Anti-cell adhesion molecule L1 (L1CAM) antibodies and their uses

Abstract

This description provides antibodies that bind specifically to L1CAM and compositions comprising these antibodies. It also provides methods for preventing or treating diseases or conditions involving tumors using anti-L1CAM antibodies.

Description

FIELD OF THE INVENTION The present disclosure provides antibodies that specifically bind to the L1 cell adhesion molecule (L1CAM), compositions comprising the antibodies, and a method of using the antibodies to prevent or treat diseases or conditions comprising a tumor ( for example, bile duct cancer, melanoma, pancreatic cancer, glioma, breast cancer, lymphoma, lung cancer, kidney cancer, prostate cancer, fibrosarcoma, colon adenocarcinoma, liver cancer, and / or ovarian cancer) in one subject. BACKGROUND OF THE INVENTION L1 cell adhesion molecule (L1CAM) is one of the immunoglobulin superfamily cell adhesion molecules (CAMs) that mediates adhesion between cells on the cell surface. It has a molecular weight of 200 to 220 kDa. L1CAM was first known as a protein that mediates neuron-neuron adhesion and is involved in neurite outgrowth and neuronal migration. Lee V. et al., Proc. nati. Acad. Sel.74:5021-5025 (1997); McGuire JC. et al., Cell. 15(2):357-365 (1978). L1CAM is predominantly expressed in the brain. Ref. 313908 normal human. In addition, L1CAM expression is found in some renal and hematopoietic cells, peripheral nerves, intestinal crypt cells, and ganglia, but is not found in other normal cells. Huszar M. et al., Human Pathology 37:1000-1008 (2006). An antibody that specifically binds to the L1CAM protein can be used for the diagnosis and prevention or treatment of diseases in which LIGAN is overexpressed (eg, cancer). Accordingly, there is a need to create antibodies that specifically bind to LIGAN and are capable of modulating LIGAN activity. BRIEF DESCRIPTION OF THE INVENTION One aspect of the present disclosure relates to an isolated antibody, or antigen-binding fragment thereof, that specifically binds to the same epitope of the L1 cell adhesion molecule (LIGAN) as a reference antibody comprising a variable region of heavy chain (VH) and a light chain variable region (VL), wherein: (a) the VH of the reference antibody comprises SEQ. ID NO.: 23 and the VL of the reference antibody comprises SEQ. ID NO.: 24, (b) the VH of the reference antibody comprises SEQ. ID NO. : 25 and the VL of the reference antibody comprises SEQ. ID NO.: 26, (c) the VH of the reference antibody comprises SEQ. ID NO.: 27 and the VL of the reference antibody comprises SEQ. ID NO.: 28, (d) the VH of the ΜΛ / / UUOO f ¿reference antibody comprises SEQ. ID NO.: 29 and the VL of the reference antibody comprises SEQ. ID NO.: 30, or (e) the VH of the reference antibody comprises SEQ. ID NO.: 31 and the VL of the reference antibody comprises SEQ. ID NO. :32. Also provided herein is the anti-LICAM antibody, or antigen-binding fragment thereof, wherein the antibody, or antigen-binding fragment thereof, comprises the VH complementarity determining region 1 (CDR1), CDR2 from VH and CDR3 from VH, and VL CDR1, VL CDR2 and VL CDR3, wherein at least one amino acid is in the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the antibody, or antigen-binding fragment thereof, is different from the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the mAb417 antibody, and wherein the VH CDR1 of the mAb417 antibody comprises RFGMH (SEQ. ID NO.: 2); the VH CDR2 of the antibody mAb417 comprises FISNDGSNKYYADSVKG (SEQ. ID NO.: 9); the VH CDR3 of antibody mAb417 comprises GRAYGSGSLFDP (SEQ. ID NO.: 10); VL CDR1 of antibody mAb417 comprises RASRTISIYVN (SEQ. ID NO.: 6); VL CDR2 of antibody mAb417 comprises AASNLHS (SEQ. ID NO.: 7); and the VL CDR3 of antibody mAb417 comprises QQSIGRGWT (SEQ ID NO: 11). The present disclosure further provides the isolated antibody, or antigen-binding fragment thereof, that cross-competes for binding to the L1CAM epitope with a reference antibody comprising a heavy chain (VH) variable region and a heavy chain (VH) variable region. light chain (VL), wherein: (a) the VH of the reference antibody comprises SEQ. ID NO.: 23 and the VL of the reference antibody comprises SEQ. ID NO.: 24, (b) the VH of the reference antibody comprises SEQ. ID NO.: 25 and the VL of the reference antibody comprises SEQ. ID NO.: 26, (c) the VH of the reference antibody comprises SEQ. ID NO.: 27 and the VL of the reference antibody comprises SEQ. ID NO.: 28, (d) the VH of the reference antibody comprises SEQ. ID NO.: 29 and the VL of the reference antibody comprises SEQ. ID NO.: 30, or (e) the VH of the reference antibody comprises SEQ. ID NO.: 31 and the VL of the reference antibody comprises SEQ. ID NO.: 32, wherein the antibody, or antigen-binding fragment thereof, comprises the VH complementarity determining region 1 (CDR1), VH CDR2 and VH CDR3, and VL CDR1, VL CDR2 and VL CDR3, wherein at least one amino acid in VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the antibody, or antigen binding fragment thereof , is different from the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of antibody mAb 417, and wherein the VH CDR1 of the ΜΛ / / UUOO l antibody mAb417 comprises RFGMH (SEQ. ID NO.: 2); the VH CDR2 of the antibody mAb417 comprises FISNDGSNKYYADSVKG (SEQ. ID NO.: 9); the VH CDR3 of antibody mAb417 comprises GRAYGSGSLFDP (SEQ. ID NO.: 10); VL CDR1 of antibody mAb417 comprises RASRTISIYVN (SEQ. ID NO.: 6); VL CDR2 of antibody mAb417 comprises AASNLHS (SEQ. ID NO.: 7); and the VH CDR3 of antibody mAb417 comprises QQSIGRGWT (SEQ. ID NO.: 11). In certain aspects, the at least one amino acid difference comprises (i) glutamine at residue 5 in CDR2 of VH; (ii) serine at residue 8 in the CDR1 of VL; and / or (iii) proline at residue 8 in the CDR3 of VL of the anti-LICAM antibody, or antigen binding fragment thereof. In certain aspects, the at least one amino acid difference comprises (i) alanine, glycine, phenylalanine, tyrosine, threonine, proline, and tryptophan at residues 3 to 9, respectively, in CDR3 of VL; (ii) alanine, glycine, phenylalanine, tyrosine, serine, proline, and tryptophan at residues 3 to 9, respectively, in CDR3 of VL or (iii) leucine, valine, or histidine, tryptophan, or phenylalanine, tyrosine, proline, and tryptophan at residues 4 to 9, respectively, in the CDR3 of VL of the anti-LICAM antibody, or antigen-binding fragment thereof. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises CDR3 ΜΛ / / UU JO 1 of VL of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 13, SEO. ID NO.: 15, SEO. ID NO.: 17, SEQ. ID NO.: 19 or SEQ. ID NO.: 21. In some aspects, the VH CDR1 of the anti-LICAM antibody comprises RFGMH (SEQ. ID NO.: 2). In some aspects, the VH CDR2 of the anti-LICAM antibody comprises FISNEGSNKYYADSVKG (SEQ. ID NO.: 10). In some aspects, the VH CDR3 of the anti-LICAM antibody comprises GRAYGSGSLFDP (SEQ ID NO: 4). In some aspects, the VL CDR1 of the anti-LICAM antibody comprises RASRTISSYVN (SEQ ID NO:12). In some aspects, the CDR2 of VL of the anti-LICAM antibody comprises AASNLHS (SEQ. ID NO.: 7). In some aspects, the CDR3 of VL of the anti-LICAM antibody comprises QQSIGRGPVT (SEQ. ID NO.: 13). In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, of the present disclosure comprises a heavy chain CDR1, CDR2, and CDR3 and a light chain CDR1, CDR2, and CDR3, wherein the heavy chain CDR1, CDR2, and CDR3 includes QQSIGRGPVT (SEQ. ID NO.:13), QQAGFYTPWT (SEQ. ID NO.:15), QQAGFYSPWT (SEQ. ID NO.:17), QQSLHFYPWT (SEQ. ID NO.:19), or QQSLVWYPWT (SEQ ID NO.:21). The present disclosure further provides the anti-LICAM antibody, or antigen-binding fragment thereof, described herein as having one or more characteristics ΜΛ / / UUOO l selected from the group consisting of: (a) shows improved productivity compared to the mAb417 antibody; (b) shows improved affinity as measured by equilibrium dissociation constant (Kd) compared to the mAb417 antibody; (c) shows an improved PI value compared to the mAb417 antibody; (d) shows improved affinity as measured by the association constant (K) compared to the mAb417 antibody; or (e) any combination of these. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein shows improved productivity compared to ΜΛ / / UU JO i with the mAb417 antibody, wherein the improved productivity is at least 55 mg / L, at least 56 mg / L, at least 57 mg / L, at least 58 mg / L, at least 59 mg / L, at least around mg / L, at least around mg / L, at least around mg / L, at least around mg / L, at least around mg / L, at least around mg / L , at least around mg / L, at least around mg / L, at least around mg / L, at least around mg / L, at least around mg / L, at least around mg / L, at least least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about 81 mg / L, at least about 82 mg / L, at least about 83 mg / L, at least about 84 mg / L, or at least about 85 mg / L, when expressed according to Example 3. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein shows improved affinity as measured by the equilibrium dissociation constant (Kd) compared to the mAb417 antibody, where the improved Kd is less than 2.6 X 10~10M, less than 2.5 X 10-10M, less than 2.0 X 10~10M, less than 1.5 X 10~10M, less than 1.0 X 10~10M, less than 9 X ΙΟ-11M, less less than 8 X ΙΟ-11M, less than 7 X ICu11M, less than 6 X ICC11M, less than 5 X ΙΟ-11M, less than 4 X 10-11M, less than 3 X ΙΟ-11M, less than 2 X ΙΟ-11M , less than 1 X 10-11M, less than 9 X 10~12M, less than 8 X 10~12M, less than 7 X ICC12M, less than 6 X 10~12M, less than 5 X 10-12M, less than 4 X 10“12M, less than 3 X 10-12M, less than 2 X 10~12M, less than 1 X 10~12M, less than 9 X 10~13M, or less than 8 X 10~13M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein shows improved affinity as measured by the association constant (K) compared to the mAb417 antibody, where the improved K is lower. to 5 X 10~10M, less than 4 X 10-10M, less than 3 X 10~10M, less than 2 X 10~10M, less than 1.0 X 10~10M, less than 9 X ΙΟ-11M, less than 8 X 10-11M, less than 7 X ΙΟ-11M, less than 6 X 10-11M, less than 5 X ΙΟ-11M, less than 4 X ΙΟ-11M, less than 3 X 10-11M, less than 2 X 10-11M, less than 1 X 10-11M, less than 9 X 10~12M, less than 8 X 10~12M, less than 7 X 10~12M, less than 6 X 10~12M, less than 5 X 10~12M, less than 4 X 10~12M, less than 3 X 10~12M, less than 2 X 10-12M, less than 1 X 10-12M, less than 9 X 10~13M, or less than 8 X 10~13M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein exhibits an improved PI value compared to the mAb417 antibody, wherein the improved PI value is less than 9.6, less than 9.5, less than 9.4, less than 9.3, less than 9.2, less than 9.1, less than 9.0, less than 8.9, less than 8.8, less than 8.7, less than 8.6, less than 8.5, less than 8.4, less than 8.3, less than 8.2, less than 8.1, less than 8.0, less than 7.9, less than 7.8, less than 7.7, or less than 7.6. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises a VH CDR1, CDR2 and CDR3 and a VL CDR1, CDR2 and CDR3; wherein VH CDR1, CDR2 and CDR3 comprise RFGMH (SEQ ID NO.: 2), FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) and GRAYGSGSLFDP (SEQ. ID NO.: 4), respectively; and wherein CDR1, CDR2 and CDR3 of VL comprise RASRTISSYVN VIA / / UU JO i (SEQ. ID NO.: 12), AASNLHS (SEO. ID NO.: 7) and QQSIGRGPVT (SEQ. ID NO.: 13), respectively. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein VH CDR1, CDR2 and CDR3 comprise RFGMH (SEQ ID NO: 2), FISNEGSNKYYADSVKG (SEQ ID NO: 10) and GRAYGSGSLFDP (SEQ ID NO: 4), respectively; and wherein the VL CDR1, CDR2 and CDR3 comprise RASRTISSYVN (SEQ ID NO.: 12), AASNLHS (SEQ ID NO.: 7) and QQAGFYSPWT (SEQ. ID NO.: 17), respectively. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein VH CDR1, CDR2 and CDR3 comprise RFGMH (SEQ ID NO: 2), FISNEGSNKYYADSVKG (SEQ ID NO: 10) and GRAYGSGSLFDP (SEQ ID NO: 4), respectively; and wherein the VL CDR1, CDR2 and CDR3 comprise RASRTISSYVN (SEQ ID NO.: 12), AASNLHS (SEQ ID NO.: 7) and QQAGFYTPWT (SEQ. ID NO.: 17), respectively. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein VH CDR1, CDR2 and CDR3 comprise RFGMH (SEQ ID NO.: 2), FISNEGSNKYYADSVKG (SEQ ID ΜΛ / / UUOO i NO.: 10) and GRAYGSGSLFDP (SEQ. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2 and CDR3 comprise RASRTISSYVN (SEQ ID NO.: 12), AASNLHS (SEQ ID NO.: 7) and QQSLHFYPWT (SEQ. ID NO.: 19), respectively. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein VH CDR1, CDR2 and CDR3 comprise RFGMH (SEQ ID NO.: 2), FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) and GRAYGSGSLFDP (SEQ. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2 and CDR3 comprise RASRTISSYVN (SEQ ID NO.: 12), AASNLHS (SEQ ID NO.: 7) and QQSLVWYPWT (SEQ. ID NO.: 19), respectively. In some aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEQ. ID NO.: 23). In other aspects, the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least at least 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ SIGRGPVTFG QGTKLEIK (SEQ. ID NO.: 24). In some aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEQ. ID NO.: 27). In other aspects, the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least at least 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ AGFYSPWTFG QGTKLEIK (SEQ. ID NO.: 28). In some aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEQ. ID NO.: 25). In some aspects, the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least at least 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence determined as DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ AGFYTPWTFG QGTKLEIK (SEO. ID NO.: 26). In other aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTLY LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEQ. ID NO.: 29). In some aspects, the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least at least 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ΜΛ / I / UUOO l¿ ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYC QQSLHFYPWT FG QGTKLEIK (SEQ. ID NO.: 30). In other aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEQ. ID NO.: 31). In some aspects, the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, described herein comprises an amino acid sequence that is at least at least 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the determined amino acid sequence as DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYC QQSLVWYPWT FG QGTKLEIK (SEQ. ID NO.: 32). In some aspects, the anti-LICAM antibody VH, or antigen-binding fragment thereof, described in the ΜΛ / / UUOO he present comprises SEC. ID NO.: 23 and the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 24. In other aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 25 and the VL of the anti-LICAM antibody, or antigen-binding fragment thereof comprises SEQ. ID NO.: 26. In some aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 27 and the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 28. In other aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 29 and the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 30. In some aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO. : 29 and the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 30. In other aspects, the VH of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 31 and the VL of the anti-LICAM antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 32. Also provided herein is the anti-LICAM antibody, or antigen-binding fragment thereof, described herein, comprising a heavy chain (HC) and a light chain (LC), wherein the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 38 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 39. In some aspects, the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO. : 40 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 41. In some aspects, the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 42 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 43. In some aspects, the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 44 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 45. In some aspects, the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 46 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 20. In some aspects, wherein the anti-LICAM antibody is selected from the group consisting of an IgG1, IgG2, IgG3, IgG4, a variant thereof, and any combination thereof. In some aspects, the anti-LICAM antibody is a chimeric antibody or a human antibody. In some In aspects, the anti-LICAM antibody comprises a Fab, a Fab', an F(ab')2, an Fv or a single chain Fv (scFv). Some aspects of the present disclosure refer to a nucleic acid encoding the anti-LICAM antibody, a vector comprising the nucleic acid, a host cell comprising the vector. In some aspects, the host cell is selected from the group consisting of an E. coli, Pseudomonas, Bacillus, Streptomyces, yeast, CHO, YB / 20, NSO, PER-C6, HEK-293T, NIH-3T3, HeLa cell. , BHK, Hep G2, SP2 / 0, Rl.l, B-W, L-M, COS 1, COS 7, BSC1, BSC40, BMT10, plant cell, insect cell, and a human cell in tissue culture. Some aspects of the present disclosure relate to an immunoconjugate comprising the anti-LICAM antibody, or antigen-binding fragment thereof, described herein, linked to an agent. Also provided herein is a bispecific or multispecific antibody comprising the anti-LICAM antibody, or antigen-binding fragment, and an antibody, or antigen-binding fragment thereof, that binds an antigen. Some aspects of the present description refer to a composition comprising the anti-LICAM antibody, the nucleic acid, the vector, the host cell, the immunoconjugate or the bispecific antibody or ΜΛ / / UUOO f ¿ multispecies described herein and a carrier. Also provided herein is a kit comprising the anti-LICAM antibody described herein and instructions for use. Aspects of the present disclosure relate to a method of producing an antibody that specifically binds to a human L1CAM protein, comprising culturing the host cell under suitable conditions and isolating the antibody. Also provided herein is a method of treating a disease or condition in a subject in need thereof, comprising administering to the subject the anti-LICAM antibody, nucleic acid, vector, host cell, immunoconjugate, or bispecific antibody or multispecific described herein. In some aspects, the disease or condition comprises a tumor. In some aspects, the tumor comprises bile duct cancer, melanoma, pancreatic cancer, glioma, breast cancer, lymphoma, lung cancer, kidney cancer, prostate cancer, fibrosarcoma, colon adenocarcinoma, liver cancer, or ovarian cancer. In another aspect, the anti-LICAM antibody, nucleic acid, vector, cell, immunoconjugate, bispecific or multispecific antibody suppresses tumor growth and / or improves infiltration. ΜΛ / / UU JO l of immune cells in the tumor. Some aspects of the present disclosure relate to the method comprising administering an additional therapeutic agent. In some aspects, the additional therapeutic agent comprises chemotherapy, immunotherapy, radiation therapy, or combinations thereof. In some aspects, the additional therapeutic agent is an immune checkpoint inhibitor. Other features and advantages of the present description will be apparent from the following detailed description and examples which should not be construed as limiting. The contents of all cited references, including scientific articles, journal articles, GenBank entries, patents, and patent applications cited throughout this application are incorporated herein by reference. BRIEF DESCRIPTION OF THE FIGURES Figures 1A-1D show the analysis of the antigen binding specificity of Ab417 variants to human LCAM1 in CHO-DG44 (Figure ΙΑ), NCI-H522 (Figure IB), SKOV3 (Figure 1C) and B16F1 (Figure 1C) cells. ID) by using flow cytometry. Figures 2A-2F show the quality of purified Ab417 (Figure 2A) and Ab417 variants: Ab612 (Figure 2B), Ab4H5 (Figure 2C), Ab2C2 (Figure 2D), Ab4H6 (Figure 2E) and Ab5D12 (Figure 2F) measured. by size exclusion high performance liquid chromatography (SEC-HPLC). Figures 3A-3D show the analysis of the tumor growth inhibitory effect of Ab417 variants. Figure 3A shows changes in tumor volume of the Choi-CK xenograft model after administration of Ab417 (10 mg / kg), Ab612 (10 mg / kg), control hFc (human Fe) antibody (3.3) mg / kg, and negative control (PBS) (*p < 0.05, significant difference from the isotype control group using Dunnett's t-test). Figure 3B shows changes in body weights of the Choi-CK xenograft model after administration of Ab417, Ab612, control hFc and negative control (PBS). Figure 3C shows the tumor weights of the Choi-CK xenograft model after administration of Ab417 (10 mg / kg), Ab612 (10 mg / kg), Ab612 (10 mg / kg), control hFc antibody (3.3) mg / kg, and negative control (vehicle). (*p < 0.01, significant difference from isotype control group using Dunnett's t-test). Figure 3D shows the images of tumors from each group of eight mice euthanized after the end of the experiment as described in Figure 3C. DETAILED DESCRIPTION OF THE DESCRIPTION Disclosed herein is an isolated antibody, or an antigen-binding fragment thereof, that binds ΜΛ / / UUOO l specifically to the same epitope of the L1 cell adhesion molecule (L1CAM) as the reference antibody; cross-competes for binding to an L1CAM epitope with a control antibody and exhibits one or more of the properties described herein; and / or prevent and / or treat diseases or conditions comprising a tumor. To facilitate understanding of the description described herein, various terms and phrases are defined. Additional definitions are set forth throughout the detailed description. I. Definitions Throughout the description, the term an or an entity refers to one or more of that entity; for example, an antibody is understood to represent one or more antibodies. As such, the terms one (or one), one or more, and at least one may be used interchangeably herein. Likewise, and / or, when used herein, should be considered as a specific description of each of the two elements or components specified with or without the other. Thus, the term and / or, as used in a phrase such as A and / or B, is herein intended to include A and B, A or B, A (alone) and B (alone). Also, the term and / or, as used in a phrase such as A, B, and / or C, is intended to encompass each of the following: A, B, and C; A, B or C; A or C; A or B; B. ΜΛ / / UU JO l ¿ or C; A and C; A and B; B and C; A (only) ; B (alone) ; and C (alone). It is understood that when aspects are described herein with the language that comprises, other analogous aspects described in terms of consists of and / or consists essentially of are also provided. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one skilled in the art to which the present description relates. For example, the Concise Dictionary of Biomedicine and Molecular Biology, Juo, Pei-Show, 2nd ed., 2002, CRC Press; The Dictionary of Cell and Molecular Biology, 3rd ed., 1999, Academic Press; and the Oxford Dictionary Of Biochemistry And Molecular Biology, Revised, 2000, Oxford University Press, provide the expert with a general dictionary of various of the terms used herein. Units, prefixes, and symbols are indicated in their accepted International System of Units (SI) form. Numeric ranges include the numbers that define the range. Unless otherwise indicated, amino acid sequences are written from left to right in amino to carboxy orientation. The titles provided herein are not limitations of the various aspects of the description, which may be taken with reference to the description as a whole. Therefore, the terms VIA / / UU JO i defined immediately below are more fully defined by reference to the description in its entirety. The term "around" is used herein to mean approximately, roughly, around, or in the regions of. When the term around is used in conjunction with a numerical interval, it modifies that interval by extending the limits above and below the stated numerical values. In general, the term around can shift a numeric value above and below the value set by a variant of, say, 10 percent plus or minus (greater or less). The term cell adhesion molecule L1 or L1C.AM refers to one of the integral membrane glycoproteins belonging to the cell adhesion molecules (CAM) of the immunoglobulin superfamily. The term L1CAM includes any variant or isoform of L1CAM that is naturally expressed by cells. Accordingly, the antibodies described herein may cross-react with different isoforms of the same species (eg, different isoforms of human L1CAM), or cross-react with L1CAM from species other than human (eg, L1CAM of mouse). Alternatively, the antibodies may be specific to human L1CAM and may not cross-react with other species. L1CAM, or any variant e ΜΛ / / UU JO i isoform thereof, can be isolated from cells or tissues that naturally express them or produced recombinantly using techniques known in the art and / or described herein. Human L1CAM (UniProt ID NO. P32004-1; SEQ. ID NO.: 1) is a type 1 integral membrane glycoprotein composed of 1257 amino acids and once spanning the cell membrane, and its amino-terminal fragment exists outside the cell membrane and its carboxyl-terminal fragment exists in the cytoplasm. The extracellular domain of L1CAM includes 11 domains of six immunoglobulin type 2 domains (Igl, Ig2, Ig3, Ig4, Ig5, and Ig6), five fibronectin III-type domains (Fnl, Fn2, Fn3, Fn4, and Fn5), and twenty binding sites. N-glycosylation. US Patent #9,777,060. At least two additional isoforms of human L1CAM have been identified. Isoform 2, (UniProt ID NO: P32004-2; SEQ ID NO: 3), consists of 1253 amino acids. Isoform 2 lacks amino acid residues 1177-1180 relative to the human L1CAM amino acid sequence. Isoform 3, (UniProt ID NO: P32004-3; SEQ ID NO: 5), consists of 1248 amino acids. Isoform 3 lacks amino acid residues 1177-1180 and has the following difference at amino acid residues 26-31 (YEGHHV L) from the human L1CAM amino acid sequence. ΜΛ / / UU JO i The amino acid sequences of the three known human L1CAM isotherms are shown below. (A) Human L1CAM (UniProt ID NO: P32004-1; SEQ ID NO: 1) MWALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLWFPTDDISLKC EASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASN KLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESWLPCNPPPSAEPLRIYWMNSKILHI KQDERVTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKP RLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLK VGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQP EVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYWQ LPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGI RDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDP SLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDWESRAQL LWGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGK VPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETWTPEAAPEKNPVDVKGEGNET TNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQ AVNS QGKGPE PQVTIGYS GE DYPQAIPE LE GIEILNS SAVLVKWRPVDLAQVKGHLRGYNV TYWREGSQRKHSKRHIHKDHWVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTF STPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRD PELRTHNLTDLSP HLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSV VSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKER MFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKD KEDTQVDSEARPMKDETFGEYRSLESDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVD VQFNEDGSFIGQYSGKKEKEAAGGNDSSGATSPINPAVALE (B) Isoforma 2 de L1CAM humana (UniProt ID ΜΛ / / UU JO l η.° Ρ32004-2; SEQ. ID NO.: 3) MWALRYVWPLLLCSPCLLIQIPEEYEGHHVMEPPVITEQSPRRLWFPTDDISLKC EASGKPEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASN KLGTAMSHEIRLMAEGAPKWPKETVKPVEVEEGESWLPCNPPPSAEPLRIYWMNSKILHI KQDERVTMGQNGNLYFANVLT SDNHS DYICHAHFPGTRT11QKE PIDLRVKATNSMIDRKP RLLFPTNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLK VGEEDDGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQP EVTWRINGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYWQ LPAKILTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGI RDLQANDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDP SLQPSITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDWESRAQL LWGSPGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGK VPGNQTSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETWTPEAAPEKNPVDVKGEGNET TNMVITWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLVVSNTSTFVPYEIKVQ AVNSQGKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNV TYWREGSQRKHSKRHIHKDHVWPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTF STPEGVPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRD PELRTHNLTDLSPHLRY RFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSV VSWVPKEGQCNFRFHILFKALGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKER MFRHQMAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKD KEDTQVDSEARPMKDETFGEYSDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFN E DGS FIGQYS GKKEKEAAGGNDS S GAT S PINPAVALE (C) Isoforma 3 de L1CAM humana (UniProt ID n.° P32004-3; SEQ. ID NO.: 5) VIA / / UU JO l MWALRYVWPLLLCSPCLLIQIPEELMEPPVITEQSPRRLWFPTDDISLKCEASGK PEVQFRWTRDGVHFKPKEELGVTVYQSPHSGSFTITGNNSNFAQRFQGIYRCFASNKLGTA MSHEIRLMAEGAPKWPKETVKPVEVEEGESVVLPCNPPPSAEPLRIYWMNSKILHIKQDER VTMGQNGNLYFANVLTSDNHSDYICHAHFPGTRTIIQKEPIDLRVKATNSMIDRKPRLLFP TNSSSHLVALQGQPLVLECIAEGFPTPTIKWLRPSGPMPADRVTYQNHNKTLQLLKVGEED DGEYRCLAENSLGSARHAYYVTVEAAPYWLHKPQSHLYGPGETARLDCQVQGRPQPEVTWR INGIPVEELAKDQKYRIQRGALILSNVQPSDTMVTQCEARNRHGLLLANAYIYWQLPAKI LTADNQTYMAVQGSTAYLLCKAFGAPVPSVQWLDEDGTTVLQDERFFPYANGTLGIRDLQA NDTGRYFCLAANDQNNVTIMANLKVKDATQITQGPRSTIEKKGSRVTFTCQASFDPSLQPS ITWRGDGRDLQELGDSDKYFIEDGRLVIHSLDYSDQGNYSCVASTELDWESRAQLLWGS PGPVPRLVLSDLHLLTQSQVRVSWSPAEDHNAPIEKYDIEFEDKEMAPEKWYSLGKVPGNQ TSTTLKLSPYVHYTFRVTAINKYGPGEPSPVSETWTPEAAPEKNPVDVKGEGNETTNMVI TWKPLRWMDWNAPQVQYRVQWRPQGTRGPWQEQIVSDPFLWSNTSTFVPYEIKVQAVNSQ GKGPEPQVTIGYSGEDYPQAIPELEGIEILNSSAVLVKWRPVDLAQVKGHLRGYNVTYWRE GSQRKHSKRHIHKDHWVPANTTSVILSGLRPYSSYHLEVQAFNGRGSGPASEFTFSTPEG VPGHPEALHLECQSNTSLLLRWQPPLSHNGVLTGYVLSYHPLDEGGKGQLSFNLRDPELRT HNLTDLSPHLRYRFQLQATTKEGPGEAIVREGGTMALSGISDFGNISATAGENYSWSWVP KEGQCNFRFHILFKA LGEEKGGASLSPQYVSYNQSSYTQWDLQPDTDYEIHLFKERMFRHQ MAVKTNGTGRVRLPPAGFATEGWFIGFVSAIILLLLVLLILCFIKRSKGGKYSVKDKEDTQ VDSEARPMKDETFGEYSDNEEKAFGSSQPSLNGDIKPLGSDDSLADYGGSVDVQFNEDGSF IGQEASGNDSPA SVATLEG G The human L1CAM signal sequence corresponds to amino acids 1-19 (underlined). Thus, the mature isotherms of human L1CAM isotherm 1, human L1CAM isotherm 2, and human L1CAM isotherm 3 consist of amino acids 20 to 1257, 1253, or 1248, respectively. ΜΛ / I / UUOO l¿ The terms antibody and antibodies are terms of the art and may be used interchangeably herein and refer to a molecule with an antigen binding site that specifically binds to an antigen. Terms as used herein include whole antibodies and any antigen-binding fragments (ie, antigen-binding fragments) or single chains thereof. An antibody refers, in one aspect, to a glycoprotein comprising at least two heavy (H) and two light (L) chains interconnected by disulfide bonds, or an antigen-binding fragment thereof. In another aspect, an antibody refers to a single chain antibody comprising a single variable domain, eg, VHH domain. Each heavy chain comprises a heavy chain variable region (abbreviated herein as VH) and a heavy chain constant region. In certain naturally occurring antibodies, the heavy chain constant region comprises three domains, CH1, CH2, and CH3. In certain naturally occurring antibodies, each light chain comprises a light chain variable region (abbreviated herein as VL) and a light chain constant region. The light chain constant region comprises one domain, CL. The VH and VL regions can also be subdivided into regions of hypervariability, called complementarity determining regions (CDRs), interspersed with regions that are more conserved, called framework regions (FRs). . Each VH and VL is composed of three CDRs and four FRs, arranged from the amino terminus to the carboxyl terminus in the following order: FR1, CDR1, FR2, CDR2, FR3, CDR3, and FR4. The variable regions of the heavy and light chains contain a binding domain that interacts with an antigen. The constant regions of antibodies can mediate the binding of immunoglobulin to host factors or tissues, including various cells of the immune system (eg, effector cells) and the first component (Clq) of the classical complement system. The term Kabat numbering and similar terms, which refer to a numbering system of amino acid residues in the heavy and light chain variable regions of an antibody, or an antigen-binding fragment thereof, are recognized in the art. In certain aspects, CDRs can be determined according to the Kabat numbering system (see, for example, Kabat EA & Wu TT (1971) Ann NY Acad Sel 190: 382-391 and Kabat EA et al., (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242). Using the Kabat numbering system, the CDRs within a heavy chain molecule of ΜΛ / I / UUOO (¿ antibodies are typically present at amino acid positions 31 to 35, which may optionally include one or two additional amino acids, after 35 (referred to in the Kabat numbering scheme as 35A and 35B) (CDR1) , amino acid positions 50 to 65 (CDR2) and amino acid positions 95 to 102 (CDR3) Using the Kabat numbering system, the CDRs within an antibody light chain molecule are typically present at amino acid positions 24 to 34 (CDR1), amino acid positions 50 to 56 (CDR2), and amino acid positions 89 to 97 (CDR3).In a specific aspect, the CDRs of the antibodies described herein have been determined according to the scheme of Kabat numbering. The phrases Kabat amino acid position numbering, Kabat position, and grammatical variants of this numbering system used for heavy chain variable domains or light chain variable domains of the antibody compilation in Kabat et al., Sequences of Proteins of Immunological Interest, 5th ed., Public Health Service, National Institutes of Health, Bethesda, Md. (1991). Use of this numbering system allows the actual linear amino acid sequence to contain fewer amino acids or additional amino acids corresponding to a reduction or insertion in a variable domain FR or CDR. For example, a heavy chain variable domain may include a single amino acid insertion (residue 52a, according to Kabat) after CDR2 residue 52 and the inserted residues (eg, residues 82a, 82b, and 82c, etc., according to Kabat) after residue 82 of heavy chain FW. See Table 1. Table 1 ΜΛ / / UUOO f ¿ Sudo Kabst AbM Otaria L24-L34 L344.B4 L24-L34 U I 13 W-L97 Hi (Nummciáni <te KoKw' H't íNsínwfseúbi 4« Chote) H2 H50-H5H HVAV W-HKd HíR-HAD Kabat residue numbering can be determined for a given antibody by aligning regions of homology of the antibody sequence with a standard Kabat numbering sequence. Chothia, instead, refers to the location of the structural loops (Chothia and Lesk, J. Mol. Biol. 196:901-917 (1987)). The end of the CDR-H1 loop according to Chothia, when numbered using the Kabat numbering convention, varies between H32 and H34 depending on the length of the loop (this is because the Kabat numbering scheme places inserts at H35A and H35B; if neither 35A nor 35B are present, the loop ends at 32; if only 35A is present, the loop ends at 33; if both 35A and 35B are present, the loop ends at 34). AbM hypervariable regions represent a midpoint between Kabat CDRs and Chothia structural loops and are used by Oxford Molecular's AbM antibody modeling software. IMGT (ImMunoGeneTics) also provides a numbering system for immunoglobulin variable regions, including CDRs. See, p. e.g., Lefranc, M.P. et al., Dev. Comp. Immunol. 27: 55-77 (2003), which is incorporated herein by this reference. The IMGT numbering system was based on an alignment of over 5000 sequences, structural data, and hypervariable loop characterization and allows easy comparison of variable regions and CDRs for all species. According to the IMGT numbering scheme, VH-CDR1 is found at positions 26 to 35, VH-CDR2 is found at positions 51 to 57, VH-CDR3 is found at positions 93 to 102, VL-CDR1 is is found at positions 27 to 32, VL-CDR2 is found at positions 50 to 52, and VL-CDR3 is found at positions 89 to 97. For all heavy chain constant region amino acid positions mentioned in the present description, the numbering is done according to the EU index first described in Edelman et al., 1969, Proc. nati. Acad. Sel. USA 63(1) :78-85, describing the amino acid sequence of the myeloma EU protein, which is the first human IgG1 sequencing. The EU index of Edelman et al. also reported in Kabat et al., 1991, Sequences of Proteins of Immunological Interest, 5th Edition, United States Public Health Service, National Institutes of Health, Bethesda. Therefore, the phrases index of EU as stated in Kabat or index of EU of Kabat and position ... according to index of EU as stated in Kabat and its grammatical variants refer to the residue numbering system based on in the human IgGl EU antibody of Edelman et al. as reported in Kabat 1991. The numbering system used for the variable domains (both heavy and light chain) and the amino acid sequence of the light chain constant region is that reported in Kabat 1991. Antibodies can be of any type (for example, IgG, IgE, IgM, IgD, IgA, or IgY), any class (for example, IgD, IgG2, IgG3, IgG4, IgAl, or IgA2), or any subclass (for example, IgG1, IgG2, IgG3, and IgG4 in humans; and IgG1, IgG2a, IgG2b, and IgG3 in mice) of the immunoglobulin molecule. Immunoglobulins, eg IgGl, exist in several allotypes, differing from each other by at most a few amino acids. An antibody described herein can be of any of the commonly known isotypes, classes, subclasses, or allotypes. in certain In respects, the antibodies described herein are of the IgG1, IgG2, IgG3 or IgG4 subclass or any hybrid of these. In certain aspects, the antibodies are of the human IgG1 subclass or of the human IgG2 or human IgG4 subclass. Antibody includes, by way of example, both naturally occurring and non-naturally occurring antibodies; monoclonal and polyclonal antibodies; chimeric and humanized antibodies; human and non-human antibodies; fully synthetic antibodies; single chain antibodies; monospecific antibodies; multispecies antibodies (including bispecies antibodies); tetrameric antibodies comprising two heavy chain and two light chain molecules; an antibody light chain monomer; an antibody heavy chain monomer; an antibody light chain dimer, an antibody heavy chain dimer; an antibody light chain-antibody heavy chain pair; intrabodies; heteroconjugate antibodies; monovalent antibodies; camelid antibodies; affybodies; anti-idiotypic (anti-Id) antibodies (including, eg, anti-anti-Id antibodies) and single domain antibodies (sdAbs), which include binding molecules consisting of a single monomeric variable antibody domain that are fully capable of binding antigen (eg, a VH domain or a VL domain). Harmen Μ. M. and Haard H. J. Appl Mícrobiol Bíotechnol. 77(1): 13-22 (2007)). The term "antigen-binding fragment" of an antibody, as used herein, refers to one or more fragments of an antibody that retain the ability to specifically bind an antigen (eg, human L1CAM). Such fragments are, for example, between about 8 and about 1500 amino acids in length, suitably between about 8 and about 745 amino acids in length, suitably between about 8 to about 300 amino acids in length, for example, about 8 to about 200 amino acids or about 10 to about 50 or 100 amino acids. It has been shown that the antigen-binding function of an antibody can be performed by fragments of a full-length antibody. Examples of binding fragments comprised within the term antigen-binding fragment of an antibody, eg, an anti-LICAM antibody described herein, include (i) a Fab fragment, a monovalent fragment consisting of the VL domains , VH, CL and CH1; (ii) an F(ab')2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge region; (iii) an Fd fragment consisting of the VH and CH1 domains; (iv) an Fv fragment consisting of the VL and VH domains of a single arm of an antibody, ΜΛ / / UUOO f¿ and disulfide-linked Fv (sdFv); (v) a dAb fragment (Ward et al., (1989) Nature 341:544-546), consisting of a VH domain; and (vi) an isolated complementarity determining region (CDR) or (vi) a combination of two or more isolated CDRs that can optionally be linked by a synthetic linker. Furthermore, although the two domains of the Fv fragment, VL and VH, are encoded by separate genes, they can be joined, using recombinant methods, through a synthetic linker that allows them to form a single protein chain in which the VL and VL regions VH join together to form monovalent molecules (known as single-chain Fv (scFv)); see, p. eg , Bird et al., (1988) Science 242:423-426; and Huston et al., (1988) Proc. nati. Acad. sci . USA 85:5879-5883). Single chain antibodies are also intended to be encompassed by the term antigen-binding fragment of an antibody. These antibody fragments are obtained using standard techniques known to those skilled in the art, and the fragments are examined for utility in the same manner as intact antibodies. Antigen-binding fragments can be produced by recombinant DNA techniques, or by enzymatic or chemical cleavage of intact immunoglobulins. As used herein, the terms variable region or variable domain are used interchangeably and are ΜΛ / / UU JO f ¿ common in the art. The variable region typically refers to a fragment of an antibody, generally a fragment of a light or heavy chain, typically about amino acids 110 to 120 amino acids from the amino terminus in the mature heavy chain and about 90 to 115 amino acids in the mature heavy chain. mature light chain, which differ widely in sequence between antibodies and are used in the binding and specificity of a particular antibody for its particular antigen. Sequence variability is concentrated in regions called complementarity determining regions (CDRs), while the more conserved regions in the variable domain are called framework regions (FRs). Without wishing to be bound by any particular theory or mechanism, it is believed that the CDRs of the heavy and light chains are primarily responsible for antibody-antigen interaction and specificity. In certain aspects, the variable region is a human variable region. In certain aspects, the variable region comprises murine or rodent CDRs and human framework regions (FRs). In particular aspects, the variable region is a primate (eg, non-human primate) variable region. In certain aspects, the variable region comprises murine or rodent CDRs and primate (eg, non-human primate) framework regions (FRs). As used herein, the term heavy chain, when used in reference to an antibody, can refer to any other type, eg, alpha (a), delta (δ), epsilon (s), gamma (γ) and mu (μ), based on the amino acid sequence of the constant domain, giving rise to the IgA, IgD, IgE, IgG, and IgM antibody classes, respectively, including IgG subclasses, eg, IgGl, IgG2, IgG3 and IgG4. As used herein, the term light chain, when used in reference to an antibody, can refer to any other type, eg, kappa (k) or lambda (A) based on the amino acid sequence of the constant domains. . Light chain amino acid sequences are known in the art. In specific aspects, the light chain is a human light chain. The terms VL and VL domain are used interchangeably to refer to the light chain variable region of an antibody. The terms VH and VH domain are used interchangeably to refer to the heavy chain variable region of an antibody. As used herein, the terms constant region and constant domain are interchangeable and have a common meaning in the art. The constant region is an antibody fragment, for example, a carboxyl-terminal fragment of a heavy and / or light chain that is not directly involved in the binding of an antibody to antigen but may have various effector functions, such as interaction with the Fe receptor. The constant region of an immunoglobulin molecule generally has a more conserved amino acid sequence than an immunoglobulin variable domain. An Fe region (fragment crystallizable region) or Fe or Fe domain refers to the C-terminal region of the heavy chain of an antibody that mediates the binding of immunoglobulin to host factors or tissues, including binding to Fe receptors. located on various cells of the immune system (eg, effector cells) or on the first component (Clq) of the classical complement system. Thus, an F region comprises the constant region of an antibody excluding the first constant region immunoglobulin domain (eg, CH1 or CL). In the IgG, IgA and IgD isotypes of antibodies, the Fe region comprises two identical protein fragments, derived from the second (CH2) and third (CH3) constant domains of the two heavy chains of the antibody; the IgM and IgE Fe regions comprise three heavy chain constant domains (CH 2-4 domains) in each polypeptide chain. For IgG, the Fe region comprises the immunoglobulin Cy2 and Cy3 domains and the hinge between Cyl and Cy2. TO ΜΛ / I / UU JO ( ¿ Although the boundaries of the Fe region of an immunoglobulin heavy chain may vary, the Fe region of human IgG heavy chain is generally defined to extend from an amino acid residue at position C226 or P230 (or amino acid between these two amino acid residues) to the carboxy terminus of the heavy chain, where numbering is according to the Kabat EU index The CH2 domain of a human IgG Fe region extends from around the amino acid 231 to around amino acid 340, while the CH3 domain is positioned on the C-terminal side of a CH2 domain in an Fe region, that is, it extends from around amino acid 341 to around amino acid 447 of an IgG. As used herein, the Fe region can be a naturally occurring sequence Fe, including any allotypic variants, or a variant Fe (eg, a non-naturally occurring Fe).Fe can also refer to this region in isolation or in combination. in the context of a Fe-comprising protein polypeptide, such as a binding protein comprising a Fe region, also called a Fe fusion protein (eg, an antibody or immunoadhesion). A native sequence Fe region or native sequence Fe region comprises an amino acid sequence that is identical to the amino acid sequence of a naturally occurring Fe region. Natural sequence human Fc regions include a human IgGl Fc region of ΜΛ / I / UU JO l ¿ natural sequence; a native sequence human IgG2 F region; a native sequence human IgG3 Fe region; and a naturally occurring sequence human IgG4 Fe region, as well as naturally occurring variants thereof. Wild-type Fe includes the various allotypes of Fe (see, for example, Jefferis et al., (2009) mAbs 1:1; Vidarsson G. et al. Front Immunol. 5:520 (published online Oct. 20). of 2014)). An Fe or FcR receptor is a receptor that binds to the Fe region of an immunoglobulin. FcRs that bind to an IgG antibody comprise receptors of the FcyR family, which include allelic variants and alternatively spliced ​​forms of these receptors. The FcyR family consists of three activating receptors (FcyRI, FcyRIII, and FcyRIV in mice; FcyRIA, FcyRIIA, and FcyRIIIIA in humans) and one inhibitory receptor (FcyRIIB). Human IgGl binds to most human Fe receptors and elicits the strongest Fe effector functions. It is considered equivalent to murine IgG2a with respect to the types of activating Fe receptors to which it binds. In contrast, human IgG4 elicits the lowest Fe effector functions. Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014). The constant region can be manipulated, for example, by recombinant technology, to remove one or more ΜΛ / / UU JO f ¿ effector functions. An effector function refers to the interaction of an Fe region of an antibody with an Fe ligand or receptor, or a biochemical event that results from it. Examples of effector functions include Clq binding, complement-dependent cytotoxicity (CDC), Fe receptor binding, FcyR-mediated effector functions such as ADCC, and antibody-dependent cell-mediated phagocytosis (ADCP). in English), and downregulation of a cell surface receptor (eg, the B cell receptor; BCR). In general, effector functions require the combination of the Fc region with a binding domain (eg, an antibody variable domain). Accordingly, the term a constant region without the Fe function includes constant regions without one or more, or reduced, effector functions mediated by the Fe region. The effector functions of an antibody can be reduced or prevented by different approaches. The effector functions of an antibody can be reduced or avoided by the use of antibody fragments without the Fc region (eg, as a Fab, F(ab')2, single-chain Fv (scFv), or an sdAb that consists of a monomeric VH or VL domain). Alternatively, so-called aglycosylated antibodies can be generated by removing sugars that are attached to particular residues in the ΜΛ / / UUOO l Fe region to reduce the effector functions of an antibody while retaining other valuable attributes of the Fe region (eg, long half-life and heterodimerization). Aglycosylated antibodies can be generated, for example, by removal or alteration of the residue to which the sugar is attached, removal of sugars enzymatically, production of the antibody in cells cultured in the presence of a glycosylation inhibitor, or expression of the glycosylation agent. antibody on cells incapable of glycosylating proteins (eg, bacterial host cells). See, for example, US Publication No. 20120100140. Another approach is to use F regions of an IgG subclass that have reduced effector function. For example, IgG2 and IgG4 antibodies are characterized by having lower levels of Fe effector functions than IgG1 and IgG3. The residues closest to the hinge region in the CH2 domain of the Fe part are responsible for the effector functions of antibodies, as it contains a largely overlapping binding site for Clq (complement) and IgG-Fc (FcyR) receptors. ) on effector cells of the innate immune system. Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014). Thus, antibodies with reduced effector functions or no Fe can be prepared by generating, for example, a chimeric Fe region comprising a CH2 domain from an IgG antibody of the IgG4 isotype and a CH3 domain from an IgG antibody of the IgG1 isotype, or a chimeric Fc region comprising the hinge region of IgG2 and the CH2 region of IgG4 (see, for example, Lau C. et al. J. Immunol. 191:4769-4777 (2013)), or an Fc region with mutations giving as a result impaired Fe effector functions, eg, reduced or absent Fe functions. Such Fe regions with mutations are known in the art. See, for example, US Publication No. 20120100140 and US and PCT applications cited therein and An et al., mAbs 1:6, 572-579 (2009); the disclosures of which are incorporated by reference in their entirety. An antibody hinge, hinge domain, hinge region, or hinge region are used interchangeably and refer to the domain of a heavy chain constant region that joins the CH1 domain to the CH2 domain and includes the top, middle, and bottom hinge fragments (Roux et al., J. Immunol. 1998 161:4083). The hinge provides varying levels of flexibility between the binding and effector regions of an antibody and also provides sites for intermolecular disulfide bonding between the two heavy chain constant regions. As used herein, a hinge begins at Glu216 and ends at Gly237 for all IgG isotypes (Roux et al., 1998 J Immunol 161:4083). The wild-type hinge sequences IgGl, IgG2, IgG3 and IgG4 are known in the art. See, for example, Kabat EA et al., (1991) Sequences of Proteins of Immunological Interest, fifth edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242; Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014). The term CH1 domain refers to the heavy chain constant region that joins the variable domain to the hinge in a heavy chain constant domain. As used herein, a CH1 domain begins at A118 and ends at V215. The term CH1 domain includes wild-type CH1 domains, as well as naturally occurring variants thereof (eg, allotypes). The CH1 domain sequences of IgG1, IgG2, IgG3 and IgG4 (including wild type and allotypes) are known in the art. See, for example, Kabat EA et al., (1991) mentioned above and Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014). Illustrative CH1 domains include CH1 domains with mutations that modify an antibody's biological activity, eg, half-life, eg, described in US Publication No. 20120100140 and US Patents and Publications and PCT publications cited herein. The term CH2 domain refers to the heavy chain constant region that hinges to the CH3 domain in a heavy chain constant domain. As used herein, a CH2 domain begins at P238 and ends at K340. The term CH2 domain includes wild-type CH2 domains, as well as naturally occurring variants thereof (eg, allotypes). The CH2 domain sequences of IgG1, IgG2, IgG3 and IgG4 (including wild type and allotypes) are known in the art. See, for example, Kabat EA et al. , (1991) mentioned above and Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014). Illustrative CH2 domains include CH2 domains with mutations that modify the biological activity of an antibody, eg, reduced Fe half-life and / or effector function, eg, described in US Publication No. 20120100140 and patents. and US publications and PCT publications cited therein. The term CH3 domain refers to the heavy chain constant region that is C-terminal to the CH2 domain in a heavy chain constant domain. As used herein, a CH3 domain begins at G341 and ends at K447. The term CH3 domain includes wild-type CH3 domains, as well as naturally occurring variants thereof (eg, allotypes). The CH3 domain sequences of IgG1, IgG2, IgG3 and IgG4 (including wild type and allotypes) are known in the art. See, for example, Kabat EA et al., (1991) mentioned above and Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014). Illustrative CH3 domains include CH3 domains with mutations that modify an antibody's biological activity, eg, half-life, eg, described in US Publication No. 20120100140 and US Patents and Publications and PCT publications cited herein. As used herein, isotype refers to the class of antibody (eg, IgG1, IgG2, IgG3, IgG4, IgM, IgAl, IgA2, IgD, and IgE antibody) that is encoded by the constant chain region genes. heavy. Allotype refers to naturally occurring variants within a specific isotype group, which variants differ by a few amino acids (see, for example, Jefferis et al., (2009) mAbs 1:1). The antibodies described herein can be of any allotype. IgG1, IgG2, IgG3 and IgG4 allotypes are known in the art. See, for example, Kabat EA et al., (1991) mentioned above; Vidarsson G. et al. Front Immunol. 5:520 (published online 2014-10-20) ; and Lefranc MP, mAbs 1:4, 1-7 (2009). The phrases an antibody that recognizes an antigen and an antibody specific for an antigen are used interchangeably herein with the term an antibody that specifically binds to an antigen. An isolated antibody, as used herein, refers to an antibody that is substantially free of other antibodies that have different antigenic specificities (for example, an isolated antibody that specifically binds L1CAM is substantially free of antibodies that bind specifically to antigens other than L1CAM). However, an isolated antibody that specifically binds to an L1CAM epitope may cross-react with other L1CAM proteins from different species. Binding affinity generally refers to the strength of the sum total of non-covalent interactions between a single binding site on a molecule (eg, an antibody) and its binding partner (eg, an antigen). . Unless otherwise indicated, as used herein, binding affinity refers to the intrinsic binding affinity that reflects a 1:1 interaction between members of a binding pair (eg, antibody and antigen ) . The affinity of a molecule X for its partner Y can be represented, in general terms, by the dissociation constant (Kd). Affinity can be measured and / or expressed in a variety of ways known in the art, including, but not limited to, equilibrium dissociation constant (Kd) and equilibrium association constant (KA). KD is calculated as the koff / kon ratio and is expressed as a molar concentration (M), while KAse is calculated from the kon / koff ratio. The kon refers to the constant of ΜΛ / / UUOO l rate of association of, for example, an antibody to an antigen, and kOff refers to the dissociation of, for example, an antibody to an antigen. The kOny kOff can be determined by techniques known to a person skilled in the art, such as immunoassays (for example, enzyme-linked immunosorbent assay (ELISA)), BIACORE®, BLI (Biolayer Interferometry), or kinetic exclusion assay ( KINEXA®) . As used herein, the terms specifically binds, specifically recognizes, specifically binds, selectively binds, and selectively binds are analogous terms in the context of antibodies and refer to molecules (eg, antibodies) that bind to an antigen. (eg, an epitope or an immune complex) as one of skill in the art understands the binding. For example, a molecule that specifically binds to an antigen can bind to other peptides or polypeptides, generally with lower affinity as determined by, for example, immunoassays, BIACORE®, KINEXA® 3000 instrument (Sapidyne Instruments, Boise, ID). , or other assays known in the art. In a specific aspect, molecules that specifically bind to an antigen bind to the antigen with a Ka that is at least 2 logs, 2.5 logs, 3 logs, 4 logs, or greater than the Ka when the molecules bind to another antigen. Antibodies typically bind specifically to their cognate antigen with high affinity, as reflected by an ICC5a dissociation constant (Kd) of ΙΟ-11M or less. In general, any Kd greater than about ΙΟ-4M is considered to indicate non-specific binding. As used herein, an antibody that specifically binds to an antigen refers to an antibody that binds to the antigen and substantially identical antigens with high affinity, meaning that it has a Kd of ΙΟ-7M or less, preferably ICn8M. or less, even more preferably ICE9M or less, and even more preferably between ICC8M and 10~10M or less, when determined by, for example, immunoassays (eg, ELISA), surface plasmon resonance (SPR) technology in a BIACORE™ 2000 instrument with the use of the default antigen, or BLI (Biolayer Interferometry), but does not bind with high affinity to unrelated antigens. As used herein, the term "antigen" refers to any natural or synthetic immunogenic substance, such as a protein, peptide, or hapten. An antigen can be L1CAM or a fragment thereof. As used herein, an epitope is a term of the art and refers to a localized region of an antigen to which an antibody can specifically bind. An epitope can be, for example, contiguous amino acids of a polypeptide (linear or contiguous epitope) or an epitope can, for example, be formed from two or more non-contiguous regions of a polypeptide or polypeptides (conformational epitope, nonlinear, discontinuous or non-contiguous). Epitopes formed from contiguous amino acids are typically, but not always, retained upon exposure to denaturing solvents, whereas epitopes formed by tertiary folding are typically lost upon treatment with denaturing solvents. An epitope typically includes at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, or 20 amino acids in a single spatial conformation. Methods for determining which epitopes are bound by a given antibody (i.e., epitope mapping) are known in the art and include, for example, immunoblotting and immunoprecipitation assays, where overlapping or contiguous peptides from (for example, L1CAM ) are tested for reactivity with a given antibody (eg, anti-LICAM antibody). Methods for determining the spatial conformation of epitopes include techniques described herein and in the art, for example, X-ray crystallography, two-dimensional nuclear magnetic resonance, and HDX-MS (see, for example, Epitope Mapping Protocols in Methods in Molecular Biology, Vol. 66, G.E. Morris, Ed. (1996)). In certain respects, it is possible to determine the ΜΛ / / UU JO l ¿ epitope to which an antibody binds by, for example, NMR spectroscopy, X-ray diffraction crystallography assays, ELISA assays, hydrogen / deuterium exchange in conjunction with mass spectrometry (e.g., spectrometry mass and electrospray liquid chromatography), matrix-based oligopeptide scanning assays, and / or mutagenesis mapping (eg, site-directed mutagenesis mapping). For X-ray crystallography, crystallization can be achieved using any of the methods known in the art (for example, Giege R et al., (1994) Acta Crystallogr D Blol Crystallogr 50(Pt 4): 339-350; McPherson A (1990) Eur J Biochem 189: 1-23; Chayen NE (1997) Structure 5: 1269-1274; McPherson A (1976) J Blol Chem 251: 6300-6303). Antibody:antigen crystals can be studied using well known X-ray diffraction techniques and can be refined using computer software such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc.; see, for example, Meth Enzymol (1985) volumes 114 and 115, ed Wyckoff HW et al.; U.S. 2004 / 0014194), and BUSTER (Bricogne G (1993) Acta Crystallogr D Blol Crystallogr 49 (Pt 1) : 37-60; Bricogne G (1997) Meth Enzymol 276A: 361-423, ed Carter CW, Roversi P et al., (2000) Acta Crystallogr D Blol Crystallogr 56 (Pt 10): 1316-1323). Mutagenesis mapping studies can be performed using any method known to one of skill in the art. See, for example, Champe M et al., (1995) J Biol Chem 270: 1388-1394 and Cunningham BC & Wells JA (1989) Science 244: 1081-1085 for a description of mutagenesis techniques, including techniques of Alanine scanning mutagenesis. The term epitope mapping refers to the process of identifying the molecular determinants for antibody-antigen recognition. The phrase "binds to the same epitope as a reference antibody" means that the antibodies bind to the same segment of amino acid residues, as determined by a given method. Techniques for determining whether antibodies bind to the same epitope on L1CAM with the antibodies described herein include, for example, epitope mapping methods, such as X-ray analysis of antigen:antibody complex crystals that provide atomic resolution. of the epitope and hydrogen / deuterium exchange mass spectrometry (HDX-MS). Other methods monitor antibody binding to antigen fragments or mutated variations of the antigen where loss of binding due to a modification of an amino acid residue within the antigen sequence is often considered an indication of an epitope component. In addition, computational combinatorial methods can also be used for epitope mapping. These methods are ΜΛ / / UU JO f ¿ are based on the ability of the antibody of interest to affinity isolate specific short peptides from combinatorial phage display peptide libraries. Antibodies having the same VH and VL sequences or the same CDR1, 2 and 3 are expected to bind to the same epitope. Antibodies that compete with another antibody to bind to a target refer to antibodies that inhibit (partially or completely) the binding of the other antibody to the target. Whether two antibodies compete with each other for binding to a target, i.e. whether and to what extent one antibody inhibits the binding of the other antibody to a target, can be determined using known competition experiments, e.g. plasmon resonance analysis. (SPR) BIACORE®. In some aspects, one antibody competes with and inhibits the binding of another antibody to a target by at least 50%, 60%, 70%, 80%, 90%, or 100%. The level of inhibition or competition can be different depending on which antibody is the blocking antibody (ie, the cold antibody that is first incubated with the target). Proficiency tests can be carried out as described, for example, in Ed Harlow and David Lane, Cold Spring Harb Protocol; 2006; doi: 10.1101 / pdb.prot4277 or in Chapter 11 of Using Antibodies by Ed Harlow and David Lane, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA 1999. Two antibodies cross-compete if the antibodies block on both sensed by at least 50%, i.e. regardless of whether one or the other antibody comes into contact with the antigen first in the competition experiment. Competitive binding assays to determine whether two antibodies compete or cross-compete for binding include: competition for binding to cells expressing L1CAM, eg, by flow cytometry, as described in the Examples. Other methods include: SPR (e.g., BIACORE®), BLI (biolayer interferometry), solid phase direct or indirect radioimmunoassay (RIA), solid phase direct or indirect enzyme immunoassay (EIA), sandwich competition assay (see Stahli et al., Methods in Enzymology 9:242 (1983)); Solid phase direct biotin-avidin EIA (see Kirkland et al., J. Immunol. 137:3614 (1986)); solid phase direct labeled assay, solid phase direct labeled sandwich assay (see Harlow and Lane, Antibodies: A Laboratory Manual, Cold Spring Harbor Press (1988)); Solid phase direct labeling RIA using 1-125 labeling (see Morel et al., Mol. Immunol. 25(1) :7 (1988)); Solid phase direct biotin-avidin EIA (Cheung et al., Virology 176:546 (1990)); and RIA direct labeling (Moldenhauer et al., Scand. J. Immunol. 32:77 (1990)). As used herein, the terms specific binding, binding ΜΛ / / UU JO f ¿ selective, binds selectively, binds specifically refer to the binding of an antibody to an epitope on a predetermined antigen. Normally, the antibody (i) binds with an equilibrium dissociation constant (Kd) of about less than 10~7M, such as about less than 10~8Μ, ΙΟ-9Μ or 1CU10M or even less when determined by, for example , surface plasmon resonance (SPR) technology on a BIACORE® 2000 instrument using the predetermined antigen, e.g., recombinant human MICA or MICB as analyte and antibody as ligand, or Scatchard assay for antibody binding to antigen-positive cells , and (ii) binds to the default antigen with an affinity that is at least twice its binding affinity to a non-specific antigen (eg, BSA, casein) other than the default antigen or a closely related antigen. Accordingly, an antibody that specifically binds to human L1CAM refers to an antibody that binds to cell-bound or soluble human L1CAM with a Kd of 10~7M or less, such as about less than 10~8Μ, 10~9Μ or 10~10M or even less. An antibody that cross-reacts with cynomolgus L1CAM refers to an antibody that binds to cynomolgus L1CAM with a Kd of 1CU7M or less, such as about less than 1CU8M, 10~9M or 1CU10M or even less. In some aspects, antibodies that do not cross-react with L1CAM from a non-human species exhibit essentially undetectable binding against these proteins in standard binding assays. The term kaSoCo ka, as used herein, is intended to refer to the rate of association of a particular antibody-antigen interaction, while the term kdis or kd, as used herein, is intended to refer to the rate of dissociation of a particular antibody-antigen interaction. The term Kd, as used herein, is intended to refer to the dissociation constant, which is derived from the ratio of kd to ka (ie, Kd / ka) and is expressed as a molar concentration (M). Kd values ​​for antibodies can be determined using methods established in the art. Available methods for determining the Kd of an antibody include surface plasmon resonance, a biosensor system such as a BIACORE® system, BLI (biolayer interferometry) or flow cytometry, and Scatchard analysis. As used herein, the term "high affinity" for an IgG antibody refers to an antibody having a Kd of 10~8M or less, 10~9M or less, or 10~10M or less for a target antigen. However, high affinity binding may vary for other antibody isotypes. For example, high affinity binding for an IgM isotype refers to an antibody that has a Kd of 10-10M or less, ΜΛ / / UUOO l or 10-8M or less . The term ECso in the context of an in vitro or in vivo assay using an antibody, or antigen-binding fragment thereof, refers to the concentration of an antibody, or antigen-binding fragment thereof, that induces a response that is 50% of the maximum response, that is, intermediate between the maximum response and the reference value. A bispecific or bifunctional antibody is an artificial hybrid antibody with two different heavy / light chain pairs and two different binding sites. Bispecific antibodies can be produced by a variety of methods, including hybridoma fusion or linkage of Fab' fragments. See, for example, Songsivilai & Lachmann, Clin. Exp. Immunol. 79:315-321 (1990); Kostelny et al., J. Immunol. 148, 1547-1553 (1992). The term "monoclonal antibody," as used herein, refers to an antibody that displays a single binding specificity and affinity for a particular epitope or an antibody composition in which all antibodies display a single binding specificity and affinity for a particular epitope. Accordingly, the term "human monoclonal antibody" refers to an antibody or antibody composition that exhibits a single binding specificity and that has variable regions and ΜΛ / / UU JO f ¿ optional constants derived from human germline immunoglobulin sequences. In one aspect, the human monoclonal antibodies are produced by a hybridoma that includes a B cell obtained from a transgenic non-human animal, eg. eg , a transgenic mouse, having a genome comprising a human heavy chain transgene and a light chain transgene fused with an immortalized cell and / or by a combinatorial library of recombinant human antibodies. The term "recombinant human antibody" includes all human antibodies that are prepared, expressed, created, or isolated by recombinant means, such as (a) antibodies isolated from an animal (eg, a mouse) that is transgenic or transchromosomal for genes of human immunoglobulin or a hybridoma prepared therefrom, (b) antibodies isolated from a host cell transformed to express the antibody, e.g. g., from a transectome, (c) antibodies isolated from a combinatorial library of recombinant human antibodies, and (d) antibodies prepared, expressed, created, or isolated by other means involving splicing of human immunoglobulin gene sequences to other DNA sequences. Such recombinant human antibodies comprise variable and constant regions using particular human germline immunoglobulin sequences encoded by the ΜΛ / / UU JO l germline genes, but include subsequent rearrangements and mutations that may occur, for example, during antibody maturation. As is known in the art (see, for example, Lonberg (2005) Nature Biotech. 23(9):1117-1125), the variable region contains the antigen-binding domain, which is encoded by several genes that are rearranged to form a specific antibody to a foreign antigen. In addition to rearrangement, the variable region can be further modified by multiple single amino acid changes (termed somatic mutation or hypermutation) to increase the affinity of the antibody for the foreign antigen. The constant region will change in further response to an antigen (ie isotype switch). Thus, somatically mutated rearranged nucleic acid molecules encoding heavy chain and light chain immunoglobulin polypeptides in response to an antigen may not have sequence identity to the original nucleic acid molecules, but may be substantially identical or similar. (ie, with at least 80% identity). A human antibody (HuMAb) refers to an antibody having variable regions in which both the framework and CDR regions are derived from human germline immunoglobulin sequences. Furthermore, if the antibody contains a constant region, the constant region is also derived from human germ line immunoglobulin sequences. The antibodies described herein may include amino acid residues not encoded by human germline immunoglobulin sequences (eg, mutations introduced by random or site-specific mutagenesis in vitro or by somatic mutation in vivo). However, as used herein, the term "human antibody" is not intended to include antibodies in which CDR sequences derived from the germ lines of another mammalian species, such as mouse, were grafted onto human framework sequences. The terms human antibodies and fully human antibodies are used synonymously. A chimeric antibody refers to an antibody in which the variable regions are derived from one species and the constant regions are derived from another species, such as an antibody in which the variable regions are derived from a mouse antibody and the constant regions are derived from a mouse antibody. human. The phrase cross-reacts, as used herein, refers to the ability of an antibody described herein to bind L1CAM from a different species. For example, an antibody described herein that binds to human L1CAM can also bind to another species of L1CAM (eg, mouse L1CAM). As used herein, the ΜΛ / / UUOO f ¿ cross-reactivity can be measured by detecting a specific reactivity with purified antigen in binding assays (eg, SPR, ELISA) or by binding to, or otherwise functionally interacting with, cells physiologically expressing L1CAM. Methods for determining cross-reactivity include standard binding assays as described herein, for example, BIACORE® surface plasmon resonance (SPR) analysis using a BIACORE® 2000 SPR instrument (Biacore AB, Uppsala, Sweden), or flow cytometry techniques. The term naturally occurring, as applied to an object herein, refers to the fact that an object can be found in nature. For example, a polypeptide or polynucleotide sequence that is present in an organism (including viruses) that can be isolated from a source in nature and has not been intentionally modified by man in the laboratory is naturally occurring. A polypeptide refers to a chain comprising at least two consecutively linked amino acid residues, with no upper limit on the length of the chain. One or more amino acid residues in the protein may contain a modification such as, but not limited to, glycosylation, phosphorylation, or disulfide bond formation. A protein can comprise one or more of ΜΛ / / UU JO l Polypeptides. The term nucleic acid molecule, as used herein, is intended to include DNA molecules and RNA molecules. A nucleic acid molecule can be single-stranded or double-stranded and can be cDNA. Conservative amino acid substitutions refers to substitutions of an amino acid residue with an amino acid residue having a similar side chain. Families of amino acid residues with similar side chains have been defined in the art. These families include amino acids with basic side chains (eg, lysin, arginine, histidine), acidic side chains (eg, aspartic acid, glutamic acid), uncharged polar side chains (eg, glycine, asparagine, glutamine, serine, threonine, tyrosine, cysteine, tryptophan), nonpolar side chains (eg, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine), beta branched side chains (eg, threonine, valine, isoleucine) and aromatic side chains (eg, tyrosine, phenylalanine, tryptophan, histidine). In some aspects, a predicted nonessential amino acid residue in an anti-LICAM antibody is replaced with another amino acid residue from the same family of side chains. Methods for identifying conservative nucleotide and amino acid substitutions that do not abolish antigen binding are ΜΛ / / UU JO l ¿ known in the art (see, for example, Brummell et al., Biochem. 32: 1180-1187 (1993); Kobayashi et al. Protein Eng. 12(10):879-884 (1999 and Burks et al. Proc. Nati. Acad. Sel. USA 94:412-417 (1997)). The percent identity between two sequences is a function of the number of identical positions the sequences share, (i.e., % homology = # of identical positions / n.0 total positions x 100), taking into account the number of of spaces, and the length of each space, that must be entered for optimal alignment of the two sequences. Sequence comparison and determination of percent identity between two sequences can be accomplished by a mathematical algorithm, as described in the non-limiting examples below. Percent identity between two nucleotide sequences can be determined using the GAP program in the GCG software package (available at worldwideweb.gcg.com), using an NWSgapdna.CMP matrix and a space weight of 40, 50, 60, 70 or 80 and a length weight of 1, 2, 3, 4, 5, or 6. The percent identity between two nucleotide or amino acid sequences can also be determined using the algorithm of E. Meyers and W. Miller (CABIOS, 4: 11-17 (1989)) which has been incorporated into the ALIGN program (version 2.0), using a PAM120 weight residual table, a gap length penalty of 12, and a ΜΛ / / UUOO f ¿ gap penalty of 4. In addition, the percent identity between two amino acid sequences can be determined using the algorithm of Needleman and Wunsch (J. Mol. Biol. (48):444-453 (1970)) which has been incorporated into the GAP program in the GCG software package (available at http: / / www.gcg.com), using either a Blossum 62 matrix or a PAM250 matrix, and a space weighting of 16, 14, 12, 10 , 8, 6, or 4 and a length weight of 1, 2, 3, 4, 5, or 6. The nucleic acid and protein sequences described herein can further be used as a query sequence for searching public databases to, for example, identify related sequences. Searches can be performed using the NBLAST and XBLAST (version 2.0) programs by Altschul, et al. (1990) J. Mol. Biol. 215:403-10. BLAST nucleotide searches can be performed with the NBLAST program, score=100, wordlength=12 to obtain nucleotide sequences homologous to the nucleic acid molecules described herein. BLAST protein searches can be performed with the XBLAST program, score=50, wordlength=3 to obtain amino acid sequences homologous to the protein molecules described herein. To obtain gapped alignments for comparison purposes, Gapped BLAST can be used, as ΜΛ / / UUOO f¿ described in Altschul et al., (1997) Nucleic Aclds Res. 25(17):3389-3402. When using the BLAST and Gapped BLAST programs, the default parameters of the respective programs (eg, XBLAST and NBLAST) may be used. See worldwideweb.nebí.nlm.nih.gov. The nucleic acids may be present in whole cells, in a cell lysate, or in a substantially pure or partially purified form. A nucleic acid is isolated or rendered substantially pure when it is purified from other cellular components or other contaminants, for example, other nucleic acids (for example, the other parts of the chromosome) or cellular proteins, by standard techniques, including alkaline / with SDS, CsCl banding, column chromatography, agarose gel electrophoresis and others known in the art. See, F. Ausubel, et al., ed. Current Protocols in Molecular Biology, Greene Publishing and Wiley Interscience, New York (1987). Nucleic acids, eg cDNA, can be mutated according to standard techniques to provide gene sequences. For coding sequences, these mutations can affect the amino acid sequence as desired. In particular, DNA sequences substantially homologous to natural or derived change, constant, and V, D, J sequences and other sequences are contemplated. ΜΛ / / UU JO f ¿ of this type described herein (where derivative indicates that a sequence is identical to or modified from another sequence). The term "vector" as used herein is intended to refer to a nucleic acid molecule capable of transporting another nucleic acid to which it has been linked. One type of vector is a plasmid, which refers to a circular double-stranded DNA loop into which additional DNA segments can be ligated. Another type of vector is a viral vector, wherein additional DNA segments can be ligated into the viral genome. Certain vectors are capable of autonomous replication in a host cell into which they are introduced (eg, bacterial vectors containing a bacterial origin of replication and mammalian episomal vectors). Other vectors (eg, non-episomal mammalian vectors) can integrate into the genome of a host cell upon introduction into the host cell and thus replicate along with the host genome. In addition, certain vectors are capable of directing the expression of genes to which they are operably linked. The vectors are referred to herein as recombinant expression vectors (or simply, expression vectors). In general, expression vectors of utility in ΜΛ / I / UU JO l ¿ recombinant DNA techniques are usually found in the form of plasmids. In the present description, plasmid and vector can be used interchangeably since plasmid is the most commonly used form of vector. However, other forms of expression vectors are also included, such as viral vectors (eg, replication-defective retroviruses, adenoviruses, and adeno-associated viruses), which serve equivalent functions. The term recombinant host cell (or simply host cell), as used herein, is intended to refer to a cell comprising a nucleic acid that is not naturally present in the cell, and may be a cell in which has introduced a recombinant expression vector. It should be understood that the terms are not intended to refer only to the particular cell in question, but to the progeny of the cell. Since certain modifications may occur in successive generations by mutations or environmental influences, such progeny may not, in fact, be identical to the original cell, but is equally included within the scope of the term host cell as used herein. As used herein, the term "linked" refers to the association of two or more molecules. The bond can be covalent or non-covalent. The link can also be genetic (ie, recombinantly fused). Linkages can be achieved using a wide variety of art-recognized techniques, such as chemical conjugation and recombinant protein production. An immune response is as understood in the art and generally refers to a biological response within a vertebrate against foreign or abnormal agents, eg, cancer cells, which response protects the organism against these agents and the diseases they cause. . An immune response is mediated by the action of one or more cells of the immune system (for example, a T cell, B cell, natural killer (NK) cell, macrophage, eosinophil, mast cell, dendritic cell, or neutrophil) and soluble macromolecules produced by any of these cells or the liver (including antibodies, cytokines, and complement) that results in the selective targeting, binding, damage, destruction, and / or elimination from the vertebrate body of invading pathogens, pathogen-infected cells, or tissues , cancer cells or other abnormal cells or, in cases of autoimmunity or pathological inflammation, normal human cells or tissues. An immune reaction includes, for example, the activation or inhibition of a T cell, for example, an effector T cell, a Th cell, a CD4+ cell, a CD8+ T cell, or a Treg cell, or the activation or inhibition of any another cell of the immune system, eg, NK cell. "Immunotherapy" refers to the treatment of a subject who has or is at risk of contracting or recurring a disease by a method comprising inducing, potentiating, suppressing, or otherwise modifying the immune system or an immune response. As used herein, "administer" refers to the physical introduction of a therapeutic agent or a composition comprising a therapeutic agent to a subject, using any of a variety of delivery methods and systems known to those skilled in the art. Preferred routes of administration for the antibodies described herein include intravenous, intraperitoneal, intramuscular, subcutaneous, spinal, or other parenteral routes of administration, eg, by injection or infusion. As used herein, the term "parenteral administration" means modes of administration other than enteral and topical administration, usually by injection, and includes, but is not limited to, intravenous, intraperitoneal, intramuscular, intraarterial, intrathecal, intralymphatic, intralesional, intracapsular, intraorbital, intracardiac, intradermal, transtracheal, subcutaneous, subcuticular, subcapsular intraarticular, subarachnoid, ΜΛ / I / UUOO l ¿ intraventricular, intravitreal, epidural and intrasternal, as well as in vivo electroporation. Alternatively, an antibody described herein can be administered by a non-parenteral route, such as a topical, epidermal, or mucosal route of administration, eg, intranasal, oral, vaginal, rectal, sublingual, or topical. The administration can also be carried out, for example, once, several times, and / or for one or more prolonged periods. As used herein, the phrase "suppresses tumor growth" includes any measurable decrease in tumor growth, eg, inhibition of tumor growth by at least about 10%, eg, at least about 10%. 20%, at least about 30%, at least about 40%, at least about 50%, at least about 60%, at least about 70%, at least about 80%, at least about 90% %, at least around 99%, or 100%. In some aspects, tumor growth inhibition is measured as percentage tumor growth inhibition (TGI%). The TGI% can be determined by calculating the TGI at date t which is calculated from all treatment animals according to the formula: [l-((Tt / To) / (Ct / Co) ) ] / [( Ct-Co) / Ct] * 100 [Formula 1], where Tt= size of the individual tumor of the treated animal at time 't', To = size ΜΛ / / UU JO f ¿ of the individual tumor of the treated animal at the first measurement, Ct = mean size of the tumors of the control animals at time 't', Co = mean size of the tumor of the control animals at the first measurement. As used herein, cancer refers to a broad group of diseases characterized by the uncontrolled growth of abnormal cells in the body. Unregulated cell division can lead to the formation of malignant tumors or cells that invade nearby tissues and can metastasize to distant parts of the body via the lymphatic system or bloodstream. The terms treat and treatment, as used herein, refer to any type of intervention or process performed on the subject, or the administration of an active agent to the subject, with the aim of reversing, alleviating, ameliorating, inhibiting, or slow or prevent the progression, development, severity, or recurrence of a symptom, complication, condition, or biochemical evidence associated with a disease, or enhance overall survival. The treatment may be of a subject having a disease or a subject not having a disease (eg, for prophylaxis). The term effective dose or effective dosage is defined as an amount sufficient to achieve a desired effect, or at least partially achieve it. A therapeutically effective amount therapeutically effective dose of a drug or therapeutic agent is any amount of the drug that, when used alone or in combination with another therapeutic agent, promotes regression of disease as evidenced by a decrease in the severity of symptoms of the disease. disease, an increase in the frequency and duration of periods without symptoms of the disease, an increase in overall survival (the period of time from the date of diagnosis or the start of treatment for a disease, such as cancer, in which patients diagnosed with the disease are still living), or a prevention of deterioration or disability due to the affliction of the disease. A therapeutically effective amount or dose of a drug includes a prophylactically effective amount or prophylactically effective dose, which is any amount of the drug that, when administered alone or in combination with another therapeutic agent to a subject at risk of developing a disease or of suffering from a recurrence of the disease, inhibits the development or recurrence of the disease. It is possible to assess the ability of a therapeutic agent to promote disease regression or inhibit disease development or recurrence using a variety of methods known to those skilled in the art, such as in human subjects during clinical trials. , in animal model systems that predict the ΜΛ / / UUOO l efficacy in humans or by evaluating the activity of the agent in in vitro assays. By way of example, an anticancer agent is a drug that promotes the regression of cancer in a subject. In some aspects, a therapeutically effective amount of the drug promotes the regression of the cancer to the point of elimination. To promote regression of cancer means that administration of an effective amount of the drug, alone or in combination with an antineoplastic agent, results in a reduction in tumor growth or size, tumor necrosis, a decrease in severity of at least one disease symptom, an increase in the frequency and duration of disease-symptom-free periods, an increase in overall survival, a prevention of deterioration or disability due to disease affliction, or an amelioration of disease symptoms the disease in the patient. Furthermore, the terms effective and efficacy with respect to a treatment include both pharmacological efficacy and physiological safety. Pharmacological efficacy refers to the ability of the drug to promote the regression of the cancer in the patient. Physiological safety refers to the level of toxicity or other adverse physiological effects at the cellular, organ and / or organism level (adverse effects) resulting from the ΜΛ / I / UU JO (¿ drug administration. By way of example, for the treatment of tumors, a therapeutically effective amount or dose of the drug inhibits cell growth or tumor growth by at least about 20%, at least about 40%, at least about 60%, or by at least about 80% relative to untreated subjects. In some aspects, a therapeutically effective amount or dose of the drug completely inhibits cell growth or tumor growth, ie, inhibits cell growth or tumor growth by 100%. It is possible to assess the ability of a compound to inhibit tumor growth using the assays described below. Alternatively, this property of a composition can be assessed by examining the compound's ability to inhibit cell growth, inhibition in vitro can be measured by assays known to the skilled person. In some aspects described herein, tumor regression can be observed and continue for a period of at least about 20 days, at least about 40 days, or at least about 60 days. As used herein, the term "subject" includes any human or non-human animal. The term non-human animal includes all vertebrates, eg, mammals and non-mammals, such as non-human primates, sheep, dogs, cows, chickens, amphibians, reptiles, etc. ΜΛ / / UU JO f ¿ As used herein, the terms ug and uM are used interchangeably with pg and μΜ, respectively. Various aspects described herein are described in more detail in the following subsections. II. Anti-LICAM antibodies Described herein are antibodies, eg, monoclonal antibodies, which are characterized by particular functional elements or properties. For example, the antibodies specifically bind to mammalian (eg, human and mouse) L1CAM and exhibit one or more of the following functional properties: (a) shows improved productivity compared to antibody mAb417 (b) shows improved affinity as measured by equilibrium dissociation constant (Kd) compared to antibody mAb417; (c) shows an improved PI value compared to the mAb417 antibody; (d) shows improved affinity as measured by the association constant (K) compared to the mAb417 antibody; (e) prevent and / or treat diseases or conditions that comprise a tumor; or (f) any combination of these. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, shows improved productivity compared to the mAb417 antibody, for example, the improved productivity is at least 55 mg / L, at least 56 mg / L , at least 57 mg / L, at least 58 mg / L, at least 59 mg / L, at least about 60 mg / L, at least about 61 mg / L, at least about 62 mg / L, at least about 63 mg / L, at least about 64 mg / L, at least about 65 mg / L, at least about 66 mg / L, at least about 67 mg / L, at least about 68 mg / L, at least about 69 mg / L, at least about 70 mg / L, at least about 71 mg / L, at least about 72 mg / L, at least about 73 mg / L, at least about 74 mg / L, at least about 75 mg / L, at least about 76 mg / L, at least about 77 mg / L, at least about 78 mg / L, at least about 79 mg / L, at least about 80 mg / L, at least about 81 mg / L, at least about d e 82 mg / L, at least about 83 mg / L, at least about 84 mg / L, or at least about 85 mg / L, when expressed according to Example 3. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with high affinity, eg, with a Kd of less than 2.6 X 10~10M, less than 2.5 X 10~ 10M, less than 2.0 X 10~10M, less than 1.5 X 10~10M, less than 1.0 X 10~10Μ, less than 9 X ΙΟ-11M, less than 8 X 10-11M, less than 7 X 10-11M, less than 6 X ΙΟ-11M, less than 5 X 10-11M, less than 4 X ΙΟ-11M, less than 3 X ΙΟ-11Μ, less than 2 X ΙΟ- 11M, less than 1 X ΙΟ-11M, less than 9 X ΙΟ-12M, less than 8 X 10-12M, less than 7 X 10-12M, less than 6 X ICC12M, less than 5 X ICC12M, less than 4 X 10~12M, less than 3 X 10~12M, less than 2 X 10~12M, less than 1 X 10~12M, less than 9 X 10~13M, or less than 8 X 10~13M, e.g. eg , as measured by the biolayer interferometry (BLI) method (eg, as described in the examples). In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with a KD of less than 2 X ICr10M, less than 1.9 X 10~10M, less than 1.8 X ICC10M, less than 1.7 X 10~10M, less than 1.6 X l(h10M, less than 1.5 X 10~10Μλ less than 1.4 X 10~10M, less than 1.3 X 10~10M, less than 1.2 X ICC10M, or less than 1.1 X 10~ 10M In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with a Kd less than 1.1 X ICr10M.In other aspects, the anti-LICAM antibody, or antigen-binding fragment antigen thereof, specifically binds to human L1CAM with a Kd of less than 9 X 10~12M.In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with a lower Kd at 1 X 10~12M.In some aspects, the anti-LICAM antibody, or antigen-binding fragment of VIA / I / UU JO l ¿ this, specifically binds to human L1CAM with a Kd less than 8 X ΙΟ-11M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with a Kd of less than 1 X 10-12M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with a KD of less than 1.05 X 10~10M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with a Kd of about 8.22 X 10~12M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds human L1CAM with a KD of about 7.4 X 10-11M. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds human L1CAM with a Kd of about 9.6 X 10~nM. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, specifically binds to human L1CAM with high affinity, for example, with a Κ less than 5 X ICC10M, less than 4 X 10~10M, less than 3 X 10~10M, less than 2 X 10~10M, less than 1.0 X 10~10M, less than 9 X 10-11M, less than 8 X ΙΟ-11M, less than 7 X 10-11M, less than 6 X ΙΟ-11M, less than 5 X 10-11M, less than 4 X ΙΟ-11M, less than 3 X ΙΟ-11M, less than 2 X 10-11M, less than 1 X ΙΟ-11M, less than 9 X 10~12Μ, less than 8 X 10~12Μ, less than 7 X 10~12Μ, less than 6 X 10~12Μ, less than 5 X 10~12Μ, less than 4 X 10~12Μ, less than 3 X 10~12Μ, less than 2 X 10~12Μ, less than 1 X ΙΟ-12Μ, less than 9 X ΙΟ-13Μ, or less than 8 X 10~13M, e.g. eg , as measured by ELISA (eg , as described in the Examples). Standard assays for evaluating the binding capacity of antibodies to L1CAM from various species are known in the art, including, for example, ELISA, Western blotting, and RIA. Suitable assays are described in detail in the examples. The binding kinetics (eg, binding affinity) of antibodies can also be assessed by standard assays known in the art, such as ELISA, BIACORE® or KINEXA® assays. Assays to assess the effects of antibodies on the functional properties of L1CAM (eg, ligand binding) are described in more detail below and in the Examples. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, exhibits an enhanced isoelectric point (PI) value of less than 9.6, less than 9.5, less than 9.4, less than 9.3, less than 9.2, less than less than 9.1, less than 9.0, less than 8.9, less than 8.8, less than 8.7, less than 8.6, less than 8.5, less than 8.4, less than 8.3, less than 8.2, less than 8.1, less than 8.0, less than 7.9 , less than 7.8, less than 7.7, or less than 7.6., as measured by the capillary isoelectric focusing (cIEF) method (for example, as described in the Examples). In certain aspects, anti-LICAM antibodies, or antigen-binding fragments thereof, specifically bind to the same L1CAM epitope as a reference antibody comprising a heavy chain (VH) variable region and a light chain variable region. (VL), wherein: (a) the VH of the reference antibody comprises SEQ. ID NO.: 23 and the VL of the reference antibody comprises SEQ. ID NO.: 24, (b) the VH of the reference antibody comprises SEQ. ID NO.: 25 and the VL of the reference antibody comprises SEQ. ID NO.: 26, (c) the VH of the reference antibody comprises SEQ. ID NO.: 27 and the VL of the reference antibody comprises SEQ. ID NO.: 28, (d) the VH of the reference antibody comprises SEQ. