Figure 19] 19 depicts an exemplary variable heavy chain CDR2 of an anti-Gal3 antibody disclosed herein. In some embodiments, any of the compositions or methods provided herein can comprise one or more of the CDRs provided herein. [Figure 20] Figure 20 depicts an exemplary variable heavy chain CDR3 of an anti-Gal3 antibody disclosed herein. In some embodiments, any of the compositions or methods provided herein can comprise one or more of the CDRs provided herein. [Figure 21] 21 depicts an exemplary variable light chain CDR1 of an anti-Gal3 antibody disclosed herein. In some embodiments, any of the compositions or methods provided herein can comprise one or more of the CDRs provided herein. [Figure 22] 22 depicts an exemplary variable light chain CDR2 of an anti-Gal3 antibody disclosed herein. In some embodiments, any of the compositions or methods provided herein can comprise one or more of the CDRs provided herein. [Figure 23] Figure 23 depicts an exemplary variable light chain CDR3 of an anti-Gal3 antibody disclosed herein. In some embodiments, any of the compositions or methods provided herein can comprise one or more of the CDRs provided herein. [Figure 24-1] Figure 24-1 depicts exemplary heavy chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VH sequences provided herein. [Figure 24-2] Figure 24-2 depicts exemplary heavy chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VH sequences provided herein. [Figure 24-3] Figure 24-3 depicts exemplary heavy chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VH sequences provided herein. [Figure 24-4] Figure 24-4 depicts exemplary heavy chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VH sequences provided herein. [Figure 24-5] Figure 24-5 depicts exemplary heavy chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VH sequences provided herein. [Figure 25-1] Figure 25-1 depicts exemplary light chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VL sequences provided herein. [Figure 25-2] Figure 25-2 depicts exemplary light chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VL sequences provided herein. [Figure 25-3] Figure 25-3 depicts exemplary light chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VL sequences provided herein. [Figure 25-4] Figure 25-4 depicts exemplary light chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VL sequences provided herein. [Figure 25-5]Figure 25-5 depicts exemplary light chain variable region sequences of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the VL sequences provided herein. [Figure 26-1] Figure 26-1 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-2] Figure 26-2 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-3] Figure 26-3 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-4] Figure 26-4 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-5] Figure 26-5 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-6] Figure 26-6 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-7]Figure 26-7 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 26-8] Figure 26-8 depicts exemplary heavy chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain sequences provided herein. [Figure 27-1] Figure 27-1 depicts exemplary light chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain sequences provided herein. [Figure 27-2] Figure 27-2 depicts exemplary light chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain sequences provided herein. [Figure 27-3] Figure 27-3 depicts exemplary light chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain sequences provided herein. [Figure 27-4] Figure 27-4 depicts exemplary light chain sequences of the anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain sequences provided herein. [Figure 28] 28 depicts exemplary combinations of variable heavy chain CDR1, CDR2, and CDR3 of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chain CDR combinations provided herein. [Figure 29] 29 depicts exemplary combinations of variable light chain CDR1, CDR2, and CDR3 of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chain CDR combinations provided herein. [Figure 30] Figure 30 depicts exemplary combinations of heavy and light chain CDRs of the anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy and light chain CDR combinations provided herein. [Figure 31] 31 depicts exemplary combinations of heavy and light chain variable regions of the anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the combinations of heavy and light chain variable regions provided herein. [Figure 32] 32 depicts exemplary combinations of heavy and light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy and light chains provided herein. [Figure 33] FIG. 33 depicts peptides found to bind to exemplary antibodies disclosed herein (following the peptide nomenclature depicted in FIG. 17 and discussed herein) and binning of these exemplary antibodies. [Figure 34A] FIG. 34A depicts the plasma concentration of an exemplary anti-Gal3 antibody conjugated to biotin in C57BL6 mice implanted with GL261-LUC murine glioblastoma tumors 4 days after iv administration of the anti-Gal3 antibody. [Figure 34B]Figure 34B depicts the concentration of an exemplary anti-Gal3 antibody conjugated to biotin found in tumor and normal brain tissue of C57BL6 mice implanted with GL261-LUC mouse glioblastoma tumors 4 days after iv administration of the anti-Gal3 antibody. [Figure 34C] Figure 34C depicts the relative concentrations of biotin-conjugated anti-Gal3 antibody found in either tumors or normal brain tissue of C57BL6 mice implanted with GL261-LUC mouse glioblastoma tumors compared to their respective plasma 4 days after iv administration of anti-Gal3 antibody. [Figure 34D] FIG. 34D depicts immunoblots of the apoptotic marker PARP and GAPDH loading control in brain tumor lysates isolated from C57BL6 mice implanted with GL261-LUC murine glioblastoma tumors after iv administration of anti-Gal3 antibody. [Figure 34E] FIG. 34E depicts a graphical representation of the relative amounts of PARP normalized to the GAPDH loading control quantified from the immunoblots in FIG. 34D. [Figure 35-1] Figure 35-1 depicts an alignment of some embodiments of the VH or VL CDR regions of various embodiments of anti-Gal3 antibodies. In some embodiments, any method or composition provided herein can use any one, two, three, four, five, six, or seven of the consensus CDRs provided herein. [Figure 35-2] Figure 35-2 depicts an alignment of some embodiments of the VH or VL CDR regions of various embodiments of anti-Gal3 antibodies. In some embodiments, any method or composition provided herein can use any one, two, three, four, five, six, or seven of the consensus CDRs provided herein. [Figure 35-3]Figure 35-3 depicts an alignment of some embodiments of the VH or VL CDR regions of various embodiments of anti-Gal3 antibodies. In some embodiments, any method or composition provided herein can use any one, two, three, four, five, six, or seven of the consensus CDRs provided herein. [Figure 35-4] Figure 35-4 depicts an alignment of some embodiments of the VH or VL CDR regions of various embodiments of anti-Gal3 antibodies. In some embodiments, any method or composition provided herein can use any one, two, three, four, five, six, or seven of the consensus CDRs provided herein. [Figure 35-5] Figure 35-5 depicts an alignment of some embodiments of the VH or VL CDR regions of various embodiments of anti-Gal3 antibodies. In some embodiments, any method or composition provided herein can use any one, two, three, four, five, six, or seven of the consensus CDRs provided herein. [Figure 36] FIG. 36 depicts the KD(M) values ​​of Gal3 binding for exemplary anti-Gal3 antibodies disclosed herein. [Figure 37-1] Figure 37-1 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-2] Figure 37-2 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-3]Figure 37-3 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-4] Figure 37-4 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-5] Figure 37-5 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-6] Figure 37-6 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-7] Figure 37-7 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-8] Figures 37-8 depict nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-9]Figure 37-9 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-10] Figure 37-10 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 37-11] Figure 37-11 depicts nucleic acid sequences encoding exemplary heavy chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chain variable regions encoded by the nucleic acids provided herein. [Figure 38-1] Figure 38-1 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-2] Figure 38-2 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-3] Figure 38-3 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-4]Figure 38-4 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-5] Figure 38-5 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-6] Figure 38-6 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-7] Figure 38-7 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-8] Figure 38-8 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-9] Figure 38-9 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-10]Figure 38-10 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 38-11] Figure 38-11 depicts nucleic acid sequences encoding exemplary light chain variable regions of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chain variable regions encoded by the nucleic acids provided herein. [Figure 39-1] Figure 39-1 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-2] Figure 39-2 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-3] Figure 39-3 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-4] Figure 39-4 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-5]Figure 39-5 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-6] Figure 39-6 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-7] Figure 39-7 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-8] Figure 39-8 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-9] Figure 39-9 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-10] Figure 39-10 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-11]Figure 39-11 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-12] Figure 39-12 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-13] Figure 39-13 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-14] Figure 39-14 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-15] Figure 39-15 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-16] Figure 39-16 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-17]Figure 39-17 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-18] Figure 39-18 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-19] Figure 39-19 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-20] Figure 39-20 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-21] Figure 39-21 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-22] Figure 39-22 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-23]Figure 39-23 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 39-24] Figure 39-24 depicts nucleic acid sequences encoding exemplary heavy chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the heavy chains encoded by the nucleic acids provided herein. [Figure 40-1] Figure 40-1 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-2] Figure 40-2 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-3] Figure 40-3 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-4] Figure 40-4 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any of the compositions or methods provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-5]Figure 40-5 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-6] Figure 40-6 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-7] Figure 40-7 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-8] Figure 40-8 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-9] Figure 40-9 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-10] Figure 40-10 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-11]Figure 40-11 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 40-12] Figure 40-12 depicts nucleic acid sequences encoding exemplary light chains of anti-Gal3 antibodies disclosed herein. In some embodiments, any composition or method provided herein can include one or more of the light chains encoded by the nucleic acids provided herein. [Figure 41A] Figure 41A depicts a graphical representation of an assessment of the relative binding affinity of transforming growth factor beta (TGF-b) receptor type 1 (TGFBR1), TGF-b receptor type 2 (TGFBR2), TGF-b receptor type 3 (TGFBR3), or a combination thereof, to galectin-3 (GAL3) as measured by enzyme-linked immunosorbent assay (ELISA). [Figure 41B] FIG. 41B depicts the binding kinetics of the interaction of Gal3 with the TGF-b receptor as measured by surface plasmon resonance. [Figure 42] FIG. 42 depicts a graphical representation of the assessment of the relative binding affinities of TGFBR1 and GAL3 after blocking with anti-GAL3 antibodies as measured by ELISA. [Figure 43A] Figure 43A depicts a graphical representation of the assessment of the relative expression of genes associated with fibrosis in LX2 cells treated with TGF-b and either mouse anti-GAL3 antibody or vehicle control as measured by quantitative reverse transcriptase polymerase chain reaction (qRT-PCR). [Figure 43B] Figure 43B depicts a graphical representation of the assessment of the relative expression of genes associated with fibrosis in LX2 cells treated with TGF-b and either humanized anti-GAL3 antibody or vehicle control as measured by qRT-PCR. [Figure 44A]FIG. 44A depicts a graphical representation of an assessment of the relative binding affinities of VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, and PDGFRb to galectin-3 as measured by enzyme-linked immunosorbent assay (ELISA). [Figure 44B] Figure 44B depicts a graphical representation of the assessment of the relative binding affinities of ErbB2, HGFR (cMet), TNF sRI, CTLA4, CD47, and PD-L1 to galectin-3 as measured by enzyme-linked immunosorbent assay (ELISA). [Figure 44C] FIG. 44C depicts a graphical representation of the assessment of the relative binding affinity of FGFR1 alpha-IIIb to galectin-3 as measured by enzyme-linked immunosorbent assay (ELISA). [Figure 44D] FIG. 44D depicts a graphical representation of the assessment of the relative binding affinities of FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR IIIc, FGFR4 to galectin-3 as measured by enzyme-linked immunosorbent assay (ELISA). [Figure 44E-1] FIG. 44E-1 depicts a graphical representation of the determination of binding affinity of VEGFR2, VEGFR3, and EGFR to Gal3 as measured by SPR. [Figure 44E-2] FIG. 44E-2 depicts a graphical representation of the determination of the binding affinity of PDGFRa, PDGFRb, and ErbB2 to Gal3 as measured by SPR. [Figure 44E-3] FIG. 44E-3 depicts a graphical representation of the determination of binding affinity of VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, and ErbB2 to Gal3 as measured by SPR. [Figure 45A] FIG. 45A depicts a graphical representation of the assessment of the relative binding affinity of the tumor surface receptor EGFR to Gal3 after blocking with anti-Gal3 antibodies as measured by ELISA. [Figure 45B]FIG. 45B depicts a graphical representation of the assessment of the relative binding affinity of the tumor surface receptor VEGFR2 to Gal3 after blocking with anti-Gal3 antibody as measured by ELISA. [Figure 45C] FIG. 45C depicts a graphical representation of the assessment of the relative binding affinity of the tumor surface receptor VEGFR3 to Gal3 after blocking with anti-Gal3 antibody as measured by ELISA. [Figure 45D] FIG. 45D depicts a graphical representation of the assessment of the relative binding affinity of the tumor surface receptor PDGFRa to Gal3 after blocking with anti-Gal3 antibody as measured by ELISA. [Figure 45E] FIG. 45E depicts a graphical representation of the assessment of the relative binding affinity of the tumor surface receptor PDGFRb to Gal3 after blocking with anti-Gal3 antibody as measured by ELISA. [Figure 46A-1] FIG. 46A-1 depicts a graphical representation of the determination of the binding affinity of anti-Gal3 antibody clone 6H6 to full-length recombinant human Gal3 (rhGal3) or the C-terminal domain of Gal3 (Gal3-CRD) as measured by SPR. [Figure 46A-2] FIG. 46A-2 depicts a graphical representation of the determination of the binding affinity of anti-Gal3 antibody clone 6H6 to full-length recombinant human Gal3 (rhGal3) or the C-terminal domain of Gal3 (Gal3-CRD) as measured by SPR. [Figure 46B-1] FIG. 46B-1 depicts a graphical representation of the determination of the binding affinity of anti-Gal3 antibody clone 2D10 to full-length recombinant human Gal3 (rhGal3) or the C-terminal domain of Gal3 (Gal3-CRD) as measured by SPR. [Figure 46B-2] FIG. 46B-2 depicts a graphical representation of the determination of the binding affinity of anti-Gal3 antibody clone 2D10 to full-length recombinant human Gal3 (rhGal3) or the C-terminal domain of Gal3 (Gal3-CRD) as measured by SPR. [Figure 47A]FIG. 47A depicts a graphical representation of percent survival for hepatocellular carcinoma (HCC) cells (Hep3B, HepG2) following exposure to anti-Gal3 antibody for a duration of 72 hours compared to untreated controls. [Figure 47B] FIG. 47B depicts a graphical representation of percent survival for glioblastoma (GBM) tumor cells (U118) following exposure to anti-Gal3 antibody for a duration of 72 hours compared to untreated controls. [Figure 48] FIG. 48 depicts a graphical representation of the percent survival for GBM tumor cells (lines U87MG, U118, LN229) following exposure to control isotype and anti-Gal3 antibodies (2D10) alone or in combination with 100 μM temozolomide (TMZ) over a 72 hour duration compared to untreated controls. [Figure 49] Figure 49 depicts a graphical representation of tumor progression in GL261-LUC-implanted animals treated with control isotype, TMZ, anti-Gal3 antibody (2D10), or combination (TMZ+2D10), determined as the fold change in luminescence emission (flux / sec) after the start of treatment. [Figure 50] Figure 50 depicts the antibody affinity (KD) of anti-Gal3 humanized antibodies IMT001 (TB001) and IMT006 (TB006; 4A11.H3L1) for human, cynomolgus, and mouse Gal3. Both humanized IMT001 and IMT006, derived from mouse mAbs, have high affinity for human and cynomolgus Gal3, while IMT001 also has high affinity for mouse Gal3. [Figure 51] Figure 51 depicts a graphic representation of the inhibition of TGF-β-induced procollagen production in LX-2 cells when treated with IMT001 (TB001), IMT006 (TB006; 4A11.H3L1), and hIgG4 (isotype control) at increasing concentrations of antibody. LX-2 cells were stimulated with TGF-β (10 ng / mL) for 2 hours. [Figure 52]Figure 52 depicts a graphical representation of the inhibition of TGF-β-induced procollagen production and Gal3 expression in LX-2 cells when treated with IMT001 and 4A11.H3L1. TGF-β-stimulated expression of procollagen in LX-2 cells is increased by exogenous Gal3 and inhibited by IMT006. Gal3 increased on the LX-2 cell surface (Panel A) and in the culture medium (Panel B) in response to TGF-β stimulation. The anti-Gal3 antibody IMT006 reduced procollagen protein after either TGF-β treatment or TGF-β + rhGal3. [Figure 53] Figure 53 depicts a graphical representation of reduced Gal3 and membrane TGFBR2 expression in LX2 cells transfected with a Gal3 short hairpin RNA (shRNA) vector, as well as reduced membrane TGFbR1 expression in control LX-2 cells treated with IMT001. TGFbR2 and Gal3 expression were reduced on the cell surface of LX-2 cells as a result of Gal3 knockdown. LX-2 cells were transfected with either a short hairpin RNA vector for silencing Gal3 or a control vector, and single clones were isolated (designated LX-shGal3 and LX2-shCon, respectively). After treatment with TGF-b, Gal3 expression was significantly reduced in LX2-shGal3 compared to LX2-shCon. TGFbR2 and Gal3 expression on the cell membrane of LX2-shGal3 cells was reduced compared to LX2-shCon cells. In non-transfected LX-2 cells, treatment with IMT001 reduced plasma membrane TGFbR1. [Figure 54] Figure 54 depicts a graphical representation of the inhibition of TGF-β-induced procollagen production in LX-2 cells transfected with Gal3 shRNA vectors. Knockdown of Gal3 in LX-2 cells reduces TGF-β-induced procollagen production. The TGF-β EC50 for procollagen production in the LX2-scrambled control was 1.01 ng / mL, and the TGF-β EC50 for procollagen production in the LX2-shGal3 Gal3 knockdown cells was 2.04 ng / mL. [Figure 55] Figure 55 depicts a graphical representation of the pharmacokinetics of IMT001 in rats, with a half-life of approximately 2 weeks. The PK of IMT001 is dose-proportional in rats, with a half-life of approximately 2 weeks. [Figure 56] Figure 56 depicts a graphic representation of the tissue distribution of TB006 (IMT006, 4A11.H3L1) in mice after a single injected dose. ELISA was used to measure IMT006 exposure in plasma and tissues. [Figure 57] Figure 57 depicts a graphical representation of the assay of total and unbound Gal3 in rat plasma after treatment with IMT001. A single dose of IMT001 was given via iv at 3 mg / kg (n=3) and 30 mg / kg (n=4). Samples were collected 21 days after dosing. In SD rats treated with 30 mg / kg IMT001, there was a 2.97-fold increase in total rGal3. Unbound rGal3 was approximately 85% lower than total rGal3 in SD rats treated with 30 mg / kg IMT001. Compared to untreated rats, unbound rGal3 was 55% lower after treatment with IMT001. [Figure 58] Figure 58 depicts a graphical representation of transcriptomics in methionine-choline deficient (MCD) mice treated with mIMT001 (mouse IMT001). Statistical analysis was performed by Student's T-test; *p<0.05, **p<0.01, ***p<0.001. Significantly enriched biological functions (by clusterProfiler analysis) were observed for both genes whose expression was induced in the NASH model and genes that were inhibited by Ab treatment (overlap in the Venn diagram). [Figure 59-1] FIG. 59-1 depicts a graphical representation of Gal3 and TGFbR1 expression in the liver of MCD mice after treatment with mIMT001. [Figure 59-2] Figure 59-2 depicts a graphical representation of Gal3 and TGFbR1 expression in the liver of MCD mice after treatment with mIMT001. [Figure 60] FIG. 60 depicts a graphic representation of Gal3 and TGFbR1 expression in the liver of MCD mice after treatment with mIMT001. [Figure 61] Figure 61 depicts a graphical representation of co-immunoprecipitation analysis of TGFbR1 and TGFbR2 binding to immunoprecipitated Gal3. 293T cells were transfected with TGFbR1, TGFbR2, and Gal3-FLAG plasmids alone or in the combinations depicted. Cell lysates were collected 24 hours after transfection and analyzed by FLAG IP. Overexpressed Gal3 pulled down TGFbR1 / 2 with high specificity. The upper band in the TGFbR2 blot is glycosylated TGFbR2, and the lower band is unglycosylated TGFbR2. [Figure 62] Figure 62 depicts a graphical representation of Western blot analysis of Smad3 expression and phosphorylation status in LX-2 cells after TGF-β stimulation. LX2 cells were starved for 24 hours. Cells were exposed to 2 ng / mL of TGF-β alone or in combination with the indicated concentrations of control antibodies, IMT001 or IMT006. Cell lysates were analyzed for levels of SMAD3 and phosphorylated SMAD3 protein. GAPDH levels were used as a loading control. [Figure 63A] Figure 63A depicts a Western blot showing that Gal3 promotes the aggregation of Aβ into oligomeric forms. Aβ oligomers were detected using antibody A11, and total Aβ was detected using antibody 6E10. [Figure 63B] Figure 63B depicts a dot blot of Aβ oligomers incubated with different concentrations of anti-Gal3 antibody mTB001 (0, 10, 100 μg). The dot blot shows that Aβ oligomerization was reversed by the anti-Gal3 antibody. Aβ oligomers were detected with antibody A11, and total Aβ was detected with antibody 6E10. [Figure 63C] Figure 63C depicts quantification of the dot blot in Figure 63B detected with Aβ oligomer antibody A11. [Figure 63D-1] Figure 63D-1 depicts a dot blot of Aβ oligomers incubated with different anti-Gal3 antibodies disclosed herein. Number labels correspond to the anti-Gal3 antibodies depicted in this figure. [Figure 63D-2] Figure 63D-2 depicts a dot blot of Aβ oligomers incubated with different anti-Gal3 antibodies disclosed herein. Number labels correspond to the anti-Gal3 antibodies depicted in this figure. [Figure 64] Figure 64 depicts antibody names used throughout this disclosure, which refer to the same antibody (exemplary peptide and nucleic acid sequences are provided elsewhere in this disclosure and are appropriately attributed to at least one of the depicted names) and may be used interchangeably. Names shown in a row correspond to the same antibody. [Figure 65A] Figure 65A depicts a dot blot of the time course of aggregation of Aβ-42 peptide into oligomeric forms when incubated with various isoforms of Gal3. Gal3 isoforms tested include full-length Gal3 (expressed as E. coli), hGal3-R186S, hGal3-P64H, hGal3-65-250 (amino acids 65-250), and hGal3-CRD-His (His-tagged C-terminal domain of Gal3). Lane "0" represents no Gal3 added. The time course was performed over a 5-hour period. [Figure 65B] Figure 65B depicts the quantification of the dot blot in Figure 65A. [Figure 65C] Figure 65C depicts a dot blot of the time course of aggregation of Aβ-42 peptide into oligomeric forms when incubated with various short peptides of Gal3. Peptides A to F were tested (SEQ ID NOs: 582 to 587). hGal3-65-250 was used as a positive control. DETAILED DESCRIPTION OF THE INVENTION

[0044] Detailed Description of the Disclosure Some embodiments provided herein relate to an anti-Gal3 antibody or binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3.

[0045] Some embodiments provided herein relate to anti-Gal3 antibodies or binding fragments thereof that disrupt the interaction of Gal3 with proteins associated with proteopathies or neurological diseases. In some embodiments, there are methods and uses of the anti-Gal3 antibodies and binding fragments thereof disclosed herein for the treatment of proteopathies and / or neurological diseases.

[0046] Some embodiments provided herein relate to an anti-Gal3 antibody or binding fragment thereof that can cross the blood-brain barrier. In some embodiments, the blood-brain barrier is that of a subject with a neurological disease. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is a multispecific antibody that increases the permeability of another antibody across the blood-brain barrier. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is conjugated to a payload that increases the permeability of the payload across the blood-brain barrier.

[0047] Some embodiments provided herein relate to anti-Gal3 antibodies or binding fragments thereof that disrupt the interaction of Gal3 with cell surface markers or tumor cell surface markers. In some embodiments, there are methods and uses of the anti-Gal3 antibodies and binding fragments thereof disclosed herein for treating diseases associated with cell surface markers or tumor cell surface markers. In some embodiments, the disease is cancer, fibrosis, or an immune-related disorder.

[0048] Galectin-3 (Gal3, GAL3) plays an important role in cell proliferation, adhesion, differentiation, angiogenesis, and apoptosis. This activity is due, at least in part, to its immunomodulatory properties and binding affinity for other immunomodulatory proteins, signaling proteins, and other cell surface markers. Gal3 functions through distinct N- and C-terminal domains. The N-terminal domain (isoform 1: amino acids 1–111) contains a tandem repeat domain (TRD, isoform 1: amino acids 36–109) and is largely responsible for Gal3 oligomerization. The C-terminal domain (isoform 1: amino acids 112–250) contains a carbohydrate recognition binding domain (CRD) that binds β-galactosides.

[0049] Galectin-3 (Gal3) has been implicated in immunomodulatory activity. An example of this is the interaction of Gal3 with T-cell immunoglobulin-mucin domain-containing molecule-3 (TIM-3), which can lead to suppression of immune responses, such as T-cell activation, and allow cancer cells to escape immune clearance. This phenomenon and methods for inhibiting it are explored in U.S. Patent No. 6,223,629 (expressly incorporated herein by reference in its entirety). Anti-Gal3 antibodies and methods of use thereof are also explored, for example, in U.S. Patent No. 6,223,629 (expressly incorporated herein by reference in its entirety).

[0050] There is a long-lasting need for a deeper understanding of whether Gal3 plays a role in disease.Some diseases that may be associated with Gal3 include cancer, fibrosis, inflammatory disease, neurological disease and proteopathy, such as Alzheimer's disease.There is also a need for the development of new and improved treatments for these diseases.

[0051] Disclosed herein are various embodiments of anti-Gal3 antibodies or binding fragments thereof and methods of use, for example, for the treatment of diseases described above or otherwise provided herein.

[0052] Disclosed herein are antibodies or binding fragments thereof that bind to or are selective for Gal3, and compositions thereof. Also disclosed herein are methods for using anti-Gal3 antibodies or binding fragments thereof to disrupt the interaction of Gal3 with cell surface markers and / or proteins associated with fibrosis, liver fibrosis, kidney fibrosis, cardiac fibrosis, pulmonary fibrosis, non-alcoholic fatty liver disease, non-alcoholic steatohepatitis, sepsis, atopic dermatitis, psoriasis, cancer, brain cancer, breast cancer, colorectal cancer, kidney cancer, liver cancer, lung cancer, pancreatic cancer, bladder cancer, gastric cancer, hematological malignancies, neurodegenerative diseases, and / or proteopathies (e.g., those caused by protein misfolding or aggregation in a subject), for example, to treat diseases in a subject.

[0053] In some embodiments, the method involves an antibody that binds to Gal3 and disrupts the interaction of Gal3 with another protein. This can result in direct blockage of the interaction zone between Gal3 and the other protein, or indirect alteration, such as a conformational change in Gal3 such that Gal3 no longer binds to or is active with the other protein. It can also result from binding to the first section of Gal3, with some other portion of the antibody disrupting or altering the interaction of Gal3 with the other protein. In some embodiments, the first section of Gal3 is the N-terminal domain of Gal3, the tandem repeat domain (TRD) of Gal3, or the C-terminal domain of Gal3. In some embodiments, the antibody that binds to Gal3 does not bind to the C-terminal domain of Gal3. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, can be replaced with an antigen-binding molecule that binds to Gal3.

[0054] Alzheimer's disease (AD) is a progressive neurodegenerative disorder and the most common type of dementia. Amyloid beta (Aβ) is a major component of amyloid plaques and is therefore suspected to be a pathogenic contributor to AD. Proteolytic cleavage of the amyloid precursor protein (APP; including isoforms such as APP695) generates Aβ peptides, the aggregation of which is associated with the development of AD. Serum levels of Gal3 increase with the severity of memory loss in AD patients. Gal3 is specifically expressed in microglia, which are associated with Aβ plaques. Gal3 expression is also significantly increased in the frontal cortex of AD patients, in parallel with enhanced Aβ oligomerization. O-glycosylation can occur at Tyr-10 of Aβ peptides in human cerebrospinal fluid and is increased in AD patients.

[0055] Disclosed herein are antibodies specific for Gal3 and binding fragments thereof, and methods of using them for the treatment or prevention of neurodegenerative diseases and / or proteopathies (e.g., Alzheimer's disease). The anti-Gal3 antibodies and binding fragments thereof disclosed herein disrupt the interaction of Gal3 with proteins associated with neurodegenerative diseases and / or proteopathies. In some embodiments, the proteins associated with neurodegenerative diseases and / or proteopathies cause disease in subjects due to protein misfolding or aggregation. One non-limiting example of a protein associated with neurodegenerative diseases and / or proteopathies is amyloid-beta (Aβ) peptide.

[0056] In some embodiments, the anti-Gal3 antibodies or binding fragments disclosed herein disrupt the interaction of Gal3 with APP695. Some exemplary antibodies that strongly (e.g., at least 90%) disrupt the interaction of Gal3 with APP695 include 19B5.2E6, 7D8.2D8, F846C.1B2, F846C.1H12, F846TC.14A2, F849C.8D10, F849C.8H3, 4A11.H3L1 [IMT006-5 (TB006)], 15F Some exemplary antibodies that moderately (e.g., at least 45%) disrupt the interaction of Gal3 with APP695 include, but are not limited to, 10.2D6, F846TC.16B5, 23H9.2E4, F846C.1F5, IMT001-4[TB001], F846C.2H3, 14H10.2C9, 15FG7.2A7, 20H5.A3, F846TC.14E4, 3B11.2G2, 20D11.2C6, and 2D10.2B2. Some exemplary antibodies that moderately (e.g., at least 45%) disrupt the interaction of Gal3 with APP695 include, but are not limited to, 13G4.2F8, F846TC.7F10, F847C.12F12, and F847C.4B10. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0057] In some embodiments, the anti-Gal3 antibodies or binding fragments disclosed herein disrupt the interaction of Gal3 with Aβ (e.g., Aβ monomers, oligomers, or fibrils, or any combination thereof). Some exemplary antibodies that strongly (e.g., at least 90%) disrupt the interaction of Gal3 with Aβ monomers include, but are not limited to, 2D10.2B2, 20D11.2C6, 3B11.2G2, 20H5.A3, 846TC.14E4, 15G7.2A7, 14H10.2C9, 846C.2H3, TB001, 846C.1F5, 846TC.16B5, TB006, 846C.1B2, 846TC.14A2, 849C.8D10, and 19B5.2E6. Some exemplary antibodies that strongly (e.g., at least 90%) disrupt the interaction between Gal3 and Aβ oligomers include, but are not limited to, 2D10.2B2, 20D11.2C6, 3B11.2G2, 20H5.A3, 846TC.14E4, 14H10.2C9, TB001, 846C.1F5, and TB006. In some embodiments, the anti-Gal3 antibodies or binding fragments disclosed herein block the interaction between Gal3 and Aβ oligomers better than the small molecule Gal3 inhibitor TD139. In some embodiments, any of the anti-Gal3 antibodies or binding fragments thereof, or any configuration of any of the anti-Gal3 antibodies or binding fragments provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0058] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can at least one of, if not both, enhance cognitive function and / or attenuate the accumulation of toxic conformational species of Aβ, e.g., Aβ oligomers and / or Aβ fibrils, in a subject.

[0059] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can reduce inflammation (e.g., inflammation of the brain) and / or encephalitis in a subject.

[0060] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can do one or more of the following in the brain of a subject: reduce phospho-tau levels, reduce microglial activation (as detected by an Iba-1 antibody), or reduce Gal3 levels.

[0061] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can at least one of regenerating neuronal structures and / or reducing extracellular Aβ in a subject, if not both.

[0062] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can promote microglial phagocytic function and promote clearance of Aβ deposits in a subject.

[0063] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can inhibit Aβ aggregate (e.g., Aβ oligomers or Aβ fibrils)-mediated activation of microglia in a subject.

[0064] In some embodiments, administering any one of the anti-Gal3 antibodies or binding fragments disclosed herein can block the interaction of Gal3 with TLR4 or TREM2, or both.

[0065] Also provided herein are embodiments relating to anti-Gal3 antibodies or binding fragments and their use in methods of disrupting the interaction of Gal3 with cell surface markers, such as TGF-β, VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR, TNF-sRI, CTLA4, CD47, PD-L1, FGFR, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR IIIc, or FGFR4. In some embodiments, this disruption can be used to alter biological processes regulated by these cell surface markers. In some embodiments, the cell surface marker is a tumor cell surface marker, a cancer cell surface marker, or a fibrocyte surface marker.

[0066] Cells use a wide range of signaling molecules and cognate cell surface receptors for signal transduction and cell communication. Abnormal function of these interactions has been linked to many diseases and disorders. For example, TGF-β is a potent signaling molecule that acts with pleiotropic effects, including modulation of immune processes during the progression of cancer or fibrosis, such as liver fibrosis.

[0067] For example, biological processes regulated by TGF-β include (but are not limited to): a) TGF-β regulates many biological responses, including tissue fibrosis (liver, kidney, lung, heart, etc.), cell proliferation, apoptosis, differentiation, autophagy, and immune responses; b) TGF-β plays an essential role in liver physiology and pathology, contributing to all stages of disease progression, from liver injury to inflammation, fibrosis, cirrhosis, and hepatocellular carcinoma; c) TGF-β also mediates the epithelial-mesenchymal transition process in hepatocytes, which can directly or indirectly contribute to an increase in the myofibroblast (MFB) population; hepatic stellate cell (HSC) activation is one of the most important steps during liver fibrosis; and d) TGF-β plays an essential role in the activation of HSCs into MFBs, which are the major cause of extracellular matrix protein accumulation and prominent mediators of fibrosis. Therefore, in some embodiments, any one or more of the above processes can be disrupted through the use of Gal3 antibodies that reduce binding of Gal3 to the TGF-β receptor.

[0068] TGF-β binds to the TGF-βRII receptor, which binds to and phosphorylates TGF-βRI, triggering the recruitment of receptor-regulated SMAD proteins (R-SMADs) SMAD2 and SMAD3 to the cytoplasmic domain of activated TGF-βRI, which then phosphorylates SMAD2 / 3. Upon phosphorylation, SMAD2 / 3 form a trimer with SMAD4, which then translocates to the nucleus, where it binds to SMAD-binding elements and modulates gene expression. In some embodiments, the antibodies or binding fragments provided herein alter the binding of TGF-β to TGF-βRII by altering the manner in which TGF-β binds to its receptor. In some embodiments, the antibodies or binding fragments do not alter the binding of TGF-β to TGF-βRII by altering the manner in which TGF-β binds to Gal3.

[0069] TGF-β activates a number of SMAD-independent signaling pathways, referred to as non-canonical TGF-β pathways, such as the WNT, ERK, P38, MAPK, PI3K, and AKT pathways. In some embodiments, the antibodies or binding fragments provided herein can alter the manner in which TGF-β binds to its receptor, thereby altering the manner in which TGF-β activates these multiple SMAD-independent signaling pathways.

[0070] Inflammation plays a key role in the development of liver fibrosis. After injury, infiltrating immune cells (macrophages, lymphocytes, eosinophils, and plasma cells) are recruited to the damaged site. Lymphocytes produce secreted protein signaling molecules called cytokines and chemokines, which activate macrophages. Activated macrophages then stimulate inflammatory cells, such as lymphocytes, among others, contributing to the sustained maintenance of a pro-inflammatory environment. During fibrosis, macrophages produce pro-fibrotic factors, such as TGF-β and platelet-derived growth factor (PDGF), and control extracellular matrix turnover by regulating the balance of various matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). Macrophages are found in close proximity to collagen-producing myofibroblasts, suggesting that macrophages are highly involved in the activation of MFBs. In this context, hepatic macrophages have been described as a potential target for the treatment of liver fibrosis. In vitro and in vivo studies have demonstrated that both Kupffer cells and monocyte-derived macrophages can activate HSCs and induce their transdifferentiation through paracrine mechanisms, including through TGF-β. Endogenous liver macrophages secrete the chemokine CCL2 (a potent chemoattractant) to recruit monocytes, which can increase and promote fibrosis. Macrophages are essential players in the regulation of liver fibrosis and are an important source of TGF-β. Recent observations point to a role for TGF-β in inducing profibrotic M2-like macrophage localization via SNAIL. M2 activation / localization plays a relevant role in the development of fibrosis in mice and patients with liver fibrosis. Therefore, in some embodiments, the role of TGF-β is altered by applying one or more of the anti-Gal3 antibodies or binding fragments thereof provided herein that disrupt the interaction of Gal3 with the TGF-β receptor, thereby altering one or more of the above pathways or processes.

[0071] In some embodiments, the method involves an antibody or binding fragment thereof that binds to Gal3 and disrupts the interaction of Gal3 with a cell surface marker or cell surface receptor. In some embodiments, the cell surface marker or cell surface receptor is a cell surface marker or cell surface receptor that appears on tumor cells, immune cells, cancer cells, or fibrocytes. This can result in direct blockage of the interaction zone between Gal3 and the cell surface marker or cell surface receptor, or indirect alteration, such as a conformational change in Gal3 such that Gal3 is no longer able to bind to or be active with the cell surface marker or cell surface receptor. It can also result from binding to the first section of Gal3 while some other portion of the antibody disrupts or alters the interaction of Gal3 with the cell surface marker or cell surface receptor.

[0072] In some embodiments, the methods involve antibodies that bind to Gal3 and disrupt the interaction of Gal3 with TGF-beta receptor, VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR, TNF sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, or FGFR4, or any combination thereof. This can result in a direct blockage of the interaction zone between Gal3 and TGF-β receptor, VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR, TNF-sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, or FGFR4, or any combination thereof; or indirect alteration, e.g., a conformational change of Gal3, such that Gal3 no longer interacts with TGF-β receptor, VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR, TNF-sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, or FGFR4, or any combination thereof. The binding can be such that the antibody no longer binds to or is active with TGF-β receptor, VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR, TNF sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, or FGFR4, or any combination thereof. It can also be the result of binding to the first section of Gal3 while some other portion of the antibody interferes with or alters the interaction of Gal3 with TGF-β receptor, VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR, TNF sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, or FGFR4, or any combination thereof.

[0073] In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3. Thus, although the present disclosure also contemplates antigen-binding molecules whenever it refers to an antibody or binding fragment thereof, for brevity, the present disclosure may simply refer to an antibody or binding fragment thereof. It is noted that the term "antigen-binding molecule" encompasses antibodies and binding fragments thereof and represents a broader genus of options.

[0074] This disclosure claims priority to one or more priority documents, which may be submitted with one or more appendices. All subject matter disclosed in the priority documents and any appendices is hereby expressly contemplated as part of the disclosure in this document as further embodiments that can be combined and / or modified with any of the embodiments provided herein. All subject matter disclosed in the priority documents and appendices, including but not limited to antibodies, binding fragments thereof, antigen-binding molecules, and any methods, such as methods of manufacture, use, or treatment, may be applied to any of the embodiments or configurations disclosed in this section of the application. Similarly, all subject matter disclosed herein, including but not limited to antibodies, binding fragments thereof, antigen-binding molecules, and any methods, such as methods of manufacture, use, or treatment, is contemplated as being applied to any of the embodiments or configurations disclosed in the priority documents and appendices.

[0075] definition In the following detailed description, reference is made to the accompanying drawings, which form a part hereof. In the drawings, like symbols typically identify like components, unless context dictates otherwise. The illustrative embodiments described in the detailed description, drawings, and claims are not meant to be limiting. Other embodiments may be utilized, and other changes may be made, without departing from the spirit or scope of the subject matter presented herein. It will be readily understood that the aspects of the present disclosure, as generally described herein and illustrated in the drawings, can be adapted, substituted, combined, separated, and designed in a variety of different configurations, all of which are expressly contemplated herein.

[0076] Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which the claimed subject matter belongs. It is to be understood that the foregoing general description and the following detailed description are exemplary and explanatory only and are not restrictive of any claimed subject matter.

[0077] The section headings used herein are for organizational purposes only and should not be construed as limiting the subject matter described.

[0078] The articles "a" and "an" are used herein to refer to one or to more than one (e.g., to at least one) of the grammatical object of the article. By way of example, "an element" means one element or more than one element.

[0079] By "about" is meant an amount, level, value, number, frequency, percentage, dimension, size, amount, weight or length that varies by up to about 30, 25, 20, 15, 10, 9, 8, 7, 6, 5, 4, 3, 2, or 1% of the referenced quantity, level, value, number, frequency, percentage, dimension, size, amount, weight or length.

[0080] Throughout this specification, unless the context requires otherwise, the words "comprise," "comprises," and "comprising" are understood to imply the inclusion of a recited step or element or group of steps or elements, but not the exclusion of any other step or element or group of steps or elements. By "consisting of," it is meant to include and be limited to whatever precedes the phrase "consisting of." Thus, the phrase "consisting of" indicates that the listed elements are required or mandatory, and that no other elements may be present. By "consisting essentially of," it is meant to include any elements listed before it, and to be limited to other elements that do not interfere with or contribute to the activity or function specified in this disclosure for the listed elements. Thus, the phrase "consisting essentially of" indicates that the listed elements are required or mandatory, but that other elements are optional and may or may not be present depending on whether they substantially affect the activity or function of the listed elements.

[0081] As used herein, the terms "individual," "subject," and "patient" refer to any mammal. In some embodiments, the mammal is a human. In some embodiments, the mammal is a non-human. None of the terms require or are limited to situations characterized by the supervision (e.g., constant or intermittent) of a medical professional (e.g., a physician, registered nurse, nurse practitioner, physician assistant, orderly, or hospice worker).

[0082] The terms "polypeptide", "peptide" and "protein" are used interchangeably herein to refer to any length of amino acid polymer.Polymer may be linear, cyclic or branched, may contain modified amino acids, and may be interspersed with non-amino acids.The term also encompasses modified amino acid polymers, for example, through sulfation, glycosylation, lipidation, acetylation, phosphorylation, iodination, methylation, oxidation, proteolytic processing, phosphorylation, prenylation, racemization, selenoylation, transfer RNA-mediated addition of amino acids to proteins, for example, arginylation, ubiquitination, or any other manipulation, for example, conjugation with a labeling component.

[0083] As used herein, the term "amino acid" refers to either natural and / or unnatural or synthetic amino acids, including glycine and both the D or L optical isomers, as well as amino acid analogs and peptidomimetics.

[0084] A polypeptide or amino acid sequence "derived from" a specified protein refers to the origin of the polypeptide. Preferably, the polypeptide has an amino acid sequence essentially identical to the amino acid sequence of the polypeptide encoded in the sequence, or a portion thereof, comprising at least 10-20 amino acids, or at least 20-30 amino acids, or at least 30-50 amino acids, or an amino acid sequence immunologically identifiable from the polypeptide encoded in the sequence. The term also includes polypeptides expressed from a specified nucleic acid sequence. Peptide sequences having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to any one of the peptide sequences disclosed herein and having the same or similar functional properties are contemplated. The percent homology may be determined according to amino acid substitutions, deletions, or additions between the two peptide sequences. Peptide sequences having any percent homology to any one of the peptide sequences disclosed herein can be prepared and tested by one of skill in the art through conventional methods.

[0085] As used herein, the term "antibody" refers to the meaning ascribed to it by those skilled in the art and is further intended to include any polypeptide chain-containing molecular structure having a unique shape that fits and recognizes an epitope, with one or more non-covalent interactions stabilizing the complex between the molecular structure and the epitope. While the antibodies utilized in the present invention may be polyclonal, monoclonal antibodies are preferred because they can be reproduced in cell culture or recombinantly and can be modified to reduce their antigenicity.

[0086] In addition to whole immunoglobulins (or their recombinant counterparts), immunoglobulin fragments or "binding fragments" containing epitope-binding sites (e.g., Fab', F(ab')2, single-chain variable fragments (scFv), diabodies, minibodies, nanobodies, single-domain antibodies (sdAb), or other fragments) are useful as antibody portions in the present invention. Such antibody fragments can be generated from whole immunoglobulins by ricin, pepsin, papain, or other protease cleavage. Minimal immunoglobulins can be engineered using recombinant immunoglobulin technology. For example, "Fv" immunoglobulins for use in the present invention can be produced by linking the variable light chain region to the variable heavy chain region via a peptide linker (e.g., poly-glycine or another sequence that does not form an alpha-helix or beta-sheet motif). Nanobodies or single-domain antibodies can also be derived from selected organisms, such as dromedaries, camels, llamas, alpacas, or sharks. In some embodiments, the antibody can be a conjugate, such as a pegylated antibody, a drug, a radioisotope, or a toxin conjugate. Monoclonal antibodies directed to a specific epitope or a combination of epitopes can target and / or deplete cell populations that express markers. A variety of techniques using monoclonal antibodies to screen cell populations that express markers are available, including magnetic separation using antibody-coated magnetic beads, "panning" using antibodies attached to a solid matrix (i.e., plate), and flow cytometry (see, e.g., Patent Document 3; expressly incorporated herein by reference in its entirety).

[0087] As known in the art, the term "Fc region" is used to define the C-terminal region of an immunoglobulin heavy chain. The "Fc region" may be a native sequence Fc region or a variant Fc region. Although the boundaries of the Fc region of an immunoglobulin heavy chain can vary, the human IgG heavy chain Fc region is usually defined to stretch from the amino acid residue at position Cys226, or from Pro230, to the carboxyl terminus. The numbering of residues in the Fc region is that of the EU index as in Kabat. (Non-Patent Document 1). The Fc region of an immunoglobulin generally comprises two constant domains, CH2 and CH3. As known in the art, the Fc region can exist in a dimeric or monomeric form.

[0088] As known in the art, a "constant region" of an antibody refers to the constant region of the antibody light chain or the constant region of the antibody heavy chain, either alone or in combination.

[0089] The "variable region" of an antibody refers to the variable region of the antibody light chain or the variable region of the antibody heavy chain, either alone or in combination. As is known in the art, each of the heavy and light chain variable regions consists of four framework regions (FRs) connected by three complementarity-determining regions (CDRs), also known as hypervariable regions, which contribute to the formation of the antigen-binding site of the antibody. When a variant of a subject variable region is desired, particularly one having a substitution of an amino acid residue outside the CDR region (i.e., in the framework region), appropriate amino acid substitutions, preferably conservative amino acid substitutions, can be identified by comparing the subject variable region with the variable regions of other antibodies containing CDR1 and CDR2 sequences in the same canonical class as the subject variable region (Non-Patent Document 2).

[0090] In certain embodiments, definitive delineation of CDRs and identification of the residues that constitute the antibody binding site are achieved by solving the structure of the antibody and / or the structure of the antibody-ligand complex. In certain embodiments, this can be achieved by any of a variety of techniques known to those skilled in the art, such as X-ray crystallography. In certain embodiments, various analytical methods can be used to identify or estimate CDR regions. In certain embodiments, various analytical methods can be used to identify or estimate CDR regions. Examples of such methods include, but are not limited to, the Kabat definition, the Chothia definition, the IMGT approach (Non-Patent Document 3), computer programs such as Paratome (Non-Patent Document 4), the AbM definition, and conformational definitions.

[0091] The Kabat definition is a standard for numbering residues in antibodies and is typically used to identify CDR regions. See, e.g., Non-Patent Document 5. The Chothia definition is similar to the Kabat definition, but takes into account the location of certain structural loop regions. See, e.g., Non-Patent Document 6; Non-Patent Document 7. The AbM definition uses an integrated computer program produced by the Oxford Molecular Group to model antibody structure. See, e.g., Non-Patent Document 8; Non-Patent Document 9. The AbM definition models the tertiary structure of an antibody from its primary sequence using a combination of knowledge databases and ab initio methods, such as those described in Non-Patent Document 10. The contact definition is based on an analysis of available complex crystal structures. See, e.g., Non-Patent Document 11. In another approach, referred to herein as the "conformational definition" of CDRs, the positions of CDRs can be identified as residues that contribute enthalpic-wise to antigen binding. See, e.g., Non-Patent Document 12. Still other CDR boundary definitions may not strictly follow one of the above approaches, but nevertheless overlap with at least a portion of the Kabat CDRs, although they may be shortened or extended in light of predicted or experimental findings that certain residues or groups of residues do not significantly affect antigen binding. As used herein, CDRs can refer to CDRs defined by any approach known in the art, including combinations of approaches. The methods used herein may utilize CDRs defined according to any of these approaches. For any given embodiment containing more than one CDR, the CDRs may be defined according to any of the Kabat, Chothia, extended, IMGT, Paratome, AbM, and / or conformational definitions, or any combination thereof.

[0092] The term "compete," as used herein with respect to antibodies, means that a first antibody, or antigen-binding portion thereof, binds to an epitope in a manner sufficiently similar to that of a second antibody, or antigen-binding portion thereof, such that the binding of the first antibody to its cognate epitope is detectably reduced in the presence of the second antibody compared to the binding of the first antibody in the absence of the second antibody. Binding of the second antibody to its epitope can optionally also be detectably reduced in the presence of the first antibody, but this need not be the case. That is, a first antibody can inhibit binding of a second antibody to its epitope without the second antibody inhibiting binding of the first antibody to its respective epitope. However, antibodies are said to "cross-compete" with each other for binding of their respective epitopes if each antibody detectably inhibits binding of the other antibody to its cognate epitope or ligand, whether to the same, greater, or lesser extent. Both competing and cross-competing antibodies are encompassed by the present invention. Regardless of the mechanism by which such competition or cross-competition occurs (e.g., steric hindrance, conformational change, or binding to a common epitope, or portion thereof), those skilled in the art will recognize that, based on the teachings provided herein, such competing and / or cross-competing antibodies are encompassed and may be useful for the methods disclosed herein.

[0093] An antibody that "preferentially binds" or "specifically binds" (used interchangeably herein) to an epitope is a term well understood in the art, and methods for determining such specific or preferential binding are also well known in the art. A molecule is said to exhibit "specific binding" or "preferential binding" if it reacts or associates more frequently, and / or more rapidly, and / or with a longer duration, and / or with a higher affinity with a particular cell or substance than with alternative cells or substances. An antibody "specifically binds" or "preferentially binds" to a target if it binds with higher affinity and / or avidity and / or more readily and / or with a longer duration than it binds to other substances. For example, an antibody that specifically or preferentially binds to a CFD epitope is an antibody that binds to this epitope with higher affinity and / or avidity, and / or more readily and / or with a longer duration than it binds to other CFD epitopes or non-CFD epitopes. For example, it is understood by reading this definition that an antibody (or portion or epitope) that specifically or preferentially binds to a first target may or may not also specifically or preferentially bind to a second target. Thus, "specific binding" or "preferential binding" does not necessarily require (although can include) exclusive binding. Generally, but not necessarily, reference to binding means preferential binding.

[0094] As used herein, the term "antigen-binding molecule" refers to a molecule comprising an antigen-binding portion that binds to an antigen and, optionally, a scaffold or framework portion that allows the antigen-binding portion to adopt a conformation that facilitates binding of the antigen-binding portion or provides some additional property to the antigen-binding molecule. In some embodiments, the antigen is Gal3. In some embodiments, the antigen-binding portion comprises at least one CDR from an antibody that binds to the antigen. In some embodiments, the antigen-binding portion comprises all three CDRs from the heavy chain of the antibody that binds the antigen or from the light chain of the antibody that binds the antigen. In some embodiments, the antigen-binding portion comprises all six CDRs (three from the heavy chain and three from the light chain) from an antibody that binds the antigen. In some embodiments, the antigen-binding portion is an antibody fragment.

[0095] Non-limiting examples of antigen-binding molecules include antibodies, antibody fragments (e.g., antigen-binding fragments of antibodies), antibody derivatives, and antibody analogs. Further specific examples include, but are not limited to, single-chain variable fragments (scFv), nanobodies (e.g., VH domains of camelid heavy chain antibodies; VHH fragments, see Non-Patent Document 13), Fab fragments, Fab' fragments, F(ab')2 fragments, Fv fragments, Fd fragments, and complementarity-determining region (CDR) fragments. These molecules can be derived from any mammalian source, such as human, mouse, rat, rabbit, pig, dog, cat, horse, donkey, guinea pig, goat, or camelid. Antibody fragments may compete with intact antibodies for target antigen binding, and fragments may be produced by modification of intact antibodies (e.g., enzymatic or chemical cleavage) or synthesized de novo using recombinant DNA technology or peptide synthesis. Antigen-binding molecules can include, for example, alternative protein scaffolds or artificial scaffolds with grafted CDRs or CDR derivatives. Such scaffolds include, but are not limited to, antibody-derived scaffolds containing mutations introduced to stabilize the three-dimensional structure of the antigen-binding molecule, as well as entirely synthetic scaffolds, for example, including biocompatible polymers. See, for example, Non-Patent Document 14; Non-Patent Document 15. Additionally, in addition to peptide antibody mimics ("PAMs"), scaffolds based on antibody mimics that utilize fibronectin components as scaffolds can be used.

[0096] An antigen-binding molecule can also include proteins containing one or more antibody fragments incorporated into a single polypeptide chain or multiple polypeptide chains. For example, antigen-binding molecules may include, but are not limited to, diabodies (see, e.g., Patent Document 4; Patent Document 5; and Non-Patent Document 16); intrabodies; domain antibodies (a single VL or VH domain, or two or more VH domains joined by a peptide linker; see Non-Patent Document 17); maxibodies (two scFvs fused to an Fc region; see Non-Patent Document 18 and Non-Patent Document 19); triabodies; tetrabodies; minibodies (scFvs fused to a CH3 domain; see Non-Patent Document 20); peptibodies (one or more peptides attached to an Fc region; see Patent Document 6); linear antibodies (a pair of tandem Fd segments (VH-CH1-VH-CH1); see Non-Patent Document 21), which form a pair of antigen-binding regions together with complementary light chain polypeptides; small modular immunopharmaceuticals (see Patent Document 7); and immunoglobulin fusion proteins (e.g., IgG-scFv, IgG-Fab, 2scFv-IgG, 4scFv-IgG, VH-IgG, IgG-VH, and Fab-scFv-Fc).

[0097] In certain embodiments, the antigen-binding molecule can have the structure of, for example, an immunoglobulin. An "immunoglobulin" is a tetrameric molecule, with each tetramer containing two identical pairs of polypeptide chains, each pair having one "light" chain (approximately 25 kDa) and one "heavy" chain (approximately 50-70 kDa). The amino-terminal portion of each chain contains a variable region of approximately 100-110 or more amino acids primarily responsible for antigen recognition. The carboxy-terminal portion of each chain defines a constant region primarily responsible for effector function.

[0098] As used herein, the terms "treat" or "treatment" (as understood in the art) refer to an approach to obtain beneficial or desired results in a subject's condition, including clinical results. Beneficial or desired clinical results can include, but are not limited to, the alleviation or amelioration of one or more symptoms or conditions, whether partial or total, and whether detectable or undetectable; a reduction in the extent of the disease; stabilization (i.e., not worsening) of the disease state; prevention of the spread or spread of the disease; delay or slowing of disease progression; remission or palliation of the disease state; reduction in disease recurrence; and remission. "Treat" and "treatment," as used herein, also include prophylactic treatment. Treatment methods include administering a therapeutically effective amount of an active agent to a subject. The administering step may consist of a single administration or may include a series of administrations. The composition is administered to the subject in an amount and for a duration sufficient to treat the subject. The length of the treatment period depends on various factors, such as the severity of the condition, the age and genetic profile of the subject, the concentration of the active agent, the activity of the composition used in the treatment, or a combination thereof. It is also recognized that the effective dosage of an agent used for treatment or prevention may increase or decrease over the course of a particular treatment or prevention regime. Changes in dosage may be determined and revealed by standard diagnostic assays known in the art. In some cases, chronic administration may be required.

[0099] The term "effective amount" or "effective dose" as used herein has its plain and ordinary meaning as understood in light of the present specification, and refers to the amount of the described composition or compound that results in an observable, specified effect. The actual dosage level of the active ingredient in the active composition of the presently disclosed subject matter can be modified to administer an amount of the active composition or compound that is effective to achieve the specified response for a specific subject and / or application. The selected dosage level can be modified based on various factors, including, but not limited to, the activity of the composition, formulation, route of administration, combination with other drugs or treatments, the severity of the condition being treated, and the physical condition and past medical history of the subject being treated. In some embodiments, a minimum dose is administered, and the dose is titrated up in the absence of dose-limiting toxicity to the minimum effective dose. In addition to determining and adjusting the effective dose, evaluation of the timing and method of making such adjustments is contemplated herein.

[0100] The term "administering" includes oral administration, topical contact, administration as a suppository, intravenous, intraperitoneal, intramuscular, intralesional, intrathecal, intranasal, or subcutaneous administration to a subject, or implantation of a slow-release device, such as a mini-osmotic pump. Administration can be by any route, including parenteral and transmucosal (e.g., buccal, sublingual, palatal, gingival, nasal, vaginal, rectal, or transdermal). Parenteral administration can include, for example, intravenous, intramuscular, intraarterial, intradermal, subcutaneous, intraperitoneal, intraventricular, and intracranial. Other modes of delivery include, but are not limited to, the use of liposomal formulations, intravenous infusion, transdermal patches, and the like. By "co-administering" is meant that a first compound described herein is administered simultaneously with, immediately before, or immediately after the administration of a second compound described herein.

[0101] As used herein, the term "therapeutic target" refers to a gene or gene product, the modulation of whose activity (e.g., by expression, modulation of biological activity, etc.) can provide for modulation of a disease phenotype. As used throughout, "modulation" is meant to refer to an increase or decrease in the indicated phenomenon (e.g., modulation of biological activity refers to an increase in biological activity or a decrease in biological activity).

[0102] As used herein, the terms "standard of care," "best practice," and "standard therapy" refer to treatments that are accepted by physicians as appropriate, reasonable, effective, and / or widely used for a particular disease. The standard of care for a particular disease depends on many different factors, including the biological effectiveness of the treatment, the area or location in the body, the condition of the patient (e.g., age, weight, sex, genetic risks, other disabilities, secondary conditions), toxicity, metabolism, bioaccumulation, therapeutic index, dosage, and other factors known in the art. Determining the standard of care for a disease also depends on establishing safety and efficacy in clinical trials standardized by regulatory agencies, such as the US Food and Drug Administration, the International Council for Harmonization of Technical Requirements for Registration of Pharmaceuticals for Human Use, Health Canada, the European Medicines Agency, the Therapeutics Goods Administration, the Central Drugs Standard Control Organization of India, the National Medical Products Administration of China, the Pharmaceuticals and Medical Devices Agency, the Ministry of Food and Drug Safety, and the World Health Organization. Standard treatments for a disease may include, but are not limited to, surgery, radiation, chemotherapy, targeted therapy, or immunotherapy (e.g., PD1 / PDL1 or CTLA4 blockade). For example, temozolomide is an orally administered chemotherapy compound used as a standard of care treatment for brain cancers, such as glioblastoma and astrocytoma.Those skilled in the art will recognize that the ability of temozolomide to cross the blood-brain barrier is one aspect that determines its usefulness as a standard of care for these diseases, and that temozolomide may not necessarily be used as a standard of care treatment for other diseases.

[0103] As used herein, the term "supplement" refers to a compound, molecule, or substance that provides an effect to patients and is provided in combination with at least one other compound, molecule, or substance for treating cancer.The term "immuno-oncology supplement" refers to a supplement that provides an effect to the patient's immune system.The administration of at least two compounds, molecules, or substances can also be referred to as combination therapy.In some embodiments, at least one other compound, molecule, or substance is PD1 blockade therapy, PDL1 blockade therapy, or CTLA4 blockade therapy.

[0104] As used herein, "PD1 blockade therapy" refers to a PD1 inhibitor treatment that involves blocking the interaction between programmed cell death protein 1 (PD1) and programmed cell death ligand 1 (PDL1). Cancer cells express PDL1, and PDL1 binds to PD1 expressed on T cells or other immune cells to inhibit immune clearance of cancer cells. PD1 inhibitors block this interaction by binding to or inhibiting PD1. PD1 inhibitors include, but are not limited to, pembrolizumab, nivolumab, cemiplimab, spartalizumab, camrelizumab, sintilimab, tislelizumab, toripalimab, AMP-224, or AMP-514, or any combination thereof. As used herein, "PDL1 blockade therapy" refers to a PDL1 inhibitor treatment that behaves similarly to a PD1 inhibitor. PDL1 inhibitors bind to or inhibit PDL1. PDL1 inhibitors include, but are not limited to, atezolizumab, avelumab, durvalumab, KN035, CK-301, AUNP12, CA-170, or BMS-986189, or any combination thereof. "PD1 / PDL1 blockade therapy" refers to PD1 blockade therapy, PDL1 blockade therapy, or both. As used herein, "CTLA4 blockade therapy" refers to CTLA4 inhibitor therapy involving blocking the interaction of cytotoxic T-lymphocyte-associated protein 4 (CTLA4) with CD80 or CD86. T cells express CTLA4, which binds to CD80 or CD86 on other T cells to inhibit their immune activity. CTLA4 inhibitors include, but are not limited to, ipilimumab or tremelimumab. PD1 blockade therapy, PDL1 blockade therapy, and / or CTLA4 blockade therapy are used as standard treatments for some cancers or other diseases.

[0105] As used herein, the term "neurological disorder" refers to a disease that affects the central and / or peripheral nervous system of a patient.Neurological disorders have physical causes, such as external or internal mechanical trauma (for example, stroke or concussion), biological trauma (for example, infection), chemical trauma (for example, toxins or drugs), aging and age-related aging, genetics, and many other causes.Some neurological disorders are caused by the effects or accumulation of mutations or misfolded proteins.These diseases may involve the death of neurons or other cell types associated with the nervous system. Non-limiting examples of neurological disorders include inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopment, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, or brain cancer, or others known to those skilled in the art. Some neurological disorders may also be categorized as proteopathies.

[0106] As used herein, the term "proteopathy" refers to a disease caused by the abnormal folding or accumulation of proteins. Abnormal proteins can acquire toxic functions or lose their normal functions. It is possible that misfolded proteins can induce misfolding of otherwise normally folded proteins, resulting in the amplification of disease (e.g., prion disease). Some non-limiting examples of proteopathies include Alzheimer's disease, cerebral beta-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathy, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinal and bulbar muscular atrophy, spinocerebellar ataxia, Fragile X syndrome, Baratella-Scott syndrome, Friedrich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Palizaeus-Merzbacher disease, and disease), seipinopathy, AA (secondary) amyloidosis, type II diabetes, fibrinogen amyloidosis, dialysis amyloidosis, inclusion body myositis / myopathy, familial amyloid neuropathy, senile systemic amyloidosis, serpinopathy, atrial amyloidosis, pituitary prolactinoma, insulin amyloidosis, corneal lactoferrin amyloidosis, pulmonary alveolar proteinosis, seminal vesicle amyloidosis, cutaneous lichen amyloidosis, Mallory bodies, or odontogenic (Pindborg) tumor amyloid, or any disease caused by protein misfolding or aggregation, or others known to one of skill in the art.

[0107] As used herein, the terms "amyloid-beta," "amyloid-β," and "Aβ" have their plain and ordinary meaning as understood in light of this specification and, unless otherwise indicated, refer to amyloid-β protein or peptide, amyloid-β precursor protein or peptide, intermediates, and modifications and fragments thereof. In particular, "Aβ" refers to any peptide produced by proteolytic processing of the amyloid precursor protein (APP) gene product, particularly peptides associated with amyloid pathology.

[0108] As used herein, the term "blood-brain barrier" has its plain and ordinary meaning as understood in light of the present specification and refers to the protective cellular boundary between the circulatory system and the central nervous system. This boundary is composed of closely interacting brain capillary endothelial cells (BCECs) of capillaries connected through tight junctions, which exhibit selectivity for different small and large molecules in addition to larger particles, such as circulating immune cells and pathogenic organisms. Generally, small polar or hydrophobic molecules can naturally diffuse through the blood-brain barrier, while larger and / or more polar molecules (e.g., glucose, proteins) require specific transporters expressed by endothelial cells to be able to cross the barrier. Some antibodies have been shown to be able to cross the blood-brain barrier by having specificity for cellular receptors or transporters on endothelial cells that internalize and undergo transcytosis. The BBB functions as a physical, metabolic, and immunological barrier. As disclosed herein, in some embodiments, the antibodies or binding fragments thereof disclosed herein may be able to cross the blood-brain barrier of a subject. In some embodiments, the subject may have an intact blood-brain barrier. In some embodiments, the subject may have a damaged or improperly functioning blood-brain barrier. In some embodiments, the damaged or improperly functioning blood-brain barrier is caused by neurodegenerative diseases, including but not limited to Alzheimer's disease, or is associated with brain cancer, such as primary and / or secondary brain tumor-related damage.

[0109] As used herein, the term "neuronal regeneration" has its plain and ordinary meaning as understood in light of the present specification and refers to the new proliferation (growth) of cells or components thereof associated with the nervous system. For example, regeneration can occur with the development of neurons, glia, oligodendrocytes, astrocytes, ependymal cells, microglia, or their components, such as axons, dendrites, myelin, or new synaptic / neuronal interactions. Neuronal tissue generally regenerates much slower than other tissues in adults, although some repair occurs after injury or damage. While there are currently no treatments to enhance neuronal regeneration, research is being conducted toward treatment and prevention, such as the prevention of neurodegeneration in diseases such as Alzheimer's disease and multiple sclerosis. As disclosed herein, in some embodiments, the antibodies or binding fragments thereof disclosed herein may be capable of promoting neuronal regeneration.

[0110] The terms "cancer," "neoplasm," "tumor," and "carcinoma" are used interchangeably herein to refer to cells that exhibit relatively autonomous growth and, as a result, an abnormal growth phenotype characterized by a significant loss of cell proliferation control. Generally, cells of interest for detection or treatment in this application include precancerous (e.g., benign), malignant, premetastatic, metastatic, and nonmetastatic cells. Detection of cancerous cells is of particular interest. The term "normal," when used in the context of "normal cells," is meant to refer to cells of a non-transformed phenotype or cells that exhibit the morphology of non-transformed cells of the tissue type being examined. A "cancerous phenotype" generally refers to any of a variety of biological phenomena characteristic of cancerous cells, which may vary with the type of cancer. A cancerous phenotype is generally identified by abnormalities, such as cell growth or proliferation (e.g., uncontrolled growth or proliferation), cell cycle regulation, cell mobility, cell-cell interactions, or metastasis.

[0111] The term "tumor microenvironment" refers to the cellular environment in which a tumor resides, which includes tumor cells as well as surrounding blood vessels, immune cells, fibroblasts, bone marrow-derived inflammatory cells, lymphocytes, signaling molecules, and the extracellular matrix.

[0112] The term "immune cells" refers to cells of hematopoietic origin that are involved in the specific recognition of antigens. Immune cells include antigen-presenting cells (APCs), such as dendritic cells or macrophages, B cells, T cells, natural killer cells, and myeloid cells, such as monocytes, macrophages, eosinophils, mast cells, basophils, and granulocytes.

[0113] The term "immune response" refers to a T cell-mediated and / or B cell-mediated immune response. Exemplary immune responses include B cell responses (e.g., antibody production), T cell responses (e.g., cytokine production and cytotoxicity), and activation of cytokine-responsive cells, such as macrophages. The term "activating an immune response" refers to enhancing the level of a T cell-mediated and / or B cell-mediated immune response using methods known to those skilled in the art. In one embodiment, the level of enhancement is at least 20-50%, alternatively at least 60%, at least 70%, at least 80%, at least 90%, at least 100%, at least 120%, at least 150%, or at least 200%.

[0114] As used herein, the term "transforming growth factor beta receptor" (TGF-b receptor, or TGF-β receptor) refers to a family of serine / threonine kinase receptors expressed on the cell surface that are specific for the protein transforming growth factor beta (TGF-b, TGF-β). The interaction of TGF-b with the receptor triggers signal transduction pathways responsible for many functions, including, but not limited to, cell proliferation (growth), differentiation (e.g., stem cells, immune cells), apoptosis, homeostasis, chemotaxis, inflammation, and immune cell activation. The TGF-b receptor family includes TGF-b receptor type 1 (TGFbR1), TGF-b receptor type 2 (TGFbR2), and TGF-b receptor type 3 (TGFbR3).

[0115] As used herein, the term "vascular endothelial growth factor receptor" (VEGFR) refers to a family of tyrosine kinase receptors specific for vascular endothelial growth factor (VEGF). The VEGFR family includes VEGFR1, VEGFR2, and VEGFR3.

[0116] As used herein, the term "epidermal growth factor receptor" (EGFR, ErbB1, HER1) refers to a tyrosine kinase receptor specific for epidermal growth factor (EGF) and transforming growth factor alpha (TGFα) that belongs to the ErbB family of tyrosine kinases.

[0117] As used herein, the term "platelet-derived growth factor receptor" (PDGFR) refers to a family of tyrosine kinase receptors specific for platelet-derived growth factor (PDGF). The PDGFR family includes PDGFR alpha (PDGFRa, PDGFRα) and PDGFR beta (PDGFRb, PDGFRβ).

[0118] As used herein, the term "HER2 / neu" (ErbB2, HER2) refers to a tyrosine kinase receptor that belongs to the ErbB family of tyrosine kinases.

[0119] As used herein, the terms "hepatocyte growth factor receptor" and "tyrosine-protein kinase Met" (HGFR, cMet, c-Met) refer to the tyrosine kinase receptor specific for hepatocyte growth factor / scatter factor (HGF / SF).

[0120] As used herein, the term "tumor necrosis factor soluble receptor I" (TNF sRI) refers to the soluble fragment of TNF-α following proteolytic cleavage by TNF-α converting enzyme.

[0121] As used herein, the term "integrin-associated protein" (CD47, IAP) refers to a transmembrane surface signaling protein that belongs to the immunoglobulin superfamily.

[0122] As used herein, the term "fibroblast growth factor receptor" (FGFR) refers to a family of tyrosine kinase receptors specific for fibroblast growth factors (FGFs). The FGFR family includes FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, and FGFR4.

[0123] As used herein, the term "fibrosis" refers to a medical condition in which tissues or organs harden or scar as a result of unregulated production of extracellular matrix, such as collagen proteins. Fibrosis is associated with chronic inflammation, in which immune cells, such as macrophages, signal fibroblasts to express extracellular matrix proteins in response. This signaling is achieved through pathways such as growth receptor pathways, including but not limited to, TGF-b, EGFR, PDGFR, FGFR, VEGFR, or cMet pathways, although other pro-fibrotic pathways also exist. Fibrosis includes, but is not limited to, liver fibrosis, bridging fibrosis, cirrhosis, kidney fibrosis, pulmonary fibrosis, idiopathic pulmonary fibrosis, cystic fibrosis, cardiovascular fibrosis, arterial fibrosis, venous thrombosis, arthrofibrosis, Crohn's disease, Dupuytren's contracture, keloids, mediastinal fibrosis, myelofibrosis, Peyronie's disease, nephrogenic systemic fibrosis, progressive massive fibrosis, retroperitoneal fibrosis, or systemic sclerosis.

[0124] As used herein, the term " non-alcoholic fatty liver disease " (NAFLD) refers to the accumulation of fat in the liver as a result of causes other than alcohol use.The more serious form of NAFLD is " non-alcoholic steatohepatitis " (NASH), which is further defined by liver inflammation and fibrosis.NAFLD and NASH can ultimately lead to cirrhosis, liver cancer, liver failure or cardiovascular disease.

[0125] As used herein, the term "sepsis" refers to a condition characterized by an extreme inflammatory immune response to pathogenic infection.As used herein, the term "atopic dermatitis" (eczema) refers to an autoimmune condition characterized by inflammation of the skin, causing redness, itching, and a rash.As used herein, the term "psoriasis" refers to an autoimmune condition characterized by inflammation of the skin, resulting in red patches on the skin, itching, dryness, and a rash.

[0126] The term "% w / w" or "% wt / wt" means a percentage expressed as the weight of an ingredient or agent relative to the total weight of the composition, multiplied by 100.

[0127] Exemplary Anti-Gal3 Antibodies Unless otherwise specified, the complementarity defining regions disclosed herein are according to the IMGT definition. In some embodiments, the CDRs can alternatively be according to Kabat, Chothia, or other definitions recognized by those of skill in the art.

[0128] It is understood that antibodies having antibody names described herein may be referred to using a shortened version of the antibody name, so long as there is no conflict with another antibody described herein, e.g., 2D10.2B2 may be referred to as 2D10.

[0129] In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to a specific epitope within the Gal3 protein. In some instances, the anti-Gal3 antibody or binding fragment thereof binds to a specific epitope within the Gal3 protein having the amino acid sequence set forth in SEQ ID NO: 1, as provided in Figures 16-1 to 16-9.

[0130] In some cases, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 10, 15, or 20 amino acid residues within the peptide shown in FIG.

[0131] In some embodiments, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 10, 15, or 20 amino acid residues within amino acid residues 1-20 of SEQ ID NO: 1. In some embodiments, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 10, 15, or 20 amino acid residues within amino acid residues 31-50 of SEQ ID NO: 1. In some embodiments, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 10, 15, or 20 amino acid residues within amino acid residues 51-70 of SEQ ID NO: 1. In some embodiments, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 10, 15, or 20 amino acid residues within amino acid residues 61-80 of SEQ ID NO: 1. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0132] In some cases, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid residues within peptide 1 (SEQ ID NO:3), peptide 2 (SEQ ID NO:4), peptide 3 (SEQ ID NO:5), peptide 4 (SEQ ID NO:6), peptide 5 (SEQ ID NO:7), peptide 6 (SEQ ID NO:8), peptide 7 (SEQ ID NO:9), peptide 8 (SEQ ID NO:10), or peptide 17 (SEQ ID NO:19), or any combination thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof may bind to at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or 20 amino acid residues within peptide 6 (SEQ ID NO:8). In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0133] Some exemplary antibodies that bind to peptide 1 (SEQ ID NO: 3) are 23H9.2E4, F846C.1H5, F846TC.14A2, F846TC.7F10, F847C.10B9, F847C.12F12, F847C.26F5, and F847C.4B10.

[0134] Some exemplary antibodies that bind to peptide 2 (SEQ ID NO:4) are 15F10.2D6, 7D8.2D8, F846TC.14E4, F849C.8D10, and F849C.8H3.

[0135] Some exemplary antibodies that bind to peptide 3 (SEQ ID NO:5) are 15F10.2D6, 7D8.2D8, and F849C.8D10.

[0136] Some exemplary antibodies that bind to peptide 4 (SEQ ID NO:6) are 13A12.2E5 and 15F10.2D6.

[0137] Some exemplary antibodies that bind to peptide 5 (SEQ ID NO:7) are F846C.1B2 and F846C.1H12.

[0138] Some exemplary antibodies that bind to peptide 6 (SEQ ID NO: 8) are 13A12.2E5, 14H10.2C9, 23H9.2E4, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H12, F846C.2H3, and F846TC.16B5.

[0139] Some exemplary antibodies that bind to peptide 7 (SEQ ID NO: 9) are 14H10.2C9, 23H9.2E4, F846C.1B2, F846TC.14A2, F847C.10B9, F847C.12F12, and F847C.26F5.

[0140] Some exemplary antibodies that bind to peptide 8 (SEQ ID NO: 10) are 23H9.2E4 and F846TC.14A2.

[0141] Some exemplary antibodies that bind to peptide 17 (SEQ ID NO: 19) are 7D8.2D8, F846C.1F5, F846C.1H12, F846TC.16B5, F847C.11B1, and F849C.8H3.

[0142] In some embodiments, anti-Gal3 antibodies or binding fragments thereof are epitope binned. Epitope bins for some exemplary antibodies are depicted in Figure 33. An exemplary binning process is detailed in Example 3.

[0143] In some embodiments, antibody TB001 is categorized in bin 1.

[0144] In some embodiments, antibodies TB006, 19B5.2E6, 20H5.A3, 23H9.2E4, and 2D10.2B2 are categorized in bin 3.

[0145] In some embodiments, antibody 20D11.2C6 is categorized in bin 5.

[0146] In some embodiments, antibodies 13A12.2E5 and 3B11.2G2 are categorized in bin 7.

[0147] In some embodiments, antibodies 14H10.2C9, 15F10.2D6, 7D8.2D8, F846TC.14E4, F846TC.7F10, and F849C.8D10 are categorized in bin 8.

[0148] In some embodiments, antibody 12G5.D7 is categorized in bin 10.

[0149] In some embodiments, antibody 846.2B11 is categorized in bin 16.

[0150] In some embodiments, antibodies F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, and F846TC.16B5 are categorized in bin 17.

[0151] In some embodiments, antibody 846.4D5 is categorized in bin 24.

[0152] In some embodiments, antibodies F847C.10B9, F847C.12F12, and F847C.26F5 are categorized in bin 49. In some embodiments, any antibody that binds together with any of the bins provided herein is contemplated.

[0153] In some embodiments, the anti-Gal3 antibodies or binding fragments thereof described herein may bind to the N-terminal domain of Gal3 or a portion thereof. In some embodiments, the anti-Gal3 antibodies or binding fragments thereof described herein may bind to an epitope of Gal3 containing a GxYPG motif, where x is the amino acid alanine (A), glycine (G), or valine (V). In some embodiments, the anti-Gal3 antibodies or binding fragments thereof described herein may bind to an epitope of Gal3 containing two GxYPG motifs separated by three amino acids, where x is A, G, or V.

[0154] In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the N-terminus of Gal3, the N-terminal domain of Gal3, or the TRD of Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof does not bind to the N-terminus of Gal3, the N-terminal domain of Gal3, or the TRD of Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the C-terminus of Gal3, the C-terminal domain of Gal3, or the CRD of Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof does not bind to the C-terminus of Gal3, the C-terminal domain of Gal3, or the CRD of Gal3.

[0155] In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a dissociation constant (KD) of less than 1 nM, less than 1.2 nM, less than 2 nM, less than 5 nM, less than 10 nM, less than 13.5 nM, less than 15 nM, less than 20 nM, less than 25 nM, or less than 30 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 1 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 1.2 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 2 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 5 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 10 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 13.5 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 15 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 20 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 25 nM. In some cases, the anti-Gal3 antibody or binding fragment thereof binds to Gal3 with a KD of less than 30 nM. Exemplary Gal3 binding KD values ​​for anti-Gal3 antibodies are provided in Figure 36. In some embodiments, any method disclosed herein involving an anti-Gal3 antibody or binding fragment may be performed using an antigen-binding molecule that binds to Gal3.

[0156] Disclosed herein are anti-Gal3 antibodies or binding fragments thereof having unique sequences. In some embodiments, the anti-Gal3 antibodies or binding fragments thereof have the following sequence: (1) V H -CDR1, V H -CDR2, and V H a heavy chain variable region comprising CDR3, and (2) a V L -CDR1, V L -CDR2, and V L- a light chain variable region comprising CDR3. In some embodiments, V H CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27 to 44, 245 to 246, 397 to 399, and 588 to 615; H CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45 to 60, 247 to 248, 400 to 406, and 616 to 643; H CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61 to 81, 249 to 250, 407 to 416, and 644 to 671; L CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82 to 101, 251 to 252, 417 to 426, and 672 to 699; L CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 427 to 428, and 700 to 727, and V L -CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117-135, 254-255, 429-434, and 728-755. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0157] In some embodiments, an exemplary V H -CDR1 sequences are depicted in Figure 18. In some embodiments, exemplary V H -CDR2 sequences are depicted in Figure 19. In some embodiments, exemplary V H -CDR3 sequences are depicted in Figure 20. In some embodiments, exemplary V L -CDR1 sequences are depicted in Figure 21. In some embodiments, exemplary V L -CDR2 sequences are depicted in Figure 22. In some embodiments, exemplary V L -CDR3 sequences are depicted in Figure 23. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0158] In some embodiments, the heavy chain variable region (V H ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, 435-450, and 756-783. In some embodiments, the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, 435-450, and 756-783. In some embodiments, exemplary V H are depicted in Figures 24-1 to 24-5. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0159] In some embodiments, the light chain variable region (V L ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 451-464, and 784-811. In some embodiments, the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 451-464, and 784-811. In some embodiments, exemplary V L are depicted in Figures 25-1 to 25-5. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0160] In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises 1) V in SEQ ID NO: 136 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 161 L-CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 2) V within SEQ ID NO: 137 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 162 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 3) V within SEQ ID NO: 138 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 163 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 4) V within SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 164 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 5) V within SEQ ID NO: 140 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H-CDR2, V H - V within CDR3 and SEQ ID NO: 165 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 6) V within SEQ ID NO: 141 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 166 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 7) V within SEQ ID NO: 142 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 167 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 8) V within SEQ ID NO: 143 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 168 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 9) V within SEQ ID NO: 144 H -CDR1, V H -CDR2, VH -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 169 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 10) V within SEQ ID NO: 145 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 170 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 11) V within SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 171 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 12) V within SEQ ID NO: 146 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 172 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0161] 13) V in SEQ ID NO: 147 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 173 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 14) V within SEQ ID NO: 148 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 174 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 15) V within SEQ ID NO: 149 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 175 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 16) V within SEQ ID NO: 150 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 176 L -CDR1, V L-CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 17) V within SEQ ID NO: 151 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 177 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 18) V within SEQ ID NO: 152 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 178 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 19) V within SEQ ID NO: 153 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 179 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 20) V within SEQ ID NO: 154 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H- V within CDR3 and SEQ ID NO: 180 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 21) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 181 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 22) V within SEQ ID NO: 156 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 182 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 23) V within SEQ ID NO: 157 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 183 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 24) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 184 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0162] 25) V in sequence number 158 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 185 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 26) V within SEQ ID NO: 159 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 186 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 27) V within SEQ ID NO: 160 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 187 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, VL CDR3; 28) V within SEQ ID NO: 256 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 258 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 29) V within SEQ ID NO: 257 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 259 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 30) V within SEQ ID NO: 435 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 185 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 31) V within SEQ ID NO: 436 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 451 L -CDR1, V L -CDR2, V L-V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 32) V within SEQ ID NO: 437 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 452 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 33) V within SEQ ID NO: 438 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 453 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 34) V within SEQ ID NO: 439 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 162 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 35) V within SEQ ID NO: 440 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 454L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 36) V within SEQ ID NO: 441 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 455 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0163] 37) V in sequence number 442 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 456 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 38) V within SEQ ID NO: 443 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 457 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 39) V within SEQ ID NO: 444 H -CDR1, V H -CDR2, VH -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 458 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 40) V within SEQ ID NO: 445 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 459 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 41) V within SEQ ID NO: 446 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 460 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 42) V within SEQ ID NO: 447 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 461 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V LCDR3; 43) V within SEQ ID NO: 448 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 462 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 44) V within SEQ ID NO: 449 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 463 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 45) V within SEQ ID NO: 450 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 464 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 46) V within SEQ ID NO: 756 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 784 L -CDR1, V L -CDR2, V L -V in CDR3L -CDR1, V L -CDR2, V L CDR3; 47) V within SEQ ID NO: 757 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 785 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 48) V within SEQ ID NO: 758 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 786 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0164] 49) V in sequence number 759 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 787 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 50) V within SEQ ID NO: 760 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, VH - V within CDR3 and SEQ ID NO: 788 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 51) V within SEQ ID NO: 761 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 789 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 52) V within SEQ ID NO: 762 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 790 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 53) V within SEQ ID NO: 763 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 791 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 54) V within SEQ ID NO: 764 H -CDR1, V H -CDR2, V H-V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 792 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 55) V within SEQ ID NO: 765 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 793 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 56) V within SEQ ID NO: 766 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 794 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 57) V within SEQ ID NO: 767 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 795 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 58) V within SEQ ID NO: 768H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 796 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 59) V within SEQ ID NO: 769 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 797 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0165] 60) V in sequence number 770 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 798 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 61) V within SEQ ID NO: 771 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 799 L -CDR1, V L -CDR2, VL -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 62) V within SEQ ID NO: 772 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - CDR3 and V within SEQ ID NO: 800 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 63) V within SEQ ID NO: 773 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 801 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 64) V within SEQ ID NO: 774 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 802 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 65) V within SEQ ID NO: 775 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H- V within CDR3 and SEQ ID NO: 803 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 66) V within SEQ ID NO: 776 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 804 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 67) V within SEQ ID NO: 777 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 805 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 68) V within SEQ ID NO: 778 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 806 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 69) V within SEQ ID NO: 779 H -CDR1, V H -CDR2, V H -V in CDR3H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 807 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 70) V within SEQ ID NO: 780 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 808 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 71) V within SEQ ID NO: 781 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 809 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 72) V within SEQ ID NO: 782 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 810 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; or 73) V within SEQ ID NO: 783H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 811 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -Contains CDR3.

[0166] In some embodiments, exemplary combinations of heavy chain variable region CDRs are depicted in Figure 28. In some embodiments, exemplary combinations of light chain variable region CDRs are depicted in Figure 29. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0167] In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 7) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 8) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 9) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 10) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 17) the heavy chain variable region of SEQ ID NO: 151 and the light chain variable region of SEQ ID NO: 177; 18) the heavy chain variable region of SEQ ID NO: 152 and the light chain variable region of SEQ ID NO: 178; 19) the heavy chain variable region of SEQ ID NO: 153 and the light chain variable region of SEQ ID NO: 179; 20) the heavy chain variable region of SEQ ID NO: 154 and the light chain variable region of SEQ ID NO: 180;

[0168] 21) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) the heavy chain variable region of SEQ ID NO: 156 and the light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) the heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187; 28) the heavy chain variable region of SEQ ID NO: 256 and the light chain variable region of SEQ ID NO: 258; 29) the heavy chain variable region of SEQ ID NO: 257 and the light chain variable region of SEQ ID NO: 259; 30) the heavy chain variable region of SEQ ID NO: 435 and the light chain variable region of SEQ ID NO: 185; 31) the heavy chain variable region of SEQ ID NO: 436 and the light chain variable region of SEQ ID NO: 451; 32) the heavy chain variable region of SEQ ID NO: 437 and the light chain variable region of SEQ ID NO: 452; 33) the heavy chain variable region of SEQ ID NO: 438 and the light chain variable region of SEQ ID NO: 453; 34) the heavy chain variable region of SEQ ID NO: 439 and the light chain variable region of SEQ ID NO: 162; 35) the heavy chain variable region of SEQ ID NO: 440 and the light chain variable region of SEQ ID NO: 454; 36) the heavy chain variable region of SEQ ID NO: 441 and the light chain variable region of SEQ ID NO: 455; 37) the heavy chain variable region of SEQ ID NO: 442 and the light chain variable region of SEQ ID NO: 456; 38) the heavy chain variable region of SEQ ID NO: 443 and the light chain variable region of SEQ ID NO: 457; 39) the heavy chain variable region of SEQ ID NO: 444 and the light chain variable region of SEQ ID NO: 458; 40) the heavy chain variable region of SEQ ID NO: 445 and the light chain variable region of SEQ ID NO: 459;

[0169] 41) the heavy chain variable region of SEQ ID NO: 446 and the light chain variable region of SEQ ID NO: 460; 42) the heavy chain variable region of SEQ ID NO: 447 and the light chain variable region of SEQ ID NO: 461; 43) the heavy chain variable region of SEQ ID NO: 448 and the light chain variable region of SEQ ID NO: 462; 44) the heavy chain variable region of SEQ ID NO: 449 and the light chain variable region of SEQ ID NO: 463; 45) the heavy chain variable region of SEQ ID NO: 450 and the light chain variable region of SEQ ID NO: 464; 46) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 47) the heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 48) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 49) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 50) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 51) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 52) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 53) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 54) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 55) the heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 56) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 57) the heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 58) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 59) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 60) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798;

[0170] 61) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 62) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 63) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 64) the heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 65) the heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 66) the heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 67) the heavy chain variable region of SEQ ID NO: 777 and 68) the light chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 69) the heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 70) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 71) the heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 72) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 73) the heavy chain variable region of SEQ ID NO: 783 and the light chain variable region of SEQ ID NO: 811.

[0171] In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0172] In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a heavy chain (HC) sequence of any one of SEQ ID NOs: 188-216, 465-482. In some embodiments, exemplary HC sequences are depicted in Figures 26-1 to 26-8. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0173] In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a light chain (LC) sequence of any one of SEQ ID NOs: 217-243, 483-499. In some embodiments, exemplary LC sequences are depicted in Figures 27-1 to 27-4. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0174] In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001 (IMT001), TB006 (4A11.H3L1), 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F 846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12 F12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 847.14H4, 846T.1H2, mIMT001, 4A11.2B 5, 4A11.H1L1, 4A11.H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15G7.2A7, 19D9.2E5, 23B10 .2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 846T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9 , 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof. In some embodiments, the heavy and light chain CDRs associated with each of the above antibodies are depicted in Figure 30. In some embodiments, the V associated with each of the above antibodies is selected from the group consisting of: H and V Lare depicted in Figure 31. In some embodiments, the HC and LC associated with each of the above antibodies are depicted in Figure 32. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0175] Disclosed herein are anti-Gal3 antibodies or binding fragments thereof. In some embodiments, the anti-Gal3 antibodies or binding fragments thereof comprise: (1) V H -CDR1, V H -CDR2, and V H a heavy chain variable region comprising CDR3, and (2) a V L -CDR1, V L -CDR2, and V L - a light chain variable region comprising CDR3. In some embodiments, V H CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 36 to 44, 588 to 615, H CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 54 to 60, 616 to 643, H CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 70 to 81, 644 to 671, L CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 92 to 101, 672 to 699, L CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 111 to 116, 700 to 727, and V L - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 127-135, 728-755. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0176] In some embodiments, an exemplary V H -CDR1 sequences are depicted in Figure 18. In some embodiments, exemplary V H-CDR2 sequences are depicted in Figure 19. In some embodiments, exemplary V H -CDR3 sequences are depicted in Figure 20. In some embodiments, exemplary V L -CDR1 sequences are depicted in Figure 21. In some embodiments, exemplary V L -CDR2 sequences are depicted in Figure 22. In some embodiments, exemplary V L -CDR3 sequences are depicted in Figure 23. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0177] In some embodiments, the heavy chain variable region (V H ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 147-160, 756-783. In some embodiments, the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 147-160, 756-783. In some embodiments, exemplary V H are depicted in Figures 24-1 to 24-5. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0178] In some embodiments, the light chain variable region (V L ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 173-187, 784-811. In some embodiments, the light chain variable region is selected from the group consisting of SEQ ID NOs: 173-187, 784-811. In some embodiments, exemplary V Lare depicted in Figures 25-1 to 25-5. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0179] In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises 1) V in SEQ ID NO: 147 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 173 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 2) V within SEQ ID NO: 148 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 174 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 3) V within SEQ ID NO: 149 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 175 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 4) V within SEQ ID NO: 150 H-CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 176 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 5) V within SEQ ID NO: 151 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 177 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 6) V within SEQ ID NO: 152 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 178 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 7) V within SEQ ID NO: 153 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 179 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L-CDR2, V L CDR3; 8) V within SEQ ID NO: 154 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 180 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 9) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 181 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 10) V within SEQ ID NO: 156 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 182 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0180] 11) V in SEQ ID NO: 157 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 183L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 12) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 184 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 13) V within SEQ ID NO: 158 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 185 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 14) V within SEQ ID NO: 159 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 186 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 15) V within SEQ ID NO: 160 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, VH -CDR2, V H - V within CDR3 and SEQ ID NO: 187 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 16) V within SEQ ID NO: 756 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 784 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 17) V within SEQ ID NO: 757 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 785 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 18) V within SEQ ID NO: 758 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 786 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 19) V within SEQ ID NO: 759 H -CDR1, V H-CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 787 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 20) V within SEQ ID NO: 760 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 788 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0181] 21) V in sequence number 761 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 789 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 22) V within SEQ ID NO: 762 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 790 L -CDR1, V L -CDR2, V L -V in CDR3 L-CDR1, V L -CDR2, V L CDR3; 23) V within SEQ ID NO: 763 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 791 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 24) V within SEQ ID NO: 764 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 792 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 25) V within SEQ ID NO: 765 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 793 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 26) V within SEQ ID NO: 766 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 794 L -CDR1, VL -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 27) V within SEQ ID NO: 767 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 795 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 28) V within SEQ ID NO: 768 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 796 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 29) V within SEQ ID NO: 769 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 797 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 30) V within SEQ ID NO: 770 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, VH - V within CDR3 and SEQ ID NO: 798 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0182] 31) V in sequence number 771 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 799 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 32) V within SEQ ID NO: 772 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - CDR3 and V within SEQ ID NO: 800 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 33) V within SEQ ID NO: 773 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 801 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 34) V within SEQ ID NO: 774 H-CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 802 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 35) V within SEQ ID NO: 775 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 803 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 36) V within SEQ ID NO: 776 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 804 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 37) V within SEQ ID NO: 777 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 805 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L-CDR2, V L CDR3; 38) V within SEQ ID NO: 778 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 806 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 39) V within SEQ ID NO: 779 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 807 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 40) V within SEQ ID NO: 780 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 808 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0183] 41) V in sequence number 781 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 809L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 42) V within SEQ ID NO: 782 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 810 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; or 43) V within SEQ ID NO: 783 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 811 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3. In some embodiments, exemplary combinations of heavy chain variable region CDRs are depicted in Figure 28. In some embodiments, exemplary combinations of light chain variable region CDRs are depicted in Figure 29. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0184] In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: 1) a heavy chain variable region of SEQ ID NO: 147 and a light chain variable region of SEQ ID NO: 173; 2) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 3) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 4) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 5) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 6) a heavy chain variable region of SEQ ID NO: 152 and a light chain variable region of SEQ ID NO: 178; 7) a heavy chain variable region of SEQ ID NO: 153 and a light chain variable region of SEQ ID NO: 179; 8) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180; 9) a heavy chain variable region of SEQ ID NO: 155 and a light chain variable region of SEQ ID NO: 181; 10) a heavy chain variable region of SEQ ID NO: 156 and a light chain variable region of SEQ ID NO: 182; 11) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 12) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 13) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 14) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 15) the heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187; 16) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 17) the heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 18) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 19) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 20) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788;

[0185] 21) a heavy chain variable region of SEQ ID NO: 761 and a light chain variable region of SEQ ID NO: 789; 22) a heavy chain variable region of SEQ ID NO: 762 and a light chain variable region of SEQ ID NO: 790; 23) a heavy chain variable region of SEQ ID NO: 763 and a light chain variable region of SEQ ID NO: 791; 24) a heavy chain variable region of SEQ ID NO: 764 and a light chain variable region of SEQ ID NO: 792; 25) a heavy chain variable region of SEQ ID NO: 765 and a light chain variable region of SEQ ID NO: 793; 26) a heavy chain variable region of SEQ ID NO: 766 and a light chain variable region of SEQ ID NO: 794 27) the heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 28) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 29) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 30) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 31) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 32) the heavy chain variable region of SEQ ID NO: 772 and 33) a heavy chain variable region of SEQ ID NO: 773 and a light chain variable region of SEQ ID NO: 801; 34) a heavy chain variable region of SEQ ID NO: 774 and a light chain variable region of SEQ ID NO: 802; 35) a heavy chain variable region of SEQ ID NO: 775 and a light chain variable region of SEQ ID NO: 803; 36) a heavy chain variable region of SEQ ID NO: 776 and a light chain variable region of SEQ ID NO: 804; 37) a heavy chain variable region of SEQ ID NO: 777 and a light chain variable region of SEQ ID NO: 805; 38) a heavy chain variable region of SEQ ID NO: 778 3) the heavy chain variable region and the light chain variable region of SEQ ID NO: 806; 39) the heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 40) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 41) the heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 42) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 43) the heavy chain variable region of SEQ ID NO: 783 and the light chain variable region of SEQ ID NO: 811. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0186] In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a heavy chain (HC) sequence of any one of SEQ ID NOs: 201-216. In some embodiments, exemplary HC sequences are depicted in Figures 26-1 to 26-8. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0187] In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a light chain (LC) sequence of any one of SEQ ID NOs: 229-243. In some embodiments, exemplary LC sequences are depicted in Figures 27-1 to 27-4. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0188] In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from at least one of the group consisting of F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4, F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, or a binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846.2D4, 846.2F11, 846T.10B1, 846 and / or F847C.21H6, or a binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody selected from 846.4D5, 15F10.2D6, F846C.1B2, and F846C.1H12. In some embodiments, the heavy and light chain CDRs associated with each of the above antibodies are depicted in Figure 30. In some embodiments, the V associated with each of the above antibodies H and V Lare depicted in Figure 31. In some embodiments, the HC and LC associated with each of the above antibodies are depicted in Figure 32. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0189] In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3 to 26. In some embodiments, any anti-Gal3 antibody or binding fragment thereof, or any configuration of any anti-Gal3 antibody or binding fragment provided herein, may be replaced with an antigen-binding molecule that binds to Gal3.

[0190] In some embodiments, the anti-Gal3 antibody or binding fragment thereof belongs to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with an antibody belonging to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with an antibody belonging to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof competes with an antibody belonging to bin 3, 8, 17, or 24 for binding to Gal3.

[0191] In some cases, the anti-Gal3 antibody or binding fragment thereof comprises a humanized antibody or binding fragment thereof. In other cases, the anti-Gal3 antibody or binding fragment thereof comprises a chimeric antibody or binding fragment thereof. In some cases, the anti-Gal3 antibody comprises a full-length antibody or binding fragment thereof. In some cases, the anti-Gal3 antibody or binding fragment thereof comprises a bispecific antibody or binding fragment thereof. In some cases, the anti-Gal3 antibody or binding fragment thereof comprises a monovalent Fab', a bivalent Fab2, a single-chain variable fragment (scFv), a diabody, a minibody, a nanobody, a single-domain antibody (sdAb), or a camelid antibody or binding fragment thereof.

[0192] In some embodiments, methods of using any one of the anti-Gal3 antibodies, binding fragments thereof, or antigen-binding molecules disclosed herein for treating a disease or disorder in a subject are disclosed. In some embodiments, the methods include administering any one of the anti-Gal3 antibodies, binding fragments thereof, or antigen-binding molecules disclosed herein to a subject having, suspected of having, or at risk of developing a disease or disorder described herein.

[0193] In some embodiments, any of the embodiments and / or any anti-Gal3 antibody or binding fragment thereof disclosed herein may be used for any of the applications, methods, and uses provided herein.

[0194] Some embodiments provided herein relate to an anti-Gal3 antibody or binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3.

[0195] Some embodiments provided herein relate to anti-Gal3 antibodies or binding fragments thereof that disrupt the interaction of Gal3 with proteins associated with proteopathies or neurological diseases. In some embodiments, there are methods and uses of the anti-Gal3 antibodies and binding fragments thereof disclosed herein for the treatment of proteopathies and / or neurological diseases.

[0196] Some embodiments provided herein relate to an anti-Gal3 antibody or binding fragment thereof that can cross the blood-brain barrier. In some embodiments, the blood-brain barrier is that of a subject with a neurological disease. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is a multispecific antibody that increases the permeability of another antibody across the blood-brain barrier. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is conjugated to a payload that increases the permeability of the payload across the blood-brain barrier.

[0197] Some embodiments provided herein relate to anti-Gal3 antibodies or binding fragments thereof that disrupt the interaction of Gal3 with cell surface markers or tumor cell surface markers. In some embodiments, there are methods and uses of the anti-Gal3 antibodies and binding fragments thereof disclosed herein for treating diseases associated with cell surface markers or tumor cell surface markers. In some embodiments, the disease is cancer, fibrosis, or an immune-related disorder.

[0198] Also disclosed herein are proteins comprising one or more peptide sequences having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 18-27. In some embodiments, the protein is an antibody or binding fragment thereof. In some embodiments, the protein comprises: a) a V nucleotide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 18; H a) a CDR1 peptide sequence; b) a V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 19; H -CDR2 peptide sequence; c) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 20. H-CDR3 peptide sequence; d) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 21. L -CDR1 peptide sequence; e) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 22. L -CDR2 peptide sequence; f) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 23. L -CDR3 peptide sequence; g) a heavy chain variable region peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 24-1 to 24-5; h) a light chain variable region peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 25-1 to 25-5; i) a light chain variable region peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 26-1 to 26-8. j) a heavy chain peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences in Figures 27-1 through 27-4; or any combination thereof, including one of the provided sequences or a combination of 1, 2, 3, 4, 5, 6, 7, 8, 9, or 10 of the provided sequences. In some embodiments, the protein comprises a peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to a peptide sequence encoded by any one or more of the nucleic acid sequences in Figures 37-1 through 40-12. In some embodiments, the protein is an antibody or binding fragment thereof that binds to Gal3.

[0199] How to use In some embodiments, any of the constructs provided herein may be used for neurological disorders and / or proteopathies.

[0200] Disclosed herein are methods for treating a neurological disorder in a subject in need thereof. The method comprises administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the neurological disorder. In some embodiments, the method further comprises selecting the subject as having or at risk of suffering from a neurological disorder prior to the administering step. In some embodiments, the method further comprises detecting an alleviation of symptoms associated with the neurological disorder after the administering step. In some embodiments, the neurological disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastasis, or brain cancer, or any combination thereof. In some embodiments, the neurological disorder is Alzheimer's disease, and the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to amyloid precursor protein (APP) or amyloid beta (Aβ), or both. In some embodiments, the APP comprises the sequence of APP695 (SEQ ID NO: 2). In some embodiments, the Aβ comprises Aβ monomers, Aβ oligomers, Aβ fibrils, or any combination thereof. In some embodiments, the Aβ comprises the sequence of Aβ42 (SEQ ID NO: 244).

[0201] In some embodiments, the anti-Gal3 antibody or binding fragment thereof reduces binding of Gal3 to APP or Aβ, or both, by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof promotes the phagocytic function of microglia in a subject. In some embodiments, the anti-Gal3 antibody or binding fragment thereof inhibits Aβ-mediated activation of microglia in a subject. In some embodiments, Aβ-mediated activation of microglia is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof inhibits Aβ fibril or oligomer formation in a subject. In some embodiments, Aβ fibril or oligomer formation is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof promotes neuronal regeneration in a subject. In some embodiments, the anti-Gal3 antibody or binding fragment thereof disrupts the binding of Gal3 to Toll-like receptor 4 (TLR4) or triggering receptor expressed on myeloid cells 2 (TREM2), or both. In some embodiments, the binding of Gal3 to TLR4 or TREM2, or both, is disrupted by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages.In some embodiments, more than one anti-Gal3 antibody or its binding fragment is administered to a subject. In some embodiments, the anti-Gal3 antibody or its binding fragment is administered together with one or more additional therapeutic compositions. In some embodiments, the one or more additional therapeutic compositions comprise a cholinesterase inhibitor, an NMDA receptor antagonist, or both. In some embodiments, the cholinesterase inhibitor comprises tacrine, rivastigmine, galantamine, donepezil, or any combination thereof. In some embodiments, the NMDA receptor antagonist comprises memantine.

[0202] Also disclosed herein are methods for disrupting the binding of Gal3 to APP or Aβ, or both. In some embodiments, the method includes contacting APP or Aβ, or both, with an anti-Gal3 antibody or binding fragment thereof, thereby disrupting the binding of Gal3 to APP. In some embodiments, APP or Aβ, or both, are soluble or part of a first cell. In some embodiments, Gal3 is soluble or part of a second cell. In some embodiments, APP comprises the sequence of APP695 (SEQ ID NO: 2). In some embodiments, Aβ comprises Aβ monomers, Aβ oligomers, Aβ fibrils, or any combination thereof. In some embodiments, Aβ comprises the sequence of Aβ42 (SEQ ID NO: 244). In some embodiments, the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the above percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 85%. In some embodiments, the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 90%. In some embodiments, the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 95%. In some embodiments, the APP is contacted with more than one anti-Gal3 antibody or binding fragment thereof. In some embodiments, the Aβ is an Aβ peptide or an Aβ aggregate, or both. In some embodiments, the Aβ aggregate is an Aβ fibril or an Aβ oligomer, or both.

[0203] Also disclosed herein are methods for treating a proteopathy in a subject in need thereof. In some embodiments, the method comprises administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the proteopathy in the subject. In some embodiments, the method further comprises selecting the subject as having or at risk of developing a proteopathy prior to the administering step. In some embodiments, the method further comprises detecting remission of symptoms associated with the proteopathy after the administering step. In some embodiments, treating the proteopathy comprises treating active proteopathy in the subject, or prophylactic treatment, or both. In some embodiments, the proteopathy is selected from the group consisting of Alzheimer's disease, cerebral beta-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathies, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinobulbar muscular atrophy, spinocerebellar ataxia, fragile X syndrome, Baratella-Scott syndrome, Friedreich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Pelizaeus-Merzbacher disease, seipinopathy, AA (bipolar dementia), and AA (bipolar dementia). The present invention relates to amyloidosis, including secondary amyloidosis, type II diabetes, fibrinogen amyloidosis, dialysis amyloidosis, inclusion body myositis / myopathy, familial amyloid neuropathy, senile systemic amyloidosis, serpinopathy, atrial amyloidosis, pituitary prolactinoma, insulin amyloidosis, corneal lactoferrin amyloidosis, pulmonary alveolar proteinosis, seminal vesicle amyloidosis, cutaneous lichen amyloidosis, Mallory bodies, or odontogenic (Pindborg) tumor amyloid, or any disease caused by protein misfolding or aggregation, or any combination thereof. In some embodiments, more than one anti-Gal3 antibody or binding fragment thereof is administered to a subject. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is administered with one or more additional therapeutic compositions.In some embodiments, one or more additional therapeutic compositions comprise a cholinesterase inhibitor, an NMDA receptor antagonist, insulin, or any combination thereof.In some embodiments, the cholinesterase inhibitor comprises tacrine, rivastigmine, galantamine, donepezil, or any combination thereof.In some embodiments, the NMDA receptor antagonist comprises memantine.

[0204] Also disclosed herein are methods of administering an antibody to a subject. In some embodiments, the method comprises administering an anti-Gal3 antibody or binding fragment thereof to a subject. In some embodiments, the method further comprises selecting the subject as having or at risk for a neurological disease or proteopathy prior to the administering step. In some embodiments, the neurological disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof. In some embodiments, the neurological disorder is Alzheimer's disease. In some embodiments, the proteopathy is Alzheimer's disease, cerebral beta-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathy, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinobulbar muscular atrophy, spinocerebellar ataxia, Fragile X syndrome, Baratella-Scott syndrome, Friedreich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Pelizaeus-Merzbacher disease, seipinopathy, AA (Niigata syndrome), or amyloidosis. and / or any disease caused by protein misfolding or aggregation, or any combination thereof.In some embodiments, more than one anti-Gal3 antibody or binding fragment thereof is administered to a subject.

[0205] Also disclosed herein is a method for treating brain cancer in a subject in need thereof.In some embodiments, the method comprises administering an effective amount of anti-Gal3 antibody or its binding fragment to the subject, thereby treating brain cancer in the subject.In some embodiments, the anti-Gal3 antibody or its binding fragment has the ability to cross the blood-brain barrier.In some embodiments, the administration of anti-Gal3 antibody or its binding fragment induces apoptosis in brain cancer.

[0206] Also disclosed herein is a method for promoting neuronal regeneration in a subject in need thereof.In some embodiments, the method comprises administering to the subject an effective amount of an anti-Gal3 antibody or its binding fragment, thereby promoting neuronal regeneration in the subject.In some embodiments, the method further comprises selecting the subject as having neuronal degeneration or at risk of having neuronal degeneration before the administering step.In some embodiments, the method further comprises detecting neuronal regeneration in the subject after the administering step. In some embodiments, the subject comprises a neuronal degeneration associated with inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastasis, brain cancer, or any combination thereof. In some embodiments, the neuronal degeneration is associated with Alzheimer's disease, and the anti-Gal3 antibody or binding fragment thereof interferes with binding of Gal3 to amyloid precursor protein (APP) or amyloid beta (Aβ), or both. In some embodiments, more than one anti-Gal3 antibody or binding fragment thereof is administered to a subject.

[0207] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is administered enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof.

[0208] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3-26. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof belongs to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with antibodies belonging to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with antibodies belonging to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof competes with antibodies belonging to bin 3, 8, 17, or 24 for binding to Gal3.

[0209] When applied to any of the methods or uses disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof may be selected from any one or more of the sequences provided throughout this disclosure (e.g., V H -CDR1, V H -CDR2, V H -CDR3, V L -CDR1, V L -CDR2, V L-CDR3, heavy chain variable region, light chain variable region, heavy chain, or light chain sequence). In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises any one or more sequences shown in Figures 18-32, including any one or more CDRs, heavy chain variable region, light chain variable region, heavy chain, light chain, CDR combination, variable region combination, or heavy and light chain combination described therein. In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to a peptide sequence encoded by any one or more of the nucleic acid sequences shown in Figures 37-1 through 40-12, including any nucleic acid sequence encoding a heavy chain variable region, light chain variable region, heavy chain, or light chain.

[0210] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is H -CDR1, V H -CDR2, and V H a heavy chain variable region comprising CDR3, and (2) a V L -CDR1, V L -CDR2, and V L - a light chain variable region comprising CDR3. In some embodiments, V H CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27 to 44, 245 to 246, and 588 to 615, H CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45 to 60, 247 to 248, and 616 to 643; H - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61 to 81, 249 to 250, and 644 to 671; L CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82 to 101, 251 to 252, and 672 to 699; L CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and V L- CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117-135, 254-255, and 728-755. In some embodiments, any method disclosed herein involving an anti-Gal3 antibody or binding fragment can be performed using an antigen-binding molecule that binds to Gal3.

[0211] As applied to any of the methods disclosed herein, in some embodiments, exemplary V H -CDR1 sequences are depicted in Figure 18. In some embodiments, exemplary V H -CDR2 sequences are depicted in Figure 19. In some embodiments, exemplary V H -CDR3 sequences are depicted in Figure 20. In some embodiments, exemplary V L -CDR1 sequences are depicted in Figure 21. In some embodiments, exemplary V L -CDR2 sequences are depicted in Figure 22. In some embodiments, exemplary V L -CDR3 sequences are depicted in Figure 23. In some embodiments, any of the methods disclosed herein involving anti-Gal3 antibodies or binding fragments can be performed using antigen-binding molecules that bind to Gal3.

[0212] As applied to any of the methods disclosed herein, in some embodiments, the heavy chain variable region (V H ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, and 756-783. In some embodiments, the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, and 756-783. In some embodiments, exemplary V H are depicted in Figures 24-1 to 24-5. In some embodiments, any of the methods disclosed herein involving anti-Gal3 antibodies or binding fragments can be performed using antigen-binding molecules that bind to Gal3.

[0213] When applied to any of the methods disclosed herein, in some embodiments, the light chain variable region (V L ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 784-811. In some embodiments, the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 784-811. In some embodiments, exemplary V L are depicted in Figures 25-1 to 25-5. In some embodiments, any of the methods disclosed herein involving anti-Gal3 antibodies or binding fragments can be performed using antigen-binding molecules that bind to Gal3.

[0214] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of 1) V in SEQ ID NO: 136 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 161 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 2) V within SEQ ID NO: 137 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 162 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 3) V within SEQ ID NO: 138 H -CDR1, V H-CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 163 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 4) V within SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 164 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 5) V within SEQ ID NO: 140 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 165 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 6) V within SEQ ID NO: 141 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 166 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V LCDR3; 7) V within SEQ ID NO: 142 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 167 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 8) V within SEQ ID NO: 143 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 168 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 9) V within SEQ ID NO: 144 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 169 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 10) V within SEQ ID NO: 145 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 170 L -CDR1, V L -CDR2, V L -V in CDR3L -CDR1, V L -CDR2, V L -CDR3;

[0215] 11) V in SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 171 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 12) V within SEQ ID NO: 146 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 172 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 13) V within SEQ ID NO: 147 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 173 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 14) V within SEQ ID NO: 148 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, VH - V within CDR3 and SEQ ID NO: 174 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 15) V within SEQ ID NO: 149 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 175 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 16) V within SEQ ID NO: 150 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 176 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 17) V within SEQ ID NO: 151 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 177 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 18) V within SEQ ID NO: 152 H -CDR1, V H -CDR2, V H-V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 178 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 19) V within SEQ ID NO: 153 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 179 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 20) V within SEQ ID NO: 154 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 180 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0216] 21) V in sequence number 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 181 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L-CDR2, V L CDR3; 22) V within SEQ ID NO: 156 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 182 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 23) V within SEQ ID NO: 157 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 183 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 24) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 184 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 25) V within SEQ ID NO: 158 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 185 L -CDR1, V L -CDR2, VL -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 26) V within SEQ ID NO: 159 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 186 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 27) V within SEQ ID NO: 160 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 187 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 28) V within SEQ ID NO: 256 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 258 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 29) V within SEQ ID NO: 257 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H- V within CDR3 and SEQ ID NO: 259 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 30) V within SEQ ID NO: 756 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 784 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0217] 31) V in sequence number 757 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 785 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 32) V within SEQ ID NO: 758 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 786 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 33) V within SEQ ID NO: 759 H -CDR1, VH -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 787 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 34) V within SEQ ID NO: 760 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 788 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 35) V within SEQ ID NO: 761 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 789 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 36) V within SEQ ID NO: 762 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 790 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, VL CDR3; 37) V within SEQ ID NO: 763 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 791 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 38) V within SEQ ID NO: 764 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 792 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 39) V within SEQ ID NO: 765 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 793 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 40) V within SEQ ID NO: 766 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 794 L -CDR1, V L -CDR2, V L-V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0218] 41) V in sequence number 767 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 795 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 42) V within SEQ ID NO: 768 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 796 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 43) V within SEQ ID NO: 769 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 797 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 44) V within SEQ ID NO: 770 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H-CDR2, V H - V within CDR3 and SEQ ID NO: 798 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 45) V within SEQ ID NO: 771 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 799 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 46) V within SEQ ID NO: 772 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - CDR3 and V within SEQ ID NO: 800 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 47) V within SEQ ID NO: 773 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 801 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 48) V within SEQ ID NO: 774 H -CDR1, V H -CDR2, VH -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 802 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 49) V within SEQ ID NO: 775 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 803 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 50) V within SEQ ID NO: 776 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 804 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0219] 51) V in sequence number 777 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 805 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, VL -CDR2, V L CDR3; 52) V within SEQ ID NO: 778 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 806 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 53) V within SEQ ID NO: 779 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 807 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 54) V within SEQ ID NO: 780 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 808 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 55) V within SEQ ID NO: 781 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 809 L -CDR1, V L-CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 56) V within SEQ ID NO: 782 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 810 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; or 57) V within SEQ ID NO: 783 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 811 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3. In some embodiments, exemplary combinations of heavy chain variable region CDRs are depicted in Figure 28. In some embodiments, exemplary combinations of light chain variable region CDRs are depicted in Figure 29. In some embodiments, any of the methods disclosed herein involving anti-Gal3 antibodies or binding fragments may be performed using an antigen-binding molecule that binds to Gal3.

[0220] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises: 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 166; 7) the heavy chain variable region of SEQ ID NO: 142 and the light chain variable region of SEQ ID NO: 167; 8) the heavy chain variable region of SEQ ID NO: 143 and the light chain variable region of SEQ ID NO: 168; 9) the heavy chain variable region of SEQ ID NO: 144 and the light chain variable region of SEQ ID NO: 169; 10) the heavy chain variable region of SEQ ID NO: 145 and the light chain variable region of SEQ ID NO: 170; 11) the heavy chain variable region of SEQ ID NO: 139 and the light chain variable region of SEQ ID NO: 171; 12) the heavy chain variable region of SEQ ID NO: 146 and the light chain variable region of SEQ ID NO: 172; 13) the heavy chain variable region of SEQ ID NO: 147 and the light chain variable region of SEQ ID NO: 173 14) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 15) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 16) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 17) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 18) a heavy chain variable region of SEQ ID NO: 152 and a light chain variable region of SEQ ID NO: 178; 19) a heavy chain variable region of SEQ ID NO: 153 and a light chain variable region of SEQ ID NO: 179; 20) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180 21) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) the heavy chain variable region of SEQ ID NO: 156 and the light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) the heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187;28) a heavy chain variable region of SEQ ID NO: 256 and a light chain variable region of SEQ ID NO: 258; 29) a heavy chain variable region of SEQ ID NO: 257 and a light chain variable region of SEQ ID NO: 259; 30) a heavy chain variable region of SEQ ID NO: 756 and a light chain variable region of SEQ ID NO: 784;

[0221] 31) a heavy chain variable region of SEQ ID NO: 757 and a light chain variable region of SEQ ID NO: 785; 32) a heavy chain variable region of SEQ ID NO: 758 and a light chain variable region of SEQ ID NO: 786; 33) a heavy chain variable region of SEQ ID NO: 759 and a light chain variable region of SEQ ID NO: 787; 34) a heavy chain variable region of SEQ ID NO: 760 and a light chain variable region of SEQ ID NO: 788; 35) a heavy chain variable region of SEQ ID NO: 761 and a light chain variable region of SEQ ID NO: 789; 36) a heavy chain variable region of SEQ ID NO: 762 and a light chain variable region of SEQ ID NO: 790; 37) a heavy chain variable region of SEQ ID NO: 763 and a light chain variable region of SEQ ID NO: 791 38) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) the heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) the heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and 45) heavy chain variable region of SEQ ID NO: 771 and light chain variable region of SEQ ID NO: 799; 46) heavy chain variable region of SEQ ID NO: 772 and light chain variable region of SEQ ID NO: 800; 47) heavy chain variable region of SEQ ID NO: 773 and light chain variable region of SEQ ID NO: 801; 48) heavy chain variable region of SEQ ID NO: 774 and light chain variable region of SEQ ID NO: 802; 49) heavy chain variable region of SEQ ID NO: 775 and light chain variable region of SEQ ID NO: 803; 50) heavy chain variable region of SEQ ID NO: 776 and light chain variable region of SEQ ID NO: 804; 51) heavy chain of SEQ ID NO: 777 52) a heavy chain variable region of SEQ ID NO: 778 and a light chain variable region of SEQ ID NO: 806; 53) a heavy chain variable region of SEQ ID NO: 779 and a light chain variable region of SEQ ID NO: 807; 54) a heavy chain variable region of SEQ ID NO: 780 and a light chain variable region of SEQ ID NO: 808; 55) a heavy chain variable region of SEQ ID NO: 781 and a light chain variable region of SEQ ID NO: 809; 56) a heavy chain variable region of SEQ ID NO: 782 and a light chain variable region of SEQ ID NO: 810; or 57) a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO: 811.In some embodiments, any of the methods disclosed herein involving anti-Gal3 antibodies or binding fragments can be performed using an antigen-binding molecule that binds to Gal3.

[0222] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a heavy chain (HC) sequence of any one of SEQ ID NOs: 188-216. In some embodiments, exemplary HC sequences are depicted in Figures 26-1 through 26-8. In some embodiments, any of the methods disclosed herein involving an anti-Gal3 antibody or binding fragment may be performed using an antigen-binding molecule that binds to Gal3.

[0223] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a light chain (LC) sequence of any one of SEQ ID NOs: 217-243. In some embodiments, exemplary LC sequences are depicted in Figures 27-1 to 27-4. In some embodiments, any of the methods disclosed herein involving an anti-Gal3 antibody or binding fragment may be performed using an antigen-binding molecule that binds to Gal3.

[0224] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F 12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 847.14H4, 846T.1H2, mIMT001, 4A11.2B5, 4 A11.H1L1, 4A11.H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15G7.2A7, 19D9.2E5, 23B10.2B12 , 24D12.2H9, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 846T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9, 847.11 and at least one of 847.15D6, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

[0225] When applied to any of the methods disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.1 4E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4 B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 8 46T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4 , F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or at least one binding fragment thereof.In some embodiments, the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody selected from 846.4D5, 15F10.2D6, F846C.1B2, and F846C.1H12. In some embodiments, the heavy and light chain CDRs associated with each of the above antibodies are depicted in Figure 30. In some embodiments, the V associated with each of the above antibodies. H and V L are depicted in Figure 31. In some embodiments, the HC and LC associated with each of the above antibodies are depicted in Figure 32. In some embodiments, any of the methods disclosed herein involving anti-Gal3 antibodies or binding fragments can be performed using an antigen-binding molecule that binds to Gal3.

[0226] Also disclosed herein are anti-Gal3 antibodies or binding fragments thereof for use in treating neurodegenerative disorders in subjects in need thereof. In some embodiments, the neurodegenerative disorders include inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastasis, brain cancer, or any combination thereof. In some embodiments, the neurological disorder is Alzheimer's disease, and the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to amyloid precursor protein (APP) or Aβ, or both. In some embodiments, the APP comprises the sequence of APP695 (SEQ ID NO: 2). In some embodiments, the Aβ comprises Aβ monomers, Aβ oligomers, Aβ fibrils, or any combination thereof. In some embodiments, the Aβ comprises the sequence of Aβ42 (SEQ ID NO: 244). In some embodiments, the anti-Gal3 antibody or binding fragment thereof reduces binding of Gal3 to APP or Aβ, or both, by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof promotes the phagocytic function of microglia in a subject. In some embodiments, the anti-Gal3 antibody or binding fragment thereof inhibits Aβ-mediated activation of microglia in a subject. In some embodiments, Aβ-mediated activation of microglia is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages.In some embodiments, the anti-Gal3 antibody or binding fragment thereof inhibits Aβ fibril or oligomer formation in a subject. In some embodiments, Aβ fibril or oligomer formation is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with Toll-like receptor 4 (TLR4) or triggering receptor expressed on myeloid cells 2 (TREM2), or both. In some embodiments, the interaction of Gal3 with TLR4 or TREM2, or both, is disrupted by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the above percentages.

[0227] Also disclosed herein are anti-Gal3 antibodies or binding fragments thereof for use in treating a proteopathy in a subject in need thereof. In some embodiments, the proteopathy is selected from the group consisting of Alzheimer's disease, cerebral beta-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathy, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinocerebellar muscular atrophy, fragile X syndrome, Baratella-Scott syndrome, Friedreich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Pelizaeus-Merzbacher disease, seipinopathy, AA (analgesia), and others. and / or any disease caused by protein misfolding or aggregation, or any combination thereof.

[0228] Also disclosed herein are anti-Gal3 antibodies or binding fragments thereof for use in promoting neuronal regeneration in a subject in need thereof. In some embodiments, the subject has neuronal degeneration associated with inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof. In some embodiments, the neuronal degeneration is associated with Alzheimer's disease, and the anti-Gal3 antibody or binding fragment thereof interferes with binding of Gal3 to amyloid precursor protein (APP) or amyloid beta (Aβ), or both, in the subject. In some embodiments, more than one anti-Gal3 antibody or binding fragment thereof is administered to the subject.

[0229] When applied to any use disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3-26. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof belongs to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with antibodies belonging to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with antibodies belonging to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof competes with antibodies belonging to bin 3, 8, 17, or 24 for binding to Gal3.

[0230] When applied to any of the uses disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is H -CDR1, V H -CDR2, and V H a heavy chain variable region comprising CDR3, and (2) a V L -CDR1, V L -CDR2, and V L - a light chain variable region comprising CDR3. In some embodiments, V H CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27 to 44, 245 to 246, and 588 to 615, H CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45 to 60, 247 to 248, and 616 to 643; H - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61 to 81, 249 to 250, and 644 to 671; L CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82 to 101, 251 to 252, and 672 to 699; L CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and V L - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117-135, 254-255, and 728-755. In some embodiments, any use disclosed herein involving an anti-Gal3 antibody or binding fragment may be carried out using an antigen-binding molecule that binds to Gal3.

[0231] When applied to any of the uses disclosed herein, in some embodiments, exemplary V H -CDR1 sequences are depicted in Figure 18. In some embodiments, exemplary V H -CDR2 sequences are depicted in Figure 19. In some embodiments, exemplary V H -CDR3 sequences are depicted in Figure 20. In some embodiments, exemplary V L -CDR1 sequences are depicted in Figure 21. In some embodiments, exemplary V L -CDR2 sequences are depicted in Figure 22. In some embodiments, exemplary VL -CDR3 sequences are depicted in Figure 23. In some embodiments, any of the uses disclosed herein involving anti-Gal3 antibodies or binding fragments may be carried out with antigen-binding molecules that bind to Gal3.

[0232] When applied to any of the uses disclosed herein, in some embodiments, the heavy chain variable region (V H ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, and 756-783. In some embodiments, the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, and 756-783. In some embodiments, exemplary V H are depicted in Figures 24-1 to 24-5. In some embodiments, any of the uses disclosed herein involving anti-Gal3 antibodies or binding fragments may be carried out using antigen-binding molecules that bind to Gal3.

[0233] When applied to any of the uses disclosed herein, in some embodiments, the light chain variable region (V L ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 784-811. In some embodiments, the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 784-811. In some embodiments, exemplary V L are depicted in Figures 25-1 to 25-5. In some embodiments, any of the uses disclosed herein involving anti-Gal3 antibodies or binding fragments may be carried out using antigen-binding molecules that bind to Gal3.

[0234] When applied to any of the uses disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of 1) V in SEQ ID NO: 136 H -CDR1, V H -CDR2, VH -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 161 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 2) V within SEQ ID NO: 137 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 162 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 3) V within SEQ ID NO: 138 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 163 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 4) V within SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 164 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V LCDR3; 5) V within SEQ ID NO: 140 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 165 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 6) V within SEQ ID NO: 141 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 166 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 7) V within SEQ ID NO: 142 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 167 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 8) V within SEQ ID NO: 143 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 168 L -CDR1, V L -CDR2, V L -V in CDR3L -CDR1, V L -CDR2, V L CDR3; 9) V within SEQ ID NO: 144 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 169 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 10) V within SEQ ID NO: 145 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 170 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0235] 11) V in SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 171 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 12) V within SEQ ID NO: 146 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, VH - V within CDR3 and SEQ ID NO: 172 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 13) V within SEQ ID NO: 147 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 173 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 14) V within SEQ ID NO: 148 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 174 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 15) V within SEQ ID NO: 149 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 175 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 16) V within SEQ ID NO: 150 H -CDR1, V H -CDR2, V H-V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 176 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 17) V within SEQ ID NO: 151 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 177 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 18) V within SEQ ID NO: 152 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 178 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 19) V within SEQ ID NO: 153 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 179 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 20) V within SEQ ID NO: 154H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 180 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0236] 21) V in sequence number 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 181 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 22) V within SEQ ID NO: 156 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 182 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 23) V within SEQ ID NO: 157 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 183 L -CDR1, V L -CDR2, VL -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 24) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 184 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 25) V within SEQ ID NO: 158 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 185 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 26) V within SEQ ID NO: 159 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 186 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 27) V within SEQ ID NO: 160 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H- V within CDR3 and SEQ ID NO: 187 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 28) V within SEQ ID NO: 256 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 258 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 29) V within SEQ ID NO: 257 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 259 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 30) V within SEQ ID NO: 756 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 784 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0237] 31) V in sequence number 757 H -CDR1, VH -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 785 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 32) V within SEQ ID NO: 758 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 786 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 33) V within SEQ ID NO: 759 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 787 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 34) V within SEQ ID NO: 760 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 788 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, VL CDR3; 35) V within SEQ ID NO: 761 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 789 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 36) V within SEQ ID NO: 762 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 790 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 37) V within SEQ ID NO: 763 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 791 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 38) V within SEQ ID NO: 764 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 792 L -CDR1, V L -CDR2, V L-V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 39) V within SEQ ID NO: 765 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 793 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 40) V within SEQ ID NO: 766 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 794 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0238] 41) V in sequence number 767 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 795 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 42) V within SEQ ID NO: 768 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H-CDR2, V H - V within CDR3 and SEQ ID NO: 796 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 43) V within SEQ ID NO: 769 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 797 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 44) V within SEQ ID NO: 770 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 798 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 45) V within SEQ ID NO: 771 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 799 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 46) V within SEQ ID NO: 772 H -CDR1, V H -CDR2, VH -V in CDR3 H -CDR1, V H -CDR2, V H - CDR3 and V within SEQ ID NO: 800 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 47) V within SEQ ID NO: 773 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 801 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 48) V within SEQ ID NO: 774 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 802 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 49) V within SEQ ID NO: 775 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 803 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V LCDR3; 50) V within SEQ ID NO: 776 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 804 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0239] 51) V in sequence number 777 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 805 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 52) V within SEQ ID NO: 778 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 806 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 53) V within SEQ ID NO: 779 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 807 L -CDR1, VL -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 54) V within SEQ ID NO: 780 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 808 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 55) V within SEQ ID NO: 781 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 809 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 56) V within SEQ ID NO: 782 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 810 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; or 57) V within SEQ ID NO: 783 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H-CDR2, V H - V within CDR3 and SEQ ID NO: 811 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3. In some embodiments, exemplary combinations of heavy chain variable region CDRs are depicted in Figure 28. In some embodiments, exemplary combinations of light chain variable region CDRs are depicted in Figure 29. In some embodiments, any of the uses disclosed herein involving anti-Gal3 antibodies or binding fragments may be carried out using antigen-binding molecules that bind to Gal3.

[0240] When applied to any use disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises: 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 166; 7) the heavy chain variable region of SEQ ID NO: 142 and the light chain variable region of SEQ ID NO: 167; 8) the heavy chain variable region of SEQ ID NO: 143 and the light chain variable region of SEQ ID NO: 168; 9) the heavy chain variable region of SEQ ID NO: 144 and the light chain variable region of SEQ ID NO: 169; 10) the heavy chain variable region of SEQ ID NO: 145 and the light chain variable region of SEQ ID NO: 170; 11) the heavy chain variable region of SEQ ID NO: 139 and the light chain variable region of SEQ ID NO: 171; 12) the heavy chain variable region of SEQ ID NO: 146 and the light chain variable region of SEQ ID NO: 172; 13) the heavy chain variable region of SEQ ID NO: 147 and the light chain variable region of SEQ ID NO: 173 14) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 15) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 16) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 17) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 18) a heavy chain variable region of SEQ ID NO: 152 and a light chain variable region of SEQ ID NO: 178; 19) a heavy chain variable region of SEQ ID NO: 153 and a light chain variable region of SEQ ID NO: 179; 20) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180 21) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) the heavy chain variable region of SEQ ID NO: 156 and the light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) the heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187;28) a heavy chain variable region of SEQ ID NO: 256 and a light chain variable region of SEQ ID NO: 258; 29) a heavy chain variable region of SEQ ID NO: 257 and a light chain variable region of SEQ ID NO: 259; 30) a heavy chain variable region of SEQ ID NO: 756 and a light chain variable region of SEQ ID NO: 784;

[0241] 31) a heavy chain variable region of SEQ ID NO: 757 and a light chain variable region of SEQ ID NO: 785; 32) a heavy chain variable region of SEQ ID NO: 758 and a light chain variable region of SEQ ID NO: 786; 33) a heavy chain variable region of SEQ ID NO: 759 and a light chain variable region of SEQ ID NO: 787; 34) a heavy chain variable region of SEQ ID NO: 760 and a light chain variable region of SEQ ID NO: 788; 35) a heavy chain variable region of SEQ ID NO: 761 and a light chain variable region of SEQ ID NO: 789; 36) a heavy chain variable region of SEQ ID NO: 762 and a light chain variable region of SEQ ID NO: 790; 37) a heavy chain variable region of SEQ ID NO: 763 and a light chain variable region of SEQ ID NO: 791 38) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) the heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) the heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and 45) heavy chain variable region of SEQ ID NO: 771 and light chain variable region of SEQ ID NO: 799; 46) heavy chain variable region of SEQ ID NO: 772 and light chain variable region of SEQ ID NO: 800; 47) heavy chain variable region of SEQ ID NO: 773 and light chain variable region of SEQ ID NO: 801; 48) heavy chain variable region of SEQ ID NO: 774 and light chain variable region of SEQ ID NO: 802; 49) heavy chain variable region of SEQ ID NO: 775 and light chain variable region of SEQ ID NO: 803; 50) heavy chain variable region of SEQ ID NO: 776 and light chain variable region of SEQ ID NO: 804; 51) heavy chain of SEQ ID NO: 777 52) a heavy chain variable region of SEQ ID NO: 778 and a light chain variable region of SEQ ID NO: 806; 53) a heavy chain variable region of SEQ ID NO: 779 and a light chain variable region of SEQ ID NO: 807; 54) a heavy chain variable region of SEQ ID NO: 780 and a light chain variable region of SEQ ID NO: 808; 55) a heavy chain variable region of SEQ ID NO: 781 and a light chain variable region of SEQ ID NO: 809; 56) a heavy chain variable region of SEQ ID NO: 782 and a light chain variable region of SEQ ID NO: 810; or 57) a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO: 811.In some embodiments, any use disclosed herein involving an anti-Gal3 antibody or binding fragment can be carried out using an antigen-binding molecule that binds to Gal3. In some embodiments, the antibody has a sequence that is a consensus sequence of one, two, three, four, five, or six CDRs of any two or more (e.g., 3, 4, 5, 10, 15, 20, 25, 30, 35, 40, 50, 60, 70, or all) of the antibodies provided herein. In some embodiments, the antibody has a sequence that is a consensus sequence of the VH, VL, or VH and VL of any two or more (e.g., 3, 4, 5, 10, 15, 20, 25, 30, 35, 40, 50, 60, 70, or all) of the antibodies provided herein.

[0242] When applied to any of the uses disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a heavy chain (HC) sequence of any one of SEQ ID NOs: 188-216. In some embodiments, exemplary HC sequences are depicted in Figures 26-1 to 26-8. In some embodiments, any of the uses disclosed herein involving an anti-Gal3 antibody or binding fragment may be carried out using an antigen-binding molecule that binds to Gal3.

[0243] When applied to any of the uses disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a light chain (LC) sequence of any one of SEQ ID NOs: 217-243. In some embodiments, exemplary LC sequences are depicted in Figures 27-1 to 27-4. In some embodiments, any of the uses disclosed herein involving an anti-Gal3 antibody or binding fragment may be carried out using an antigen-binding molecule that binds to Gal3.

[0244] When applied to any use disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F 12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 847.14H4, 846T.1H2, mIMT001, 4A11.2B5, 4 A11.H1L1, 4A11.H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15G7.2A7, 19D9.2E5, 23B10.2B12 , 24D12.2H9, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 846T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9, 847.11 and at least one of 847.15D6, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

[0245] When applied to any use disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.1 4E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4 B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 8 46T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

[0246] In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4 , F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or at least one binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody selected from 846.4D5, 15F10.2D6, F846C.1B2, and F846C.1H12. In some embodiments, the heavy and light chain CDRs associated with each of the above antibodies are depicted in Figure 30. In some embodiments, the V associated with each of the above antibodies is H and V L are depicted in Figure 31. In some embodiments, the HC and LC associated with each of the above antibodies are depicted in Figure 32. In some embodiments, any of the uses disclosed herein involving anti-Gal3 antibodies or binding fragments may be carried out using antigen-binding molecules that bind to Gal3.

[0247] When applied to any of the uses disclosed herein, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is administered enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof. In some embodiments, the subject is a mammal. In some cases, the subject is a human.

[0248] Uses - Blood-brain barrier permeability In some embodiments, any one of the anti-Gal3 antibodies or binding fragments thereof disclosed herein can cross the blood-brain barrier and / or the blood-spinal cord barrier. In some embodiments, this phenomenon can be utilized by conjugating any one of the anti-Gal3 antibodies or binding fragments thereof capable of crossing the blood-brain barrier and / or the blood-spinal cord barrier to a payload to prepare an antibody conjugate. The blood-brain barrier and / or the blood-spinal cord barrier in these embodiments can be that of a mammal, such as a mouse, rat, other rodent, cat, dog, rabbit, cow, horse, sheep, pig, goat, or human. In some embodiments, the payload can be one that does not normally cross or does not effectively cross the blood-brain barrier and / or the blood-spinal cord barrier. The payload can be used to treat disease, for example, to have a cytotoxic effect on cancerous cells, or can be used for diagnosis or detection. In addition to the payloads disclosed herein, any other payload conventionally known in the art may be conjugated to any one of the anti-Gal3 antibodies or binding fragments thereof disclosed herein.

[0249] Disclosed herein is an antibody conjugate comprising any one of anti-Gal3 antibodies or their binding fragments and a payload conjugated to the anti-Gal3 antibody or its binding fragment, wherein the antibody conjugate can cross the blood-brain barrier.In some embodiments, the payload does not have the ability to cross the blood-brain barrier independently, or has low permeability across the blood-brain barrier when not conjugated to the anti-Gal3 antibody or its binding fragment.In some embodiments, the barrier is in a subject with a weakened or altered blood-brain barrier due to a disease that affects the blood-brain barrier, for example, that reduces the structural integrity of the barrier.

[0250] In some embodiments, conjugation of a payload to an anti-Gal3 antibody or binding fragment thereof increases the permeability of the payload across the blood-brain barrier by at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 200%, 300%, 400%, or 500%, or any increase within a range defined by any two of the above percentages, compared to the unconjugated payload. In some embodiments, the permeability of the payload across the blood-brain barrier is less than 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the permeability of the antibody conjugate across the blood-brain barrier. In some embodiments, the payload, the anti-Gal3 antibody or binding fragment thereof, or both are used to treat a neurological disorder, including inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastasis, or brain cancer (primary or secondary brain tumors), or any combination thereof. In some embodiments, the payload is a cytotoxic payload, a microtubule disrupting agent, a DNA modifying agent, an Akt inhibitor, a polymerase inhibitor, a detectable moiety, an immunomodulator, an immunotoxin, a nucleic acid polymer, an aptamer, a peptide, a protein, an enzyme, or any combination thereof. In some embodiments, the payload is a second antibody. In some embodiments, the second antibody does not independently have the ability to cross the blood-brain barrier, or has low permeability across the blood-brain barrier when not conjugated to an anti-Gal3 antibody or its binding fragment. In some embodiments, the blood-brain barrier is a mammalian blood-brain barrier. In some embodiments, the blood-brain barrier is a human blood-brain barrier.In some embodiments, the antibody conjugate is formulated for administration enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof.

[0251] When applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3-26. In some embodiments, the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3. In some embodiments, the anti-Gal3 antibody or binding fragment thereof belongs to bin 3, 8, 17, or 24. In some embodiments, the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody belonging to bin 3, 8, 17, or 24. In some embodiments, the interaction is disrupted by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, or 99%, or any percentage within a range defined by any two of the above percentages. In some embodiments, the anti-Gal3 antibody or binding fragment thereof competes with antibodies belonging to bins 3, 8, 17, or 24 for binding to Gal3.

[0252] As applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof may comprise any one or more of the sequences provided throughout this disclosure (e.g., V H -CDR1, V H -CDR2, V H -CDR3, V L -CDR1, V L -CDR2, V L-CDR3, heavy chain variable region, light chain variable region, heavy chain, or light chain sequence). In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises any one or more sequences shown in Figures 18-32, including any one or more CDRs, heavy chain variable region, light chain variable region, heavy chain, light chain, CDR combination, variable region combination, or heavy and light chain combination described therein. In some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to a peptide sequence encoded by any one or more of the nucleic acid sequences shown in Figures 37-1 through 40-12, including any nucleic acid sequence encoding a heavy chain variable region, light chain variable region, heavy chain, or light chain.

[0253] As applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises: (1) V H -CDR1, V H -CDR2, and V H a heavy chain variable region comprising CDR3, and (2) a V L -CDR1, V L -CDR2, and V L - a light chain variable region comprising CDR3. In some embodiments, V H CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27 to 44, 245 to 246, and 588 to 615, H CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45 to 60, 247 to 248, and 616 to 643; H - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61 to 81, 249 to 250, and 644 to 671; L CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82 to 101, 251 to 252, and 672 to 699; L CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and V L- CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117 to 135, 254 to 255, and 728 to 755.

[0254] As applied to any antibody conjugate, in some embodiments, exemplary V H -CDR1 sequences are depicted in Figure 18. In some embodiments, exemplary V H -CDR2 sequences are depicted in Figure 19. In some embodiments, exemplary V H -CDR3 sequences are depicted in Figure 20. In some embodiments, exemplary V L -CDR1 sequences are depicted in Figure 21. In some embodiments, exemplary V L -CDR2 sequences are depicted in Figure 22. In some embodiments, exemplary V L - The CDR3 sequences are depicted in Figure 23.

[0255] As applied to any antibody conjugate, in some embodiments, the heavy chain variable region (V H ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257. In some embodiments, the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257. In some embodiments, exemplary V H is depicted in Figures 24-1 to 24-5.

[0256] As applied to any antibody conjugate, in some embodiments, the light chain variable region (V L ) comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259. In some embodiments, the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259. In some embodiments, exemplary V L is depicted in Figures 25-1 to 25-5.

[0257] As applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of 1) V in SEQ ID NO: 136 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 161 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 2) V within SEQ ID NO: 137 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 162 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3; 3) V within SEQ ID NO: 138 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 163 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 4) V within SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 164 L -CDR1, VL -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 5) V within SEQ ID NO: 140 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 165 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 6) V within SEQ ID NO: 141 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 166 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 7) V within SEQ ID NO: 142 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 167 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 8) V within SEQ ID NO: 143 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, VH - V within CDR3 and SEQ ID NO: 168 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 9) V within SEQ ID NO: 144 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 169 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 10) V within SEQ ID NO: 145 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 170 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0258] 11) V in SEQ ID NO: 139 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 171 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 12) V within SEQ ID NO: 146 H-CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 172 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 13) V within SEQ ID NO: 147 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 173 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 14) V within SEQ ID NO: 148 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 174 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 15) V within SEQ ID NO: 149 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 175 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L-CDR2, V L CDR3; 16) V within SEQ ID NO: 150 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 176 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 17) V within SEQ ID NO: 151 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 177 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 18) V within SEQ ID NO: 152 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 178 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 19) V within SEQ ID NO: 153 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 179 L -CDR1, V L -CDR2, VL -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 20) V within SEQ ID NO: 154 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 180 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0259] 21) V in sequence number 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 181 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 22) V within SEQ ID NO: 156 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 182 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 23) V within SEQ ID NO: 157 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, VH -CDR2, V H - V within CDR3 and SEQ ID NO: 183 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 24) V within SEQ ID NO: 155 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 184 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 25) V within SEQ ID NO: 158 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 185 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 26) V within SEQ ID NO: 159 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 186 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 27) V within SEQ ID NO: 160 H -CDR1, V H-CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 187 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 28) V within SEQ ID NO: 256 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 258 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 29) V within SEQ ID NO: 257 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 259 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 30) V within SEQ ID NO: 756 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 784 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L-CDR3;

[0260] 31) V in sequence number 757 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 785 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 32) V within SEQ ID NO: 758 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 786 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 33) V within SEQ ID NO: 759 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 787 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 34) V within SEQ ID NO: 760 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 788 L -CDR1, VL -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 35) V within SEQ ID NO: 761 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 789 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 36) V within SEQ ID NO: 762 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 790 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 37) V within SEQ ID NO: 763 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 791 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 38) V within SEQ ID NO: 764 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, VH - V within CDR3 and SEQ ID NO: 792 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 39) V within SEQ ID NO: 765 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 793 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 40) V within SEQ ID NO: 766 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 794 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0261] 41) V in sequence number 767 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 795 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 42) V within SEQ ID NO: 768 H-CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 796 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 43) V within SEQ ID NO: 769 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 797 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 44) V within SEQ ID NO: 770 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 798 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 45) V within SEQ ID NO: 771 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 799 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L-CDR2, V L CDR3; 46) V within SEQ ID NO: 772 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - CDR3 and V within SEQ ID NO: 800 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 47) V within SEQ ID NO: 773 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 801 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 48) V within SEQ ID NO: 774 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 802 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 49) V within SEQ ID NO: 775 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 803 L -CDR1, V L -CDR2, VL -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 50) V within SEQ ID NO: 776 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 804 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3;

[0262] 51) V in sequence number 777 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 805 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 52) V within SEQ ID NO: 778 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 806 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 53) V within SEQ ID NO: 779 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, VH -CDR2, V H - V within CDR3 and SEQ ID NO: 807 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 54) V within SEQ ID NO: 780 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 808 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 55) V within SEQ ID NO: 781 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 809 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; 56) V within SEQ ID NO: 782 H -CDR1, V H -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 810 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L CDR3; or 57) V within SEQ ID NO: 783 H -CDR1, VH -CDR2, V H -V in CDR3 H -CDR1, V H -CDR2, V H - V within CDR3 and SEQ ID NO: 811 L -CDR1, V L -CDR2, V L -V in CDR3 L -CDR1, V L -CDR2, V L -CDR3. In some embodiments, exemplary combinations of heavy chain variable region CDRs are depicted in Figure 28. In some embodiments, exemplary combinations of light chain variable region CDRs are depicted in Figure 29.

[0263] When applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises: 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 6; 7) the heavy chain variable region of SEQ ID NO: 142 and the light chain variable region of SEQ ID NO: 167; 8) the heavy chain variable region of SEQ ID NO: 143 and the light chain variable region of SEQ ID NO: 168; 9) the heavy chain variable region of SEQ ID NO: 144 and the light chain variable region of SEQ ID NO: 169; 10) the heavy chain variable region of SEQ ID NO: 145 and the light chain variable region of SEQ ID NO: 170; 11) the heavy chain variable region of SEQ ID NO: 139 and the light chain variable region of SEQ ID NO: 171; 12) the heavy chain variable region of SEQ ID NO: 146 and the light chain variable region of SEQ ID NO: 172; 13) the heavy chain variable region of SEQ ID NO: 147 and the light chain variable region of SEQ ID NO: 173 14) the heavy chain variable region of SEQ ID NO: 148 and the light chain variable region of SEQ ID NO: 174; 15) the heavy chain variable region of SEQ ID NO: 149 and the light chain variable region of SEQ ID NO: 175; 16) the heavy chain variable region of SEQ ID NO: 150 and the light chain variable region of SEQ ID NO: 176; 17) the heavy chain variable region of SEQ ID NO: 151 and the light chain variable region of SEQ ID NO: 177; 18) the heavy chain variable region of SEQ ID NO: 152 and the light chain variable region of SEQ ID NO: 178; 19) the heavy chain variable region of SEQ ID NO: 153 and the light chain variable region of SEQ ID NO: 179; 20) the heavy chain variable region of SEQ ID NO: 154 and the light chain variable region of SEQ ID NO: 180 21) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) the heavy chain variable region of SEQ ID NO: 156 and the light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) the heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187;28) a heavy chain variable region of SEQ ID NO: 256 and a light chain variable region of SEQ ID NO: 258; 29) a heavy chain variable region of SEQ ID NO: 257 and a light chain variable region of SEQ ID NO: 259; 30) a heavy chain variable region of SEQ ID NO: 756 and a light chain variable region of SEQ ID NO: 784;

[0264] 31) a heavy chain variable region of SEQ ID NO: 757 and a light chain variable region of SEQ ID NO: 785; 32) a heavy chain variable region of SEQ ID NO: 758 and a light chain variable region of SEQ ID NO: 786; 33) a heavy chain variable region of SEQ ID NO: 759 and a light chain variable region of SEQ ID NO: 787; 34) a heavy chain variable region of SEQ ID NO: 760 and a light chain variable region of SEQ ID NO: 788; 35) a heavy chain variable region of SEQ ID NO: 761 and a light chain variable region of SEQ ID NO: 789; 36) a heavy chain variable region of SEQ ID NO: 762 and a light chain variable region of SEQ ID NO: 790; 37) a heavy chain variable region of SEQ ID NO: 763 and a light chain variable region of SEQ ID NO: 791 38) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) the heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) the heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and 45) heavy chain variable region of SEQ ID NO: 771 and light chain variable region of SEQ ID NO: 799; 46) heavy chain variable region of SEQ ID NO: 772 and light chain variable region of SEQ ID NO: 800; 47) heavy chain variable region of SEQ ID NO: 773 and light chain variable region of SEQ ID NO: 801; 48) heavy chain variable region of SEQ ID NO: 774 and light chain variable region of SEQ ID NO: 802; 49) heavy chain variable region of SEQ ID NO: 775 and light chain variable region of SEQ ID NO: 803; 50) heavy chain variable region of SEQ ID NO: 776 and light chain variable region of SEQ ID NO: 804; 51) heavy chain of SEQ ID NO: 777 52) a heavy chain variable region of SEQ ID NO: 778 and a light chain variable region of SEQ ID NO: 806; 53) a heavy chain variable region of SEQ ID NO: 779 and a light chain variable region of SEQ ID NO: 807; 54) a heavy chain variable region of SEQ ID NO: 780 and a light chain variable region of SEQ ID NO: 808; 55) a heavy chain variable region of SEQ ID NO: 781 and a light chain variable region of SEQ ID NO: 809; 56) a heavy chain variable region of SEQ ID NO: 782 and a light chain variable region of SEQ ID NO: 810; or 57) a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO: 811.

[0265] When applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a heavy chain (HC) sequence of any one of SEQ ID NOs: 188 to 216. In some embodiments, exemplary HC sequences are depicted in Figures 26-1 to 26-8.

[0266] When applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof comprises a light chain (LC) sequence of any one of SEQ ID NOs: 217 to 243. In some embodiments, exemplary LC sequences are depicted in Figures 27-1 to 27-4.

[0267] When applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F8 46C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F12 , F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 847.14H4, 846T.1H2, mIMT001, 4A11.2B5, 4A1 1.H1L1, 4A11.H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 846T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9, 847.11D or at least one of 847.5C2, 849.8D12, 847.5D13, 847.5F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, 847C.21H6, or a binding fragment thereof.

[0268] When applied to any antibody conjugate, in some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D 8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E 4, F846TC.16B5, F846TC.7F10, F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4B 10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846.2D4, 846.2F11, 846T.10B1, 846T.2E3, 84 6T.4C9, 846T.4E11, 846T.4F5, 846T.8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof. In some embodiments, the anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4 , F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or at least one binding fragment thereof.In some embodiments, the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody selected from 846.4D5, 15F10.2D6, F846C.1B2, and F846C.1H12. In some embodiments, the heavy and light chain CDRs associated with each of the above antibodies are depicted in Figure 30. In some embodiments, the V associated with each of the above antibodies. H and V L are depicted in Figure 31. In some embodiments, the HC and LC associated with each of the above antibodies are depicted in Figure 32.

[0269] Also disclosed herein are multispecific antibodies comprising a first binding domain that binds to Gal3 and a second binding domain that binds to a therapeutic target molecule located in the brain of a subject. In some embodiments, the second binding domain does not independently have the ability to cross the blood-brain barrier or has low permeability across the blood-brain barrier when not conjugated to an anti-Gal3 antibody or binding fragment thereof. In some embodiments, the permeability of the second binding domain across the blood-brain barrier is less than 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the permeability of the multispecific antibody across the blood-brain barrier. In some embodiments, the first binding domain that binds to Gal3 belongs to bin 3, 8, 17, or 24. In some embodiments, the first binding domain that binds to Gal3 disrupts the interaction of Gal3 with antibodies belonging to bin 3, 8, 17, or 24. In some embodiments, the first binding domain that binds to Gal3 competes with antibodies belonging to bin 3, 8, 17, or 24 for binding to Gal3. In some embodiments, the first binding domain that binds to Gal3 is a binding domain of an anti-Gal3 antibody or binding fragment thereof of any one of the antibody conjugates of claims 109-133. In some embodiments, the first binding domain is a binding domain of any one of the anti-Gal3 antibodies or bind...

Claims

1. (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ a heavy chain variable region including CDR3, and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ an anti-Gal3 antibody or a binding fragment thereof comprising a light chain variable region comprising CDR3; The V Ｈ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 36 to 44, 588 to 615, The V Ｈ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 54 to 60, 616 to 643, The V Ｈ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 70-81, 644-671, The V Ｌ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 92 to 101, 672 to 699, The V Ｌ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 111 to 116, 700 to 727, and The V Ｌ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 127 to 135, 728 to 755, An anti-Gal3 antibody or a binding fragment thereof.

2. The anti-Gal3 antibody or binding fragment thereof according to claim 1, wherein the heavy chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 147-160, 756-783.

3. The anti-Gal3 antibody or binding fragment thereof according to claim 1 or 2, wherein the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 147 to 160, 756 to 783.

4. The anti-Gal3 antibody or binding fragment thereof according to any one of claims 1 to 3, wherein the light chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 173 to 187, 784 to 811.

5. The anti-Gal3 antibody or binding fragment thereof according to any one of claims 1 to 4, wherein the light chain variable region is selected from the group consisting of SEQ ID NOs: 173 to 187, 784 to 811.

6. 1) V in SEQ ID NO: 147 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 173 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 149 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 175 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 150 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 176 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 151 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 177 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 152 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 178 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 153 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 179 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 154 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 180 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 181 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 156 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 182 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 157 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 183 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 184 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 158 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 185 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 159 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 186 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 160 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 187 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 28) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 43) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -CDR3 The anti-Gal3 antibody or binding fragment thereof according to any one of claims 1 to 5, comprising:

7. 1) a heavy chain variable region of SEQ ID NO: 147 and a light chain variable region of SEQ ID NO: 173; 2) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 3) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 4) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 5) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 6) a heavy chain variable region of SEQ ID NO: 152 and a light chain variable region of SEQ ID NO: 178; 7) a heavy chain variable region of SEQ ID NO: 153 and a light chain variable region of SEQ ID NO: 179; 8) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180; 9) a heavy chain variable region of SEQ ID NO: 155 and a light chain variable region of SEQ ID NO: 181; 10) a heavy chain variable region of SEQ ID NO: 156 and a light chain variable region of SEQ ID NO: 182; 11) a heavy chain variable region of SEQ ID NO: 157 and a light chain variable region of SEQ ID NO: 183; 12) a heavy chain variable region of SEQ ID NO: 155 and a light chain variable region of SEQ ID NO: 184; 13) a heavy chain variable region of SEQ ID NO: 158 and a light chain variable region of SEQ ID NO: 185; 14) a heavy chain variable region of SEQ ID NO: 159 and a light chain variable region of SEQ ID NO: 186; 15) a heavy chain variable region of SEQ ID NO: 160 and a light chain variable region of SEQ ID NO: 187; 16) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 17) the heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 18) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 19) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 20) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 21) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 22) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 23) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 24) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 25) the heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 26) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 27) the heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 28) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 29) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 30) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 31) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 32) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 33) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 34) the heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 35) the heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 36) the heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 37) The heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 38) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 39) The heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 40) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 41) The heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 42) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 43) The heavy chain variable region of SEQ ID NO: 783 and the light chain variable region of SEQ ID NO: 811 The anti-Gal3 antibody or binding fragment thereof according to any one of claims 1 to 6, comprising:

8. F846C. 1B2, F846C. 1F5, F846C. 1H12, F846C. 1H5, F846C. 2H3, F846TC. 14A2, F846TC. 14E4, F846TC. 16B5, F846TC. 7F10, F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T. 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C. The anti-Gal3 antibody or a binding fragment thereof according to any one of claims 1 to 7, which is selected from the group consisting of 21H6, 21H6, or a binding fragment thereof.

9. The anti-Gal3 antibody or binding fragment thereof according to any one of claims 1 to 8, wherein the antibody or binding fragment thereof is selected from the group consisting of F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4, F846TC.16B5, F846TC.7F10, F849C.8D10, F846.4D5, or a binding fragment thereof.

10. The anti-Gal3 antibody or binding fragment thereof according to any one of claims 1 to 10, which binds to one or more peptides of SEQ ID NOs: 3 to 26.

11. 1. A method of treating a neurological disorder in a subject in need thereof, comprising: administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the neurological disorder. method.

12. 12. The method of claim 11, further comprising selecting the subject as having or at risk of suffering from the neurological disorder prior to the administering step.

13. 13. The method of claim 11 or 12, further comprising detecting amelioration of symptoms associated with the neurological disorder after the administering step.

14. 14. The method of any one of claims 11 to 13, wherein the neurological disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof.

15. The method of any one of claims 11 to 14, wherein the neurological disorder is Alzheimer's disease and the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to amyloid precursor protein (APP) or amyloid beta (Aβ), or both.

16. 16. The method of claim 15, wherein the APP comprises the sequence of APP695 (SEQ ID NO: 2).

17. 17. The method of claim 15 or 16, wherein the Aβ comprises Aβ monomers, Aβ oligomers, Aβ fibrils, or any combination thereof.

18. The method of any one of claims 15 to 17, wherein the Aβ comprises the sequence of Aβ42 (SEQ ID NO: 244).

19. The method of any one of claims 15 to 18, wherein the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the aforementioned percentages.

20. The method of any one of claims 11 to 19, wherein the anti-Gal3 antibody or binding fragment thereof promotes the phagocytic function of microglia in the subject.

21. The method of any one of claims 11 to 20, wherein the anti-Gal3 antibody or binding fragment thereof reduces phospho-tau levels or Gal3 levels, or both, in the brain of the subject.

22. The method of any one of claims 11 to 21, wherein the anti-Gal3 antibody or binding fragment thereof inhibits Aβ-mediated activation of microglia in the subject.

23. 23. The method of claim 22, wherein the Aβ-mediated activation of microglia is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages.

24. The method of any one of claims 11 to 23, wherein the anti-Gal3 antibody or binding fragment thereof inhibits Aβ fibril or oligomer formation in the subject.

25. 25. The method of claim 24, wherein the Aβ fibril or oligomer formation is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages.

26. The method of any one of claims 11 to 25, wherein the anti-Gal3 antibody or binding fragment thereof promotes neuronal regeneration in the subject.

27. The method of any one of claims 11 to 26, wherein the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to Toll-like receptor 4 (TLR4) or triggering receptor expressed on myeloid cells 2 (TREM2), or both.

28. 28. The method of claim 27, wherein the binding of Gal3 to TLR4 or TREM2, or both, is disrupted by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the above percentages.

29. The method of any one of claims 11 to 28, wherein more than one anti-Gal3 antibody or binding fragment thereof is administered to the subject.

30. The method of any one of claims 11 to 29, wherein the anti-Gal3 antibody or binding fragment thereof is administered in conjunction with one or more additional therapeutic compositions.

31. 31. The method of claim 30, wherein the one or more additional therapeutic compositions comprise a cholinesterase inhibitor, an NMDA receptor antagonist, or both.

32. 32. The method of claim 31 , wherein the cholinesterase inhibitor comprises tacrine, rivastigmine, galantamine, donepezil, or any combination thereof.

33. 33. The method of claim 31 or 32, wherein the NMDA receptor antagonist comprises memantine.

34. 1. A method for disrupting binding of Gal3 to APP or Aβ, or both, comprising: contacting the APP or Aβ, or both, with an anti-Gal3 antibody or a binding fragment thereof, thereby disrupting the binding of Gal3 to APP. method.

35. 35. The method of claim 34, wherein the APP or Aβ, or both, is soluble or part of a first cell.

36. 36. The method of claim 34 or 35, wherein the Gal3 is soluble or part of a second cell.

37. The method of any one of claims 34 to 36, wherein the APP comprises the sequence of APP695 (SEQ ID NO: 2).

38. 38. The method of any one of claims 34 to 37, wherein the Aβ comprises Aβ monomers, Aβ oligomers, Aβ fibrils, or any combination thereof.

39. The method of any one of claims 34 to 38, wherein the Aβ comprises the sequence of Aβ42 (SEQ ID NO: 244).

40. The method of any one of claims 34 to 39, wherein the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 85%.

41. The method of any one of claims 34 to 40, wherein the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 90%.

42. The method of any one of claims 34 to 41, wherein the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 95%.

43. The method of any one of claims 34 to 42, wherein the APP is contacted with more than one anti-Gal3 antibody or binding fragment thereof.

44. 1. A method of treating a proteopathy in a subject in need thereof, comprising: administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby treating the proteopathy in the subject. method.

45. 45. The method of claim 44, further comprising selecting the subject as having or at risk of suffering from the proteopathy prior to the administering step.

46. 46. ​​The method of claim 44 or 45, further comprising detecting amelioration of symptoms associated with the proteopathy after the administering step.

47. 47. The method of any one of claims 44-46, wherein treating the proteopathy comprises treating an active proteopathy in the subject, or prophylactic treatment, or both.

48. The proteopathy is selected from the group consisting of Alzheimer's disease, cerebral β-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathy, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinobulbar muscular atrophy, spinocerebellar ataxia, fragile X syndrome, Baratellar-Scott syndrome, Friedreich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Pelizaeus-Merzbacher disease, seipinopathy, AA (secondary) amyloidosis, type II glycolysis, and the like.

48. The method of any one of claims 44 to 47, comprising treating a disease caused by protein misfolding or aggregation, including urinary tract amyloidosis, fibrinogen amyloidosis, dialysis amyloidosis, inclusion body myositis / myopathy, familial amyloidotic neuropathy, senile systemic amyloidosis, serpinopathy, atrial amyloidosis, pituitary prolactinoma, insulin amyloidosis, corneal lactoferrin amyloidosis, pulmonary alveolar proteinosis, seminal vesicle amyloidosis, cutaneous lichen amyloidosis, Mallory bodies, or odontogenic (Pindborg) tumor amyloid, or any disease caused by protein misfolding or aggregation, or any combination thereof.

49. The method of any one of claims 44 to 48, wherein more than one anti-Gal3 antibody or binding fragment thereof is administered to the subject.

50. The method of any one of claims 44 to 49, wherein the anti-Gal3 antibody or binding fragment thereof is administered in conjunction with one or more additional therapeutic compositions.

51. 51. The method of claim 50, wherein the one or more additional therapeutic compositions comprise a cholinesterase inhibitor, an NMDA receptor antagonist, insulin, or any combination thereof.

52. 52. The method of claim 51, wherein the cholinesterase inhibitor comprises tacrine, rivastigmine, galantamine, donepezil, or any combination thereof.

53. 53. The method of claim 51 or 52, wherein the NMDA receptor antagonist comprises memantine.

54. 1. A method of administering an antibody to a subject, comprising: administering to the subject an anti-Gal3 antibody or binding fragment thereof. method.

55. 55. The method of claim 54, further comprising selecting the subject as having or at risk of suffering from a neurological disease or proteopathy prior to said administering step.

56. 56. The method of claim 54 or 55, wherein the neurological disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof.

57. 57. The method of any one of claims 54 to 56, wherein the neurological disorder is Alzheimer's disease.

58. The proteopathy is selected from the group consisting of Alzheimer's disease, cerebral β-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathy, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinobulbar muscular atrophy, spinocerebellar ataxia, fragile X syndrome, Baratellar-Scott syndrome, Friedreich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Pelizaeus-Merzbacher disease, seipinopathy, AA (secondary) amyloidosis, type II glycolysis, and the like.

58. The method of any one of claims 54 to 57, comprising treating a disease caused by protein misfolding or aggregation, including urinary tract amyloidosis, fibrinogen amyloidosis, dialysis amyloidosis, inclusion body myositis / myopathy, familial amyloidotic neuropathy, senile systemic amyloidosis, serpinopathy, atrial amyloidosis, pituitary prolactinoma, insulin amyloidosis, corneal lactoferrin amyloidosis, pulmonary alveolar proteinosis, seminal vesicle amyloidosis, cutaneous lichen amyloidosis, Mallory bodies, or odontogenic (Pindborg) tumor amyloid, or any disease caused by protein misfolding or aggregation, or any combination thereof.

59. The method of any one of claims 54 to 58, wherein more than one anti-Gal3 antibody or binding fragment thereof is administered to the subject.

60. 1. A method of promoting neuronal regeneration in a subject in need thereof, comprising: administering to the subject an effective amount of an anti-Gal3 antibody or binding fragment thereof, thereby promoting neuronal regeneration in the subject. method.

61. 61. The method of claim 60, further comprising selecting the subject as having or at risk of having neuronal degeneration prior to said administering step.

62. 62. The method of claim 60 or 61, further comprising detecting said neuronal regeneration in said subject after said administering step.

63. 63. The method of any one of claims 60 or 62, wherein the subject has a neuronal degeneration associated with inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof.

64. The method of claim 63, wherein the neuronal degeneration is associated with Alzheimer's disease and the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to amyloid precursor protein (APP) or amyloid beta (Aβ), or both.

65. The method of any one of claims 60 to 64, wherein more than one anti-Gal3 antibody or binding fragment thereof is administered to the subject.

66. 66. The method of any one of claims 11 to 65, wherein the anti-Gal3 antibody or binding fragment thereof is administered enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof.

67. The method of any one of claims 11 to 66, wherein the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3 to 26.

68. The method of any one of claims 11 to 67, wherein the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3.

69. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ a heavy chain variable region including CDR3, and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ - comprising a light chain variable region comprising CDR3; The V Ｈ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27-44, 245-256, 588-615, The V Ｈ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45-60, 247-248, 616-643, The V Ｈ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61-81, 249-250, 644-671, The V Ｌ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82-101, 251-252, 672-699, The V Ｌ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and The V Ｌ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117-135, 254-255, 728-755, 69. The method of any one of claims 11 to 68.

70. 70. The method of any one of claims 11-69, wherein the heavy chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, 756-783.

71. 71. The method of any one of claims 11 to 70, wherein the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, 756-783.

72. 72. The method of any one of claims 11-71, wherein the light chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 784-811.

73. 73. The method of any one of claims 11-72, wherein the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 784-811.

74. the anti-Gal3 antibody or binding fragment thereof 1) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 147 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 173 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 149 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 175 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 150 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 176 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 151 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 177 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 152 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 178 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 153 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 179 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 154 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 180 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 181 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 156 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 182 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 157 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 183 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 184 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 158 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 185 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 159 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 186 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 160 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 187 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 28) V in SEQ ID NO: 256 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 258 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 257 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 259 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 43) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 44) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 45) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 46) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 47) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 48) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 49) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 50) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 51) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 52) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 53) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 54) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 55) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 56) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 57) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -CDR3 74. The method of any one of claims 11 to 73, comprising:

75. the anti-Gal3 antibody or binding fragment thereof 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 7) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 8) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 9) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 10) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; 11) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; 12) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; 13) a heavy chain variable region of SEQ ID NO: 147 and a light chain variable region of SEQ ID NO: 173; 14) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 15) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 16) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 17) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 18) the heavy chain variable region of SEQ ID NO: 152 and the light chain variable region of SEQ ID NO: 178; 19) The heavy chain variable region of SEQ ID NO: 153 and the light chain variable region of SEQ ID NO: 179; 20) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180; 21) The heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) a heavy chain variable region of SEQ ID NO: 156 and a light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) The heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187 28) the heavy chain variable region of SEQ ID NO: 256 and the light chain variable region of SEQ ID NO: 258; 29) The heavy chain variable region of SEQ ID NO: 257 and the light chain variable region of SEQ ID NO: 259; 30) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 31) The heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 32) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 33) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 34) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 35) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 36) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 37) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 38) The heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) The heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) The heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 45) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 46) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 47) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 48) The heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 49) The heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 50) the heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 51) The heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 52) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 53) the heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 54) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 55) The heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 56) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 57) The heavy chain variable region of SEQ ID NO: 783 and the light chain variable region of SEQ ID NO: 811 75. The method of any one of claims 11 to 74, comprising:

76. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

76. The method of any one of claims 11 to 75, wherein the antibody is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

77. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C.

77. The method of any one of claims 11-76, wherein the antibody is selected from the group consisting of F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

78. The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4, F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, and 846T.

78. The method of any one of claims 11 to 77, wherein the antibody is selected from the group consisting of 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

79. An anti-Gal3 antibody or binding fragment thereof for use in treating a neurodegenerative disorder in a subject in need thereof.

80. 80. The use of claim 79, wherein the neurodegenerative disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof.

81. The use of claim 79 or 80, wherein the neurological disorder is Alzheimer's disease and the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to amyloid precursor protein (APP) or Aβ, or both.

82. 82. The use of claim 81, wherein the APP comprises the sequence of APP695 (SEQ ID NO: 2).

83. 83. The use of claim 81 or 82, wherein the Aβ comprises Aβ monomers, Aβ oligomers, Aβ fibrils, or any combination thereof.

84. The use according to any one of claims 81 to 83, wherein the Aβ comprises the sequence of Aβ42 (SEQ ID NO: 244).

85. The use of any one of claims 81 to 84, wherein the anti-Gal3 antibody or binding fragment thereof reduces the binding of Gal3 to APP or Aβ, or both, by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the aforementioned percentages.

86. The use according to any one of claims 79 to 85, wherein the anti-Gal3 antibody or binding fragment thereof promotes the phagocytic function of microglia in the subject.

87. The use of any one of claims 79 to 86, wherein the anti-Gal3 antibody or binding fragment thereof inhibits Aβ-mediated activation of microglia in the subject.

88. 88. The use of claim 87, wherein the Aβ-mediated activation of microglia is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the foregoing percentages.

89. The use of any one of claims 79 to 88, wherein the anti-Gal3 antibody or binding fragment thereof inhibits Aβ fibril or oligomer formation in the subject.

90. 90. The use of claim 89, wherein the Aβ fibril or oligomer formation is inhibited by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the aforementioned percentages.

91. The use of any one of claims 79 to 90, wherein the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with Toll-like receptor 4 (TLR4) or triggering receptor expressed on myeloid cells 2 (TREM2), or both.

92. 92. The use of claim 91, wherein the interaction of Gal3 with TLR4 or TREM2, or both, is disrupted by at least 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 96%, 97%, 98%, or 99%, or any percentage within a range defined by any two of the above percentages.

93. An anti-Gal3 antibody or binding fragment thereof for use in treating a proteopathy in a subject in need thereof.

94. The proteopathy is selected from the group consisting of Alzheimer's disease, cerebral β-amyloid angiopathy, retinal ganglion cell degeneration in glaucoma, Parkinson's disease, Lewy dementia, multiple system atrophy, synucleinopathies, Pick's disease, corticobasal degeneration, tauopathy, frontotemporal lobar degeneration, Huntington's disease, dentatorubral-pallidoluysian atrophy, spinobulbar muscular atrophy, spinocerebellar ataxia, fragile X syndrome, Baratella-Scott syndrome, Friedreich's ataxia, myotonic dystrophy, Alexander disease, familial British dementia, familial Danish dementia, Pelizaeus-Merzbacher disease, seipinopathy, and AA (secondary) amyloidosis. , type II diabetes, fibrinogen amyloidosis, dialysis amyloidosis, inclusion body myositis / myopathy, familial amyloidotic neuropathy, senile systemic amyloidosis, serpinopathy, atrial amyloidosis, pituitary prolactinoma, insulin amyloidosis, corneal lactoferrin amyloidosis, pulmonary alveolar proteinosis, seminal vesicle amyloidosis, cutaneous lichen amyloidosis, Mallory bodies, or odontogenic (Pindborg) tumor amyloid, or any disease caused by protein misfolding or aggregation, or any combination thereof.

95. An anti-Gal3 antibody or binding fragment thereof for use in promoting neuronal regeneration in a subject in need thereof.

96. 96. The use of claim 95, wherein the subject has a neuronal degeneration associated with inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, brain cancer, or any combination thereof.

97. The use described in claim 96, wherein the neuronal degeneration is associated with Alzheimer's disease and the anti-Gal3 antibody or binding fragment thereof interferes with the binding of Gal3 to amyloid precursor protein (APP) or amyloid beta (Aβ), or both, in the subject.

98. The use of any one of claims 95 to 97, wherein more than one anti-Gal3 antibody or binding fragment thereof is administered to the subject.

99. The use according to any one of claims 79 to 98, wherein the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3 to 26.

100. The use of any one of claims 79 to 99, wherein the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3.

101. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ a heavy chain variable region including CDR3, and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ - comprising a light chain variable region comprising CDR3; The V Ｈ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27-44, 245-246, 588-615, The V Ｈ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45-60, 247-248, 616-643, The V Ｈ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61-81, 249-250, 644-671, The V Ｌ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82-101, 251-252, 672-699, The V Ｌ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and The V Ｌ - Use according to any one of claims 79 to 100, wherein CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117 to 135, 254 to 255, 728 to 755.

102. 102. The use of any one of claims 79 to 101, wherein the heavy chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, 756-783.

103. The use of any one of claims 79 to 102, wherein the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, 756-783.

104. 104. The use of any one of claims 79 to 103, wherein the light chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 784-811.

105. The use of any one of claims 79 to 104, wherein the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 784-811.

106. the anti-Gal3 antibody or binding fragment thereof 1) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 147 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 173 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 149 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 175 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 150 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 176 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 151 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 177 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 152 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 178 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 153 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 179 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 154 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 180 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 181 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 156 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 182 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 157 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 183 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 184 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 158 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 185 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 159 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 186 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 160 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 187 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 28) V in SEQ ID NO: 256 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 258 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 257 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 259 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 43) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 44) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 45) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 46) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 47) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 48) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 49) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 50) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 51) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 52) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 53) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 54) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 55) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 56) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 57) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -CDR3 The use according to any one of claims 79 to 105, comprising:

107. the anti-Gal3 antibody or binding fragment thereof 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 7) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 8) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 9) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 10) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; 11) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; 12) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; 13) a heavy chain variable region of SEQ ID NO: 147 and a light chain variable region of SEQ ID NO: 173; 14) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 15) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 16) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 17) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 18) the heavy chain variable region of SEQ ID NO: 152 and the light chain variable region of SEQ ID NO: 178; 19) The heavy chain variable region of SEQ ID NO: 153 and the light chain variable region of SEQ ID NO: 179; 20) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180; 21) The heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) a heavy chain variable region of SEQ ID NO: 156 and a light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) the heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187; 28) the heavy chain variable region of SEQ ID NO: 256 and the light chain variable region of SEQ ID NO: 258; 29) The heavy chain variable region of SEQ ID NO: 257 and the light chain variable region of SEQ ID NO: 259; 30) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 31) The heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 32) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 33) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 34) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 35) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 36) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 37) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 38) The heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) The heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) The heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 45) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 46) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 47) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 48) The heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 49) The heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 50) the heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 51) The heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 52) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 53) the heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 54) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 55) The heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 56) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 57) The use of any one of claims 79 to 106, comprising a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO:

811.

108. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

108. The use of any one of claims 79 to 107, wherein the antibody is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

109. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C.

109. The use of any one of claims 79 to 108, wherein the antibody is selected from the group consisting of F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

110. The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4, F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, and 846T.

110. The use of any one of claims 79 to 109, wherein the antibody is selected from the group consisting of: 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

111. The use of any one of claims 79 to 110, wherein the anti-Gal3 antibody or binding fragment thereof is administered enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof.

112. The method of any one of claims 11 to 78, wherein the anti-Gal3 antibody or binding fragment thereof is capable of crossing the blood-brain barrier.

113. The use according to any one of claims 79 to 111, wherein the anti-Gal3 antibody or binding fragment thereof is capable of crossing the blood-brain barrier.

114. 1. An antibody conjugate comprising: an anti-Gal3 antibody or binding fragment thereof; and a payload conjugated to the anti-Gal3 antibody or binding fragment thereof; Able to cross the blood-brain barrier Antibody conjugates.

115. The antibody conjugate of claim 114, wherein the payload does not independently have the ability to cross the blood-brain barrier or has low permeability across the blood-brain barrier when not conjugated to the anti-Gal3 antibody or binding fragment thereof.

116. The antibody conjugate of claim 114 or 115, wherein conjugation of the payload to the anti-Gal3 antibody or binding fragment thereof increases the permeability of the payload across the blood-brain barrier by at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 200%, 300%, 400%, or 500%, or any increase within a range defined by any two of the above percentages, compared to the unconjugated payload.

117. 117. The antibody conjugate of any one of claims 114 to 116, wherein the permeability of the payload across the blood-brain barrier is less than 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the permeability of the antibody conjugate across the blood-brain barrier.

118. The antibody conjugate of any one of claims 114 to 117, wherein the payload or the anti-Gal3 antibody or binding fragment thereof, or both, are used to treat a neurological disorder that is treated in the brain.

119. 119. The antibody conjugate of any one of claims 114-118, wherein said neurological disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastasis, or brain cancer, or any combination thereof.

120. 120. The antibody conjugate of any one of claims 114 to 119, wherein the payload is a cytotoxic payload, a microtubule disrupting agent, a DNA modifying agent, an Akt inhibitor, a polymerase inhibitor, a detectable moiety, an immunomodulator, an immunotoxin, a nucleic acid polymer, an aptamer, a peptide, a protein, an enzyme, or any combination thereof.

121. The antibody conjugate of any one of claims 114 to 120, wherein the payload is a second antibody.

122. The antibody conjugate of claim 121, wherein the second antibody does not independently have the ability to cross the blood-brain barrier or has low permeability across the blood-brain barrier when not conjugated to the anti-Gal3 antibody or binding fragment thereof.

123. The antibody conjugate of any one of claims 114 to 122, wherein the blood-brain barrier is a mammalian blood-brain barrier.

124. The antibody conjugate of any one of claims 114 to 123, wherein the blood-brain barrier is the human blood-brain barrier.

125. 125. The antibody conjugate of any one of claims 114 to 124, formulated for administration enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof.

126. The antibody conjugate of any one of claims 114 to 125, wherein the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3 to 26.

127. The antibody conjugate of any one of claims 114 to 126, wherein the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3.

128. The antibody conjugate of any one of claims 114 to 127, wherein the anti-Gal3 antibody or binding fragment thereof belongs to bin 3, 8, 17, or 24.

129. The antibody conjugate of any one of claims 114 to 128, wherein the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with antibodies belonging to bins 3, 8, 17 or 24.

130. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ a heavy chain variable region including CDR3, and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ - comprising a light chain variable region comprising CDR3; The V Ｈ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27-44, 245-246, 588-615, The V Ｈ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45-60, 247-248, 616-643, The V Ｈ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61-81, 249-250, 644-671, The V Ｌ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82-101, 251-252, 672-699, The V Ｌ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and The V Ｌ The antibody conjugate of any one of claims 114 to 129, wherein CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117 to 135, 254 to 255, 728 to 755.

131. 131. The antibody conjugate of any one of claims 114 to 130, wherein the heavy chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, 756-783.

132. The antibody conjugate of any one of claims 114 to 131, wherein the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, 756-783.

133. 133. The antibody conjugate of any one of claims 114 to 132, wherein the light chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 784-811.

134. The antibody conjugate of any one of claims 114 to 133, wherein the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 784-811.

135. the anti-Gal3 antibody or binding fragment thereof 1) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 147 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 173 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 149 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 175 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 150 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 176 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 151 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 177 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 152 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 178 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 153 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 179 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 154 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 180 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 181 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 156 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 182 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 157 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 183 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 184 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 158 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 185 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 159 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 186 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 160 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 187 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 28) V in SEQ ID NO: 256 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 258 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 257 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 259 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 43) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 44) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 45) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 46) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 47) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 48) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 49) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 50) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 51) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 52) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 53) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 54) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 55) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 56) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 57) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3. The antibody conjugate of any one of claims 114 to 134.

136. the anti-Gal3 antibody or binding fragment thereof 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 7) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 8) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 9) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 10) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; 11) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; 12) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; 13) a heavy chain variable region of SEQ ID NO: 147 and a light chain variable region of SEQ ID NO: 173; 14) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 15) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 16) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 17) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 18) the heavy chain variable region of SEQ ID NO: 152 and the light chain variable region of SEQ ID NO: 178; 19) The heavy chain variable region of SEQ ID NO: 153 and the light chain variable region of SEQ ID NO: 179; 20) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180; 21) The heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) a heavy chain variable region of SEQ ID NO: 156 and a light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) The heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187 28) the heavy chain variable region of SEQ ID NO: 256 and the light chain variable region of SEQ ID NO: 258; 29) The heavy chain variable region of SEQ ID NO: 257 and the light chain variable region of SEQ ID NO: 259; 30) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 31) The heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 32) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 33) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 34) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 35) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 36) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 37) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 38) The heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) The heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) The heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 45) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 46) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 47) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 48) The heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 49) The heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 50) the heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 51) The heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 52) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 53) the heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 54) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 55) The heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 56) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 57) The antibody conjugate of any one of claims 114 to 135, comprising a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO:

811.

137. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

137. The antibody conjugate of any one of claims 114-136, wherein the antibody conjugate is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

138. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C.

138. The antibody conjugate of any one of claims 114-137, selected from the group consisting of F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

139. The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4, F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, and 846T.

139. The antibody conjugate of any one of claims 114 to 138, selected from the group consisting of: 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

140. 140. The antibody conjugate of any one of claims 114 to 139, wherein the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody selected from 846.4D5, 15F10.2D6, F846C.1B2, and F846C.1H12.

141. A multispecific antibody comprising a first binding domain that binds to Gal3 and a second binding domain that binds to a therapeutic target molecule located in the brain of a subject.

142. 142. The multispecific antibody of claim 141, wherein the second binding domain does not independently have the ability to cross the blood-brain barrier or has low permeability across the blood-brain barrier when not conjugated to an anti-Gal3 antibody or binding fragment thereof.

143. 143. The multispecific antibody of claim 141 or 142, wherein the permeability of the second binding domain across the blood-brain barrier is less than 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the permeability of the multispecific antibody across the blood-brain barrier.

144. 144. The multispecific antibody of any one of claims 141 to 143, wherein the first binding domain that binds to Gal3 belongs to bin 3, 8, 17, or 24.

145. 145. The multispecific antibody of any one of claims 141 to 144, wherein the first binding domain that binds to Gal3 disrupts the interaction of Gal3 with antibodies belonging to bins 3, 8, 17 or 24.

146. 146. The multispecific antibody of any one of claims 141 to 145, wherein the first binding domain that binds to Gal3 competes with antibodies belonging to bin 3, 8, 17 or 24 for binding to Gal3.

147. 147. The multispecific antibody of any one of claims 141 to 146, wherein the first binding domain that binds to Gal3 is the binding domain of the anti-Gal3 antibody or binding fragment thereof of any one of the antibody conjugates of claims 114 to 140.

148. 148. A pharmaceutical composition comprising the antibody conjugate of any one of claims 114 to 140 or the multispecific antibody of any one of claims 141 to 147 and at least one pharmaceutically acceptable diluent, excipient or carrier.

149. 1. A method for delivering a payload to the central nervous system of a subject in need thereof, comprising: administering to the subject an antibody conjugate comprising an anti-Gal3 antibody or binding fragment thereof and a payload conjugated to the anti-Gal3 antibody or binding fragment thereof; the antibody conjugate is capable of crossing the blood-brain barrier; method.

150. 1. A method of increasing the permeability of a payload across the blood-brain barrier in a subject in need thereof, comprising: conjugating an anti-Gal3 antibody or a binding fragment thereof to the payload to form an antibody conjugate; method.

151. 151. The method of claim 150, further comprising administering the antibody conjugate to the subject.

152. 152. The method of any one of claims 149-151, wherein the payload does not normally cross the blood-brain barrier.

153. 153. The method of any one of claims 149-152, wherein conjugating the payload to the anti-Gal3 antibody or binding fragment thereof increases the permeability of the payload across the blood-brain barrier by at least 5%, 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, 100%, 200%, 300%, 400%, or 500%, or any increase within a range defined by any two of the foregoing percentages, compared to the unconjugated payload.

154. 154. The method of any one of claims 149-153, wherein the permeability of the payload across the blood-brain barrier is less than 95%, 90%, 80%, 70%, 60%, 50%, 40%, 30%, 20%, 10%, 9%, 8%, 7%, 6%, 5%, 4%, 3%, 2%, or 1% of the permeability of the antibody conjugate across the blood-brain barrier.

155. The method of any one of claims 149 to 154, wherein the payload, or the anti-Gal3 antibody or binding fragment thereof, or both, are used to treat a neurological disorder.

156. 156. The method of claim 155, wherein the neurological disorder comprises inflammation, encephalitis, Alzheimer's disease, Parkinson's disease, Huntington's disease, traumatic brain injury, spinal cord injury, multiple sclerosis, amyotrophic lateral sclerosis, olfactory dysfunction, aphasia, Bell's palsy, transmissible spongiform encephalopathy, Creutzfeldt-Jakob disease, fatal familial insomnia, epilepsy, seizures, neurodevelopmental disorders, Tourette's syndrome, neuroinfectious disorders, meningitis, encephalitis, bovine spongiform encephalopathy, West Nile virus encephalitis, Neuro-AIDS, Fragile X syndrome, Guillain-Barré syndrome, brain metastases, or brain cancer, or any combination thereof.

157. 157. The method of any one of claims 149-156, wherein the payload is a cytotoxic payload, a microtubule disrupting agent, a DNA modifying agent, an Akt inhibitor, a polymerase inhibitor, a detectable moiety, an immunomodulator, an immunotoxin, a nucleic acid polymer, an aptamer, a peptide, a protein, an enzyme, or any combination thereof.

158. 158. The method of any one of claims 149 to 157, wherein the payload is a second antibody.

159. The method of any one of claims 149 to 158, wherein the second antibody does not independently have the ability to cross the blood-brain barrier or has low permeability across the blood-brain barrier when not conjugated to the anti-Gal3 antibody or binding fragment thereof.

160. 160. The method of any one of claims 149 to 159, wherein the subject is a mammal.

161. 161. The method of any one of claims 149 to 160, wherein the subject is a human.

162. 162. The method of any one of claims 149-161, wherein the antibody conjugate is administered enterally, orally, intranasally, parenterally, intracranially, subcutaneously, intramuscularly, intradermally, or intravenously, or any combination thereof.

163. The method of any one of claims 149 to 162, wherein the anti-Gal3 antibody or binding fragment thereof binds to one or more peptides of SEQ ID NOs: 3 to 26.

164. The method of any one of claims 149 to 163, wherein the anti-Gal3 antibody or binding fragment thereof binds to the N-terminal domain of Gal3, the N-terminus of Gal3, or the tandem repeat domain (TRD) of Gal3.

165. The method of any one of claims 149 to 164, wherein the anti-Gal3 antibody or binding fragment thereof belongs to bin 3, 8, 17, or 24.

166. The method of any one of claims 149 to 165, wherein the anti-Gal3 antibody or binding fragment thereof interferes with the interaction of Gal3 with antibodies belonging to bins 3, 8, 17 or 24.

167. The method of any one of claims 149 to 166, wherein the anti-Gal3 antibody or binding fragment thereof competes with antibodies belonging to bins 3, 8, 17 or 24 for binding to Gal3.

168. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ a heavy chain variable region including CDR3, and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ - comprising a light chain variable region comprising CDR3; The V Ｈ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 27-44, 245-246, 588-615, The V Ｈ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 45-60, 247-248, 616-643, The V Ｈ - CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 61-81, 249-250, 644-671, The V Ｌ - CDR1 comprises an amino acid sequence selected from SEQ ID NOs: 82-101, 251-252, 672-699, The V Ｌ - CDR2 comprises an amino acid sequence selected from SEQ ID NOs: 102 to 116, 253, 700 to 727, and The V Ｌ The method according to any one of claims 149 to 167, wherein CDR3 comprises an amino acid sequence selected from SEQ ID NOs: 117 to 135, 254 to 255, 728 to 755.

169. 169. The method of any one of claims 149-168, wherein the heavy chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 136-160, 256-257, 756-783.

170. 170. The method of any one of claims 149-169, wherein the heavy chain variable region is selected from the group consisting of SEQ ID NOs: 136-160, 256-257, 756-783.

171. 171. The method of any one of claims 149-170, wherein the light chain variable region comprises an amino acid sequence having at least 75%, 80%, 85%, 90%, 95%, or 100% sequence identity to any of the sequences set forth in SEQ ID NOs: 161-187, 258-259, 784-811.

172. 172. The method of any one of claims 149-171, wherein the light chain variable region is selected from the group consisting of SEQ ID NOs: 161-187, 258-259, 784-811.

173. the anti-Gal3 antibody or binding fragment thereof 1) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 147 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 173 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 149 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 175 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 150 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 176 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 151 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 177 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 152 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 178 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 153 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 179 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 154 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 180 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 181 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 156 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 182 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 157 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 183 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 155 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 184 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 158 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 185 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 159 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 186 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 160 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 187 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -CDR3 28) V in SEQ ID NO: 256 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 258 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 257 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 259 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 43) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 44) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 45) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 46) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 47) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 48) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 49) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 50) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 51) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 52) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 53) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 54) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 55) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 56) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 57) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -CDR3 173. The method of any one of claims 149 to 172, comprising:

174. the anti-Gal3 antibody or binding fragment thereof 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 6) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 7) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 8) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 9) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 10) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; 11) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; 12) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; 13) a heavy chain variable region of SEQ ID NO: 147 and a light chain variable region of SEQ ID NO: 173; 14) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 15) a heavy chain variable region of SEQ ID NO: 149 and a light chain variable region of SEQ ID NO: 175; 16) a heavy chain variable region of SEQ ID NO: 150 and a light chain variable region of SEQ ID NO: 176; 17) a heavy chain variable region of SEQ ID NO: 151 and a light chain variable region of SEQ ID NO: 177; 18) the heavy chain variable region of SEQ ID NO: 152 and the light chain variable region of SEQ ID NO: 178; 19) The heavy chain variable region of SEQ ID NO: 153 and the light chain variable region of SEQ ID NO: 179; 20) a heavy chain variable region of SEQ ID NO: 154 and a light chain variable region of SEQ ID NO: 180; 21) The heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 181; 22) a heavy chain variable region of SEQ ID NO: 156 and a light chain variable region of SEQ ID NO: 182; 23) the heavy chain variable region of SEQ ID NO: 157 and the light chain variable region of SEQ ID NO: 183; 24) the heavy chain variable region of SEQ ID NO: 155 and the light chain variable region of SEQ ID NO: 184; 25) the heavy chain variable region of SEQ ID NO: 158 and the light chain variable region of SEQ ID NO: 185; 26) the heavy chain variable region of SEQ ID NO: 159 and the light chain variable region of SEQ ID NO: 186; 27) The heavy chain variable region of SEQ ID NO: 160 and the light chain variable region of SEQ ID NO: 187 28) the heavy chain variable region of SEQ ID NO: 256 and the light chain variable region of SEQ ID NO: 258; 29) The heavy chain variable region of SEQ ID NO: 257 and the light chain variable region of SEQ ID NO: 259; 30) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 31) The heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 32) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 33) the heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 34) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 35) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 36) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 37) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 38) The heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 39) The heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 40) the heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 41) The heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 42) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 43) the heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 44) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 45) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 46) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 47) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 48) The heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 49) The heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 50) the heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 51) The heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 52) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 53) the heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 54) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 55) The heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 56) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 57) The method of any one of claims 149 to 173, comprising a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO:

811.

175. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

175. The method of any one of claims 149-174, wherein the antibody is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, F847C.21H6, or a binding fragment thereof.

176. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C.

176. The method of any one of claims 149-175, wherein the antibody is selected from the group consisting of F847C.10B9, F847C.11B1, F847C.12F12, F847C.26F5, F847C.4B10, F849C.8D10, F849C.8H3, 846.2B11, 846.4D5, 846T.4E11, 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

177. The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of TB001, TB006, 19B5.2E6, 14H10.2C9, 15F10.2D6, 20H5.A3, 23H9.2E4, 2D10.2B2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.2H3, F846TC.14E4, F846TC.16B5, F846TC.7F10, F849C.8D10, 846.4D5, and 846T.

177. The method of any one of claims 149 to 176, wherein the antibody is selected from the group consisting of 847.11D6, 847.20H7, 847.21B11, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F2, or a binding fragment thereof.

178. The method of any one of claims 149-177, wherein the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with an antibody selected from 846.4D5, 15F10.2D6, F846C.1B2, and F846C.1H12.

179. The method of any one of claims 149 to 178, wherein the anti-Gal3 antibody or binding fragment thereof competes with antibodies belonging to bins 3, 8, 17 or 24 for binding to Gal3.

180. 1. A method for disrupting the interaction of galectin-3 (Gal3) with transforming growth factor beta (TGF-b) receptor, comprising: contacting the interaction of Gal3 with the TGF-b receptor with an antibody or binding fragment thereof that selectively binds to Gal3 and disrupts the interaction of Gal3 with the TGF-b receptor. method.

181. 181. The method of claim 180, wherein Gal3 is expressed by the cell.

182. 181. The method of claim 180, wherein the Gal3 is secreted by the cell.

183. 183. The method of any one of claims 180 to 182, wherein the TGF-b receptor is expressed by a cell.

184. 1. A method of treating fibrosis in a subject in need thereof, comprising: administering to the subject an antibody or binding fragment thereof that selectively binds to Gal3 and interferes with the interaction of Gal3 with a TGF-β receptor, thereby treating fibrosis in the subject. method.

185. 185. The method of claim 184, wherein the fibrosis is liver fibrosis, kidney fibrosis, cardiac fibrosis, arterial fibrosis, venous thrombosis, or pulmonary fibrosis.

186. 1. A method of treating non-alcoholic fatty liver disease (NAFLD) or non-alcoholic steatohepatitis (NASH) in a subject in need thereof, comprising: administering to the subject an antibody or binding fragment thereof that selectively binds to Gal3 and interferes with the interaction of Gal3 with a TGF-β receptor, thereby treating NAFLD or NASH in the subject. method.

187. 1. A method of treating an immune-related disorder in a subject in need thereof, comprising: administering to the subject an antibody or binding fragment thereof that selectively binds to Gal3 and interferes with the interaction of Gal3 with a TGF-β receptor, thereby treating the immune-related disorder in the subject. method.

188. 188. The method of claim 187, wherein the immune-related disorder is sepsis, atopic dermatitis, or psoriasis.

189. 188. The method of claim 187, wherein the immune-related disorder is cancer.

190. 190. The method of claim 189, wherein the antibody or binding fragment is administered as a supplement to PD1 / PDL1 blocking therapy and / or CTLA4 blocking therapy.

191. 191. The method of claim 190, wherein the PD1 / PDL1 blockade therapy comprises pembrolizumab, nivolumab, cemiplimab, spartalizumab, camrelizumab, sintilimab, tislelizumab, toripalimab, AMP-224, AMP-514, atezolizumab, avelumab, durvalumab, KN035, CK-301, AUNP12, CA-170, and / or BMS-986189.

192. 191. The method of claim 190, wherein the CTLA4 blocking therapy comprises ipilimumab and / or tremelimumab.

193. 193. The method of any one of claims 184 to 192, wherein the antibody or binding fragment thereof is formulated for systemic administration.

194. 194. The method of any one of claims 184 to 193, wherein the antibody or binding fragment thereof is formulated for parenteral administration.

195. The method of any one of claims 184 to 194, wherein the subject is a mammal.

196. 196. The method of claim 195, wherein the mammal is a human.

197. 197. The method of any one of claims 180 to 196, wherein the TGF-b receptor is TGF-b receptor 1, TGF-b receptor 2, or TGF-b receptor 3.

198. 1. A method for disrupting the interaction of Gal3 with a tumor cell surface marker, comprising: contacting the tumor cell surface marker with an anti-Gal3 antibody or binding fragment thereof specific for the N-terminal domain of Gal3, the N-terminus of Gal3, or the TRD of Gal3; the tumor cell surface marker is selected from the group consisting of VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR (cMet), TNF sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, and FGFR4; method.

199. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

200. The method of claim 198, wherein the antibody is selected from the group consisting of: 847.8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, 847C.21H6, or a binding fragment thereof.

200. The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of 6H6.2D6, 20H5.A3, 20D11.2C6, 4G2.2G6, 13H12.2F8, 19B5.2E6, 15G7.2A7, 23H9.2E4, 19D9.2E5, 2D10.2B2, 4A11.2B5, 14H10.2C9, 3B11.2G2, 13A12.2E5, 7D8.2D8, 15F10.2D6, 23B10.2B12, 12G5.D7, 24D12.2H9, 6B3.2D3, 13G4.2F8, 9H2.2H10, 846.1F5, 846.2H3, 846T.

200. The method of claim 189 or 199, wherein the antibody is selected from the group consisting of: 4A11.H3L1, 4A11.H1L1, and 4A11.H4L2, or a binding fragment thereof.

201. The method of any one of claims 189 to 200, wherein the anti-Gal3 antibody or binding fragment thereof is 2D10.2B2 or 6H6.2D6, or a binding fragment thereof.

202. 1. A method of treating cancer in a subject in need thereof, comprising: administering to the subject an anti-Gal3 antibody or binding fragment thereof specific for the N-terminal domain of Gal3, the N-terminus of Gal3, or the TRD of Gal3; the anti-Gal3 antibody or binding fragment thereof disrupts the interaction of Gal3 with the tumor cell surface marker; and the tumor cell surface marker is selected from the group consisting of VEGFR1, VEGFR2, VEGFR3, EGFR, PDGFRa, PDGFRb, ErbB2, HGFR (cMet), TNF sRI, CTLA4, CD47, PD-L1, FGFR1 alpha-IIIb, FGFR1 alpha-IIIc, FGFR2 alpha-IIIc, FGFR3 IIIc, and FGFR4; method.

203. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

203. The method of claim 202, wherein the antibody is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, 847C.21H6, or a binding fragment thereof.

204. The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of 6H6.2D6, 20H5.A3, 20D11.2C6, 4G2.2G6, 13H12.2F8, 19B5.2E6, 15G7.2A7, 23H9.2E4, 19D9.2E5, 2D10.2B2, 4A11.2B5, 14H10.2C9, 3B11.2G2, 13A12.2E5, 7D8.2D8, 15F10.2D6, 23B10.2B12, 12G5.D7, 24D12.2H9, 6B3.2D3, 13G4.2F8, 9H2.2H10, 846.1F5, 846.2H3, 846T.

204. The method of claim 202 or 203, wherein the antibody is selected from the group consisting of: 4A11.H3L1, 4A11.H1L1, and 4A11.H4L2, or a binding fragment thereof.

205. The method of any one of claims 202 to 204, wherein the anti-Gal3 antibody or binding fragment thereof is 2D10.2B2 or 6H6.2D6, or a binding fragment thereof.

206. 206. The method of any one of claims 202-205, wherein the cancer is brain cancer, breast cancer, colorectal cancer, kidney cancer, liver cancer, lung cancer, pancreatic cancer, bladder cancer, gastric cancer, or hematological malignancies.

207. The method of any one of claims 202 to 206, further comprising administering a standard of care treatment, wherein the anti-Gal3 antibody or binding fragment thereof is used as a supplement to the standard of care treatment.

208. 208. The method of claim 207, wherein the standard of care treatment comprises surgery, radiation, chemotherapy, targeted therapy, immunotherapy, PD1 / PDL1 blockade therapy, CTLA4 blockade therapy, temozolomide, or any combination thereof.

209. The method of any one of claims 180 to 208, wherein the antibody or binding fragment thereof binds to the N-terminal domain of Gal3.

210. the antibody or binding fragment thereof (a) Peptide 1 (ADNFSLHDALSGSGNPNPQG; SEQ ID NO: 3); (b) peptide 4 (GAGGYPGASYPGAYPGQAPP; SEQ ID NO: 6); (c) peptide 6 (GAYPGQAPPGAYPGAPGAYP; SEQ ID NO: 8); (d) peptide 7 (AYPGAPGAYPGAPAPGVYPG; SEQ ID NO: 9), or a combination thereof.

211. 211. The method of any one of claims 180 to 210, wherein the antibody or binding fragment thereof binds to an epitope of Gal3 comprising the amino acid sequence GxYPG, where X is alanine, glycine, or valine.

212. 212. The method of any one of claims 180 to 211, wherein the interaction is reduced to less than 80%, less than 75%, less than 70%, less than 65%, less than 60%, less than 55%, less than 50%, less than 45%, less than 40%, less than 35%, less than 30%, less than 25%, less than 20%, less than 15%, less than 10%, less than 5%, or less than 1% of the interaction in the absence of the antibody or binding fragment thereof.

213. 213. The method of any one of claims 180-212, wherein the antibody or binding fragment thereof binds to Gal3 with a dissociation constant (KD) of less than 1 nM, less than 1.2 nM, less than 2 nM, less than 5 nM, less than 10 nM, less than 13.5 nM, less than 15 nM, less than 20 nM, less than 25 nM, or less than 30 nM.

214. The antibody or binding fragment comprises: (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ - a heavy chain variable region comprising CDR3; and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ - a light chain variable region comprising CDR3, The V Ｈ - CDR1 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 27-36, 397-399, 588-615; The V Ｈ - CDR2 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 45-54, 400-406, 616-643; The V Ｈ - CDR3 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 61-69, 71, 408-416, 644-671; The V Ｌ - CDR1 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 82-92, 417-426, 672-699; The V Ｌ - CDR2 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 102-111, 427-428, 700-727; and The V Ｌ 214. The method of any one of claims 180 to 213, wherein CDR3 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 117-127, 429-434, 728-755.

215. the antibody or binding fragment: 1) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 436 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 451 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 438 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 453 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 439 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 440 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 454 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 441 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 455 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 442 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 456 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 443 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 457 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 444 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 458 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 445 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 459 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 446 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 460 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 447 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 461 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 448 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 462 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 449 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 463 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 450 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 464 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 28) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 43) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 44) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 45) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 46) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 47) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 48) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 49) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 50) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 51) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 52) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 53) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 54) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 55) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -CDR3 The method of any one of claims 180 to 214, comprising:

216. the antibody or binding fragment: 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; 6) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 7) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 8) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 9) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 10) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 11) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; 12) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; 13) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 14) a heavy chain variable region of SEQ ID NO: 436 and a light chain variable region of SEQ ID NO: 451; 15) the heavy chain variable region of SEQ ID NO: 438 and the light chain variable region of SEQ ID NO: 453; 16) a heavy chain variable region of SEQ ID NO: 439 and a light chain variable region of SEQ ID NO: 162; 17) a heavy chain variable region of SEQ ID NO: 440 and a light chain variable region of SEQ ID NO: 454; 18) the heavy chain variable region of SEQ ID NO: 441 and the light chain variable region of SEQ ID NO: 455; 19) the heavy chain variable region of SEQ ID NO: 442 and the light chain variable region of SEQ ID NO: 456; 20) the heavy chain variable region of SEQ ID NO: 443 and the light chain variable region of SEQ ID NO: 457; 21) the heavy chain variable region of SEQ ID NO: 444 and the light chain variable region of SEQ ID NO: 458; 22) the heavy chain variable region of SEQ ID NO: 445 and the light chain variable region of SEQ ID NO: 459; 23) the heavy chain variable region of SEQ ID NO: 446 and the light chain variable region of SEQ ID NO: 460; 24) the heavy chain variable region of SEQ ID NO: 447 and the light chain variable region of SEQ ID NO: 461; 25) the heavy chain variable region of SEQ ID NO: 448 and the light chain variable region of SEQ ID NO: 462; 26) the heavy chain variable region of SEQ ID NO: 449 and the light chain variable region of SEQ ID NO: 463; 27) the heavy chain variable region of SEQ ID NO: 450 and the light chain variable region of SEQ ID NO: 464; 28) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 29) the heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 30) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 31) The heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 32) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 33) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 34) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 35) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 36) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 37) The heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 38) The heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 39) The heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 40) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 41) The heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 42) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 43) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 44) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 45) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 46) the heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 47) the heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 48) The heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 49) the heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 50) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 51) The heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 52) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 53) the heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 54) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 55) The method of any one of claims 180 to 215, comprising a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO:

811.

217. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

217. The method of any one of claims 180-216, wherein the antibody is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, 847C.21H6, or a binding fragment thereof.

218. The antibody or binding fragment may be selected from the group consisting of 13H12.2F8, 19D9.2E5, 14H10.2C9, 2D10.2B2, 4A11.2B5, 6H6.2D6, 20H5.A3, 19B5.2E6, 23H9.2E4, 20D11.2C6, 15G7.2A7, 4G2.2G6, 3B11.2G2, 13A12.2E5, 7D8.2D8, 15F10.2D6, 12G5.D7, 24D12.2H9, 13G4.2F8, 9H2.2H10, 23B10.2B12, 6B3.2D3, 846.1F5, 846.2H3, 846T.

218. The method of any one of claims 180 to 217, wherein the antibody is selected from the group consisting of: 4A11.H3L1, 4A11.H1L1, and 4A11.H4L2, or a binding fragment thereof.

219. The method of any one of claims 180 to 218, wherein the antibody or binding fragment thereof comprises a humanized antibody or binding fragment.

220. 220. The method of any one of claims 180 to 219, wherein the antibody or binding fragment thereof comprises a full-length antibody or binding fragment thereof.

221. 221. The method of any one of claims 180 to 220, wherein the antibody or binding fragment thereof comprises a bispecific antibody or binding fragment thereof.

222. 222. The method of any one of claims 180 to 221, wherein the antibody or binding fragment thereof comprises a monovalent Fab', a bivalent Fab2, a single chain variable fragment (scFv), a diabody, a minibody, a nanobody, a single domain antibody (sdAb), or a camelid antibody, or a binding fragment thereof.

223. The method of any one of claims 180 to 222, wherein the antibody or binding fragment thereof comprises an IgG framework.

224. 224. The method of any one of claims 180-223, wherein the antibody or binding fragment thereof comprises an IgG1, IgG2, or IgG4 framework.

225. (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ - a heavy chain variable region comprising CDR3; and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ an anti-Gal3 antibody or a binding fragment thereof comprising a light chain variable region comprising CDR3, The V Ｈ - CDR1 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 27-36, 397-399; The V Ｈ - CDR2 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 45-54, 400-406, The V Ｈ - CDR3 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 61-69, 71, 408-416, The V Ｌ - CDR1 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 82-92, 417-426, The V Ｌ - CDR2 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 102-111, 427-428, and The V Ｌ - CDR3 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 117-127, 429-434; An anti-Gal3 antibody or a binding fragment thereof.

226. a) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; b) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; c) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; d) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; e) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; f) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; g) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; h) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; i) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; j) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; k) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; l) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; m) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; n) V in SEQ ID NO: 436 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 451 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; o) V in SEQ ID NO: 438 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 453 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; p) V in SEQ ID NO: 439 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; q) V in SEQ ID NO: 440 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 454 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; r) V in SEQ ID NO: 441 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 455 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; s) V in SEQ ID NO: 442 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 456 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; t) V in SEQ ID NO: 443 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 457 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; u) V in SEQ ID NO: 444 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 458 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; v) V in SEQ ID NO: 445 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 459 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; w) V in SEQ ID NO: 446 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 460 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; x) V in SEQ ID NO: 447 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 461 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; y) V in SEQ ID NO: 448 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 462 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; z) V in SEQ ID NO: 449 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V of CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 463 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V of CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or aa) V in SEQ ID NO: 450 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 464 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - The anti-Gal3 antibody or binding fragment thereof according to claim 225, comprising CDR3.

227. a) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; b) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; c) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; d) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; e) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; f) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; g) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; h) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; i) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; j) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; k) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; l) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; m) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; n) a heavy chain variable region of SEQ ID NO: 436 and a light chain variable region of SEQ ID NO: 451; o) a heavy chain variable region of SEQ ID NO: 438 and a light chain variable region of SEQ ID NO: 453; p) a heavy chain variable region of SEQ ID NO: 439 and a light chain variable region of SEQ ID NO: 162; q) a heavy chain variable region of SEQ ID NO: 440 and a light chain variable region of SEQ ID NO: 454; r) a heavy chain variable region of SEQ ID NO: 441 and a light chain variable region of SEQ ID NO: 455; s) a heavy chain variable region of SEQ ID NO: 442 and a light chain variable region of SEQ ID NO: 456; t) a heavy chain variable region of SEQ ID NO: 443 and a light chain variable region of SEQ ID NO: 457; u) a heavy chain variable region of SEQ ID NO: 444 and a light chain variable region of SEQ ID NO: 458; v) a heavy chain variable region of SEQ ID NO: 445 and a light chain variable region of SEQ ID NO: 459; w) a heavy chain variable region of SEQ ID NO: 446 and a light chain variable region of SEQ ID NO: 460; x) a heavy chain variable region of SEQ ID NO: 447 and a light chain variable region of SEQ ID NO: 461; y) a heavy chain variable region of SEQ ID NO: 448 and a light chain variable region of SEQ ID NO: 462; z) a heavy chain variable region of SEQ ID NO: 449 and a light chain variable region of SEQ ID NO: 463; or aa) An anti-Gal3 antibody or binding fragment thereof according to claim 225 or 226, comprising a heavy chain variable region of SEQ ID NO: 450 and a light chain variable region of SEQ ID NO:

464.

228. 6H6.2D6, 20H5. A3, 20D11.2C6, 4G2.2G6, 13H12.2F8, 19B5.2E6, 15G7.2A7, 23H9.2E4, 19D9.2E5, 2D10.2B 2, 4A11.2B5, 14H10.2C9, 3B11.2G2, 13A12.2E5, 7D8.2D8, 15F10.2D6, 23B10.2B12, 12G5. D7, 24D12.2H9, 6B3.2D3, 13G4.2F8, 9H2.2H10, 846.1F5, 846.2H3, 846T. 1H2, IMT-001, 4A11. The anti-Gal3 antibody or binding fragment thereof of any one of claims 225 to 227, which is selected from the group consisting of 4A11.H1L1, 4A11.H1L1, and 4A11.H4L2, or binding fragments thereof.

229. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 228, which does not bind to the C-terminus of Gal3.

230. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 229, which does not bind to the C-terminal domain of Gal3.

231. An anti-Gal3 antibody or binding fragment thereof according to any one of claims 225 to 230, which does not bind to the C-terminal carbohydrate recognition binding domain.

232. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 231, which does not bind to amino acids 112 to 250 of Gal3 or a subregion thereof.

233. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 232, which binds to the N-terminus of Gal3.

234. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 233, which binds to the N-terminal domain of Gal3.

235. The anti-Gal3 antibody or binding fragment thereof according to any one of claims 225 to 234, which binds to amino acids 1 to 111 of Gal3 or a subregion thereof.

236. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 235, which binds to the tandem repeat domain of Gal3.

237. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 236, which binds to peptide 1 (ADNFSLHDALSGSGNPNPQG; SEQ ID NO: 3).

238. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 237, which binds to peptide 6 (GAYPGQAPPGAYPGAPGAYP; SEQ ID NO: 8).

239. An anti-Gal3 antibody or a binding fragment thereof according to any one of claims 225 to 238, which binds to peptide 7 (AYPGAPGAYPGAPAPGVYPG; SEQ ID NO: 9).

240. 240. An anti-Gal3 antibody or binding fragment thereof according to any one of claims 225 to 239, which is 2D10.2B2 or 6H6.2D6, or a binding fragment thereof.

241. 241. The anti-Gal3 antibody or binding fragment thereof of any one of claims 225 to 240, selected from the group consisting of 2D10.2B2 or 6H6.2D6, or binding fragments thereof.

242. The anti-Gal3 antibody or binding fragment thereof of any one of claims 225 to 241, which inhibits tumor cell growth in vitro.

243. The anti-Gal3 antibody or binding fragment thereof according to any one of claims 225 to 242, which slows brain tumor growth.

244. A pharmaceutical composition comprising the anti-Gal3 antibody or binding fragment thereof of any one of claims 225 to 243 and at least one pharmaceutically acceptable carrier, excipient, diluent, or adjuvant.

245. An antibody that binds to human Gal3 and competes with an anti-Gal3 antibody or a binding fragment thereof for binding to human Gal3, The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T. 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, 847C.21H6, or a binding fragment thereof; antibody.

246. An antibody that binds to human Gal3 and competes with an anti-Gal3 antibody or a binding fragment thereof for binding to human Gal3, The anti-Gal3 antibody or binding fragment thereof may be selected from the group consisting of 6H6.2D6, 20H5.A3, 20D11.2C6, 4G2.2G6, 13H12.2F8, 19B5.2E6, 15G7.2A7, 23H9.2E4, 19D9.2E5, 2D10.2B2, 4A11.2B5, 14H10.2C9, 3B11.2G2, 13A12.2E5, 7D8.2D8, 15F10.2D6, 23B10.2B12, 12G5.D7, 24D12.2H9, 6B3.2D3, 13G4.2F8, 9H2.2H10, 846.1F5, 846.2H3, 846T. 1H2, IMT001, 4A11.H3L1, 4A11.H1L1, and 4A11.H4L2 or a binding fragment thereof; antibody.

247. 1. A method for identifying an antibody or binding fragment having the ability to interfere with the interaction of Gal3 with a TGF-β receptor, comprising: (a) contacting a Gal3 protein with an antibody or binding fragment that selectively binds to Gal3, thereby forming a Gal3-antibody complex; (b) contacting the Gal3-antibody complex with the TGF-β receptor protein; (c) removing unbound TGF-b receptor protein; and (d) detecting TGF-β receptor protein bound to the Gal3-antibody complex; the antibody or binding fragment has the ability to disrupt the interaction of Gal3 with the TGF-b receptor if the TGF-b receptor protein is not detected in (d); method.

248. The method of claim 247, comprising an immunoassay.

249. The method of claim 248, wherein the immunoassay is an enzyme-linked immunosorbent assay.

250. 250. The method of any one of claims 247 to 249, wherein the TGF-b receptor is TGF-b receptor 1, TGF-b receptor 2, or TGF-b receptor 3.

251. Use of an anti-Gal3 antibody or binding fragment in the manufacture of a medicament or composition for the treatment of fibrosis, liver fibrosis, non-alcoholic fatty liver disease (NAFLD), non-alcoholic steatohepatitis (NASH), renal fibrosis, cardiac fibrosis, arterial fibrosis, venous thrombosis, or pulmonary fibrosis.

252. Use of an anti-Gal3 antibody or binding fragment in the manufacture of a medicament or composition for the treatment of an immune-related disorder.

253. 253. The use of claim 252, wherein the immune-related disorder is sepsis, atopic dermatitis, or psoriasis.

254. 253. The use of claim 252, wherein the immune-related disorder is cancer.

255. The use of claim 254, wherein the medicament is used as a supplement to PD1 / PDL1 blocking therapy or CTLA4 blocking therapy.

256. 256. The use of claim 255, wherein the PD1 / PDL1 blockade therapy comprises pembrolizumab, nivolumab, cemiplimab, spartalizumab, camrelizumab, sintilimab, tislelizumab, toripalimab, AMP-224, AMP-514, atezolizumab, avelumab, durvalumab, KN035, CK-301, AUNP12, CA-170, and / or BMS-986189.

257. The use of claim 255, wherein the CTLA4 blocking therapy comprises ipilimumab and / or tremelimumab.

258. Use of an anti-Gal3 antibody or a binding fragment thereof for the treatment of fibrosis, liver fibrosis, NAFLD, NASH, kidney fibrosis, cardiac fibrosis, arterial fibrosis, venous thrombosis, or pulmonary fibrosis.

259. Use of an anti-Gal3 antibody or a binding fragment thereof for the treatment of cancer.

260. 260. The use of claim 259, wherein the cancer is brain cancer, breast cancer, colorectal cancer, kidney cancer, liver cancer, lung cancer, pancreatic cancer, bladder cancer, gastric cancer, or hematological malignancies.

261. Use of an anti-Gal3 antibody or binding fragment thereof for inhibiting tumor cell growth in vitro.

262. Use of an anti-Gal3 antibody or binding fragment thereof for retarding brain tumor growth.

263. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of: (1) V Ｈ - CDR1, V Ｈ - CDR2, and V Ｈ - a heavy chain variable region comprising CDR3; and (2) a V Ｌ - CDR1, V Ｌ - CDR2, and V Ｌ - a light chain variable region comprising CDR3, The V Ｈ - CDR1 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 27-36, 397-399, 588-615, The V Ｈ - CDR2 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 45-54, 400-406, 616-643, The V Ｈ - CDR3 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 61-69, 71, 408-416, 644-671; The V Ｌ - CDR1 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 82-92, 417-426, 672-699, The V Ｌ - CDR2 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 102-111, 427-428, 700-727, and The V Ｌ 263. The use according to any one of claims 252 to 262, wherein CDR3 comprises an amino acid sequence having at least 60%, at least 70%, at least 80%, at least 90%, or 100% sequence identity to any of the amino acid sequences set forth in SEQ ID NOs: 117-127, 429-434, 728-755.

264. the anti-Gal3 antibody or binding fragment is 1) V in SEQ ID NO: 136 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 161 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 2) V in SEQ ID NO: 137 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 3) V in SEQ ID NO: 138 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 163 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 4) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 164 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 5) V in SEQ ID NO: 139 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 171 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 6) V in SEQ ID NO: 140 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 165 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 7) V in SEQ ID NO: 141 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 166 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 8) V in SEQ ID NO: 142 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 167 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 9) V in SEQ ID NO: 143 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 168 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 10) V in SEQ ID NO: 144 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 169 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 11) V in SEQ ID NO: 145 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 170 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 12) V in SEQ ID NO: 146 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 172 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 13) V in SEQ ID NO: 148 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 174 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 14) V in SEQ ID NO: 436 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 451 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 15) V in SEQ ID NO: 438 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 453 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 16) V in SEQ ID NO: 439 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 162 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 17) V in SEQ ID NO: 440 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 454 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 18) V in SEQ ID NO: 441 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 455 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 19) V in SEQ ID NO: 442 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 456 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 20) V in SEQ ID NO: 443 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 457 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 21) V in SEQ ID NO: 444 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 458 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 22) V in SEQ ID NO: 445 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 459 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 23) V in SEQ ID NO: 446 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 460 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 24) V in SEQ ID NO: 447 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 461 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 25) V in SEQ ID NO: 448 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 462 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 26) V in SEQ ID NO: 449 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 463 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 27) V in SEQ ID NO: 450 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 464 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 28) V in SEQ ID NO: 756 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 784 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 29) V in SEQ ID NO: 757 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 785 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 30) V in SEQ ID NO: 758 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 786 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 31) V in SEQ ID NO: 759 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 787 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 32) V in SEQ ID NO: 760 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 788 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 33) V in SEQ ID NO: 761 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 789 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 34) V in SEQ ID NO: 762 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 790 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 35) V in SEQ ID NO: 763 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 791 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 36) V in SEQ ID NO: 764 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 792 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 37) V in SEQ ID NO: 765 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 793 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 38) V in SEQ ID NO: 766 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 794 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 39) V in SEQ ID NO: 767 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 795 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 40) V in SEQ ID NO: 768 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - V in CDR3 and SEQ ID NO: 796 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 41) V in SEQ ID NO: 769 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 797 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 42) V in SEQ ID NO: 770 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 798 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 43) V in SEQ ID NO: 771 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 799 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 44) V in SEQ ID NO: 772 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 800 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 45) V in SEQ ID NO: 773 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 801 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 46) V in SEQ ID NO: 774 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 802 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 47) V in SEQ ID NO: 775 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 803 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 48) V in SEQ ID NO: 776 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 804 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 49) V in SEQ ID NO: 777 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 805 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 50) V in SEQ ID NO: 778 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 806 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 51) V in SEQ ID NO: 779 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 807 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 52) V in SEQ ID NO: 780 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 808 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 53) V in SEQ ID NO: 781 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 809 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; 54) V in SEQ ID NO: 782 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 810 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - CDR3; or 55) V in SEQ ID NO: 783 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ -V in CDR3 Ｈ - CDR1, V Ｈ - CDR2, V Ｈ - CDR3 and V in SEQ ID NO: 811 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ -V in CDR3 Ｌ - CDR1, V Ｌ - CDR2, V Ｌ - Use according to any one of claims 252 to 263, comprising CDR3.

265. the antibody or binding fragment: 1) a heavy chain variable region of SEQ ID NO: 136 and a light chain variable region of SEQ ID NO: 161; 2) a heavy chain variable region of SEQ ID NO: 137 and a light chain variable region of SEQ ID NO: 162; 3) a heavy chain variable region of SEQ ID NO: 138 and a light chain variable region of SEQ ID NO: 163; 4) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 164; 5) a heavy chain variable region of SEQ ID NO: 139 and a light chain variable region of SEQ ID NO: 171; 6) a heavy chain variable region of SEQ ID NO: 140 and a light chain variable region of SEQ ID NO: 165; 7) a heavy chain variable region of SEQ ID NO: 141 and a light chain variable region of SEQ ID NO: 166; 8) a heavy chain variable region of SEQ ID NO: 142 and a light chain variable region of SEQ ID NO: 167; 9) a heavy chain variable region of SEQ ID NO: 143 and a light chain variable region of SEQ ID NO: 168; 10) a heavy chain variable region of SEQ ID NO: 144 and a light chain variable region of SEQ ID NO: 169; 11) a heavy chain variable region of SEQ ID NO: 145 and a light chain variable region of SEQ ID NO: 170; 12) a heavy chain variable region of SEQ ID NO: 146 and a light chain variable region of SEQ ID NO: 172; 13) a heavy chain variable region of SEQ ID NO: 148 and a light chain variable region of SEQ ID NO: 174; 14) a heavy chain variable region of SEQ ID NO: 436 and a light chain variable region of SEQ ID NO: 451; 15) the heavy chain variable region of SEQ ID NO: 438 and the light chain variable region of SEQ ID NO: 453; 16) a heavy chain variable region of SEQ ID NO: 439 and a light chain variable region of SEQ ID NO: 162; 17) a heavy chain variable region of SEQ ID NO: 440 and a light chain variable region of SEQ ID NO: 454; 18) the heavy chain variable region of SEQ ID NO: 441 and the light chain variable region of SEQ ID NO: 455; 19) the heavy chain variable region of SEQ ID NO: 442 and the light chain variable region of SEQ ID NO: 456; 20) the heavy chain variable region of SEQ ID NO: 443 and the light chain variable region of SEQ ID NO: 457; 21) the heavy chain variable region of SEQ ID NO: 444 and the light chain variable region of SEQ ID NO: 458; 22) the heavy chain variable region of SEQ ID NO: 445 and the light chain variable region of SEQ ID NO: 459; 23) the heavy chain variable region of SEQ ID NO: 446 and the light chain variable region of SEQ ID NO: 460; 24) the heavy chain variable region of SEQ ID NO: 447 and the light chain variable region of SEQ ID NO: 461; 25) the heavy chain variable region of SEQ ID NO: 448 and the light chain variable region of SEQ ID NO: 462; 26) the heavy chain variable region of SEQ ID NO: 449 and the light chain variable region of SEQ ID NO: 463; 27) the heavy chain variable region of SEQ ID NO: 450 and the light chain variable region of SEQ ID NO: 464; 28) the heavy chain variable region of SEQ ID NO: 756 and the light chain variable region of SEQ ID NO: 784; 29) the heavy chain variable region of SEQ ID NO: 757 and the light chain variable region of SEQ ID NO: 785; 30) the heavy chain variable region of SEQ ID NO: 758 and the light chain variable region of SEQ ID NO: 786; 31) The heavy chain variable region of SEQ ID NO: 759 and the light chain variable region of SEQ ID NO: 787; 32) the heavy chain variable region of SEQ ID NO: 760 and the light chain variable region of SEQ ID NO: 788; 33) the heavy chain variable region of SEQ ID NO: 761 and the light chain variable region of SEQ ID NO: 789; 34) the heavy chain variable region of SEQ ID NO: 762 and the light chain variable region of SEQ ID NO: 790; 35) the heavy chain variable region of SEQ ID NO: 763 and the light chain variable region of SEQ ID NO: 791; 36) the heavy chain variable region of SEQ ID NO: 764 and the light chain variable region of SEQ ID NO: 792; 37) The heavy chain variable region of SEQ ID NO: 765 and the light chain variable region of SEQ ID NO: 793; 38) The heavy chain variable region of SEQ ID NO: 766 and the light chain variable region of SEQ ID NO: 794; 39) The heavy chain variable region of SEQ ID NO: 767 and the light chain variable region of SEQ ID NO: 795; 40) the heavy chain variable region of SEQ ID NO: 768 and the light chain variable region of SEQ ID NO: 796; 41) The heavy chain variable region of SEQ ID NO: 769 and the light chain variable region of SEQ ID NO: 797; 42) the heavy chain variable region of SEQ ID NO: 770 and the light chain variable region of SEQ ID NO: 798; 43) the heavy chain variable region of SEQ ID NO: 771 and the light chain variable region of SEQ ID NO: 799; 44) the heavy chain variable region of SEQ ID NO: 772 and the light chain variable region of SEQ ID NO: 800; 45) the heavy chain variable region of SEQ ID NO: 773 and the light chain variable region of SEQ ID NO: 801; 46) the heavy chain variable region of SEQ ID NO: 774 and the light chain variable region of SEQ ID NO: 802; 47) the heavy chain variable region of SEQ ID NO: 775 and the light chain variable region of SEQ ID NO: 803; 48) The heavy chain variable region of SEQ ID NO: 776 and the light chain variable region of SEQ ID NO: 804; 49) the heavy chain variable region of SEQ ID NO: 777 and the light chain variable region of SEQ ID NO: 805; 50) the heavy chain variable region of SEQ ID NO: 778 and the light chain variable region of SEQ ID NO: 806; 51) The heavy chain variable region of SEQ ID NO: 779 and the light chain variable region of SEQ ID NO: 807; 52) the heavy chain variable region of SEQ ID NO: 780 and the light chain variable region of SEQ ID NO: 808; 53) the heavy chain variable region of SEQ ID NO: 781 and the light chain variable region of SEQ ID NO: 809; 54) the heavy chain variable region of SEQ ID NO: 782 and the light chain variable region of SEQ ID NO: 810; or 55) The use according to any one of claims 252 to 264, comprising a heavy chain variable region of SEQ ID NO: 783 and a light chain variable region of SEQ ID NO:

811.

266. The anti-Gal3 antibody or binding fragment thereof is selected from the group consisting of TB001, TB006, 12G5.D7, 13A12.2E5, 14H10.2C9, 15F10.2D6, 19B5.2E6, 20D11.2C6, 20H5.A3, 23H9.2E4, 2D10.2B2, 3B11.2G2, 7D8.2D8, F846C.1B2, F846C.1F5, F846C.1H12, F846C.1H5, F846C.2H3, F846TC.14A2, F846TC.14E4, F846TC.16B5, F846TC.7F10, and F847C. 10B9, F847C. 11B1, F847C. 12F12, F847C. 26F5, F847C. 4B10, F849C. 8D10, F849C. 8H3, 846.2B11, 846.4D5, 847.14H4, 846T. 1H2, mIMT001, 4A11.2B5, 4A11. H1L1, 4A11. H4L2, 4G2.2G6, 6B3.2D3, 6H6.2D6, 9H2.2H10, 13G4.2F8, 13H12.2F8, 15 G7.2A7, 19D9.2E5, 23B10.2B12, 24D12.2H9, 846.2D4, 846.2F11, 846T. 10B1, 846T. 2E3, 846T. 4C9, 846T. 4E11, 846T. 4F5, 846T.

266. The use of any one of claims 252 to 265, wherein the antibody is selected from the group consisting of: 8D1, 847.10C9, 847.11D6, 847.15D12, 847.15F9, 847.15H11, 847.20H7, 847.21B11, 847.27B9, 847.28D1, 847.2B8, 847.3B3, 849.1D2, 849.2D7, 849.2F12, 849.4B2, 849.4F12, 849.4F2, 849.5C2, 849.8D12, 847C.21H6, or a binding fragment thereof.

267. The anti-Gal3 antibody or binding fragment may be selected from the group consisting of 6H6.2D6, 20H5.A3, 20D11.2C6, 4G2.2G6, 13H12.2F8, 19B5.2E6, 15G7.2A7, 23H9.2E4, 19D9.2E5, 2D10.2B2, 4A11.2B5, 14H10.2C9, 3B11.2G2, 13A12.2E5, 7D8.2D8, 15F10.2D6, 23B10.2B12, 12G5.D7, 24D12.2H9, 6B3.2D3, 13G4.2F8, 9H2.2H10, 846.1F5, 846.2H3, 846T.

267. The use of any one of claims 252 to 266, wherein the antibody is selected from the group consisting of: 4A11.H3L1, 4A11.H1L1 and 4A11.H4L2, or a binding fragment thereof.

268. The use of any one of claims 252 to 267, wherein the anti-Gal3 antibody or binding fragment is 2D10.2B2 or 6H6.2D6, or a binding fragment thereof.

269. The use of any one of claims 252 to 268, wherein the anti-Gal3 antibody or binding fragment is selected from the group consisting of 2D10.2B2 and 6H6.2D6, or a binding fragment thereof.

270. The use of any one of claims 252 to 269, wherein the anti-Gal3 antibody or binding fragment is used as a supplement to standard therapeutic treatment.

271. The use of claim 270, wherein the standard of care treatment comprises surgery, radiation, chemotherapy, targeted therapy, immunotherapy, PD1 / PDL1 blockade therapy, CTLA4 blockade therapy, temozolomide, or any combination thereof.

272. An antibody or binding fragment thereof that binds to the N-terminal domain and / or TRD of Gal3.

273. An antibody or a binding fragment thereof that binds to an epitope present in a region of Gal3, The epitope is (a) Peptide 1 (ADNFSLHDALSGSGNPNPQG; SEQ ID NO: 3); (b) peptide 6 (GAYPGQAPPGAYPGAPGAYP; SEQ ID NO: 8); or (c) peptide 7 (AYPGAPGAYPGAPAPGVYPG; SEQ ID NO: 9); or any combination thereof, An antibody or a binding fragment thereof.

274. 274. The antibody or binding fragment thereof of claim 272 or 273, which is 2D10.2B2, 6H6.2D6, or a binding fragment thereof.

275. 274. The antibody or binding fragment thereof of claim 272 or 273, selected from the group consisting of 2D10.2B2 and 6H6.2D6, or binding fragments thereof.

276. 10. An anti-Gal3 antibody or binding fragment thereof according to any one of the preceding claims for use in assisting a payload to cross the blood-brain barrier of a subject.

277. The use of claim 276, wherein the subject has a neurological disorder.

278. A protein comprising one or more peptide sequences having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 18-27.

279. The protein of claim 278, which is an antibody or a binding fragment thereof.

280. a) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 18 Ｈ - CDR1 peptide sequence; b) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 19. Ｈ - CDR2 peptide sequence; c) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 20. Ｈ - CDR3 peptide sequence; d) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences in Figure 21. Ｌ - CDR1 peptide sequence; e) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences in Figure 22. Ｌ - CDR2 peptide sequence; f) V having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figure 23. Ｌ - CDR3 peptide sequence; g) a heavy chain variable region peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 24-1 through 24-5; h) a light chain variable region peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 25-1 through 25-5; i) a heavy chain peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 26-1 through 26-8; j) a light chain peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to one or more of the peptide sequences of Figures 27-1 through 27-4; or any combination thereof.

281. 281. The protein of any one of claims 278-280, comprising a peptide sequence having at least 80%, 85%, 90%, 95%, 99%, or 100% homology to a peptide sequence encoded by any one or more of the nucleic acid sequences of Figures 37-1 to 40-12.

282. The protein of any one of claims 278 to 281, which is an antibody or a binding fragment thereof that binds to Gal3.

283. Antibodies that bind to or block PGAPAPGVYP GPPSGPGAYP SSGQPSATGA.

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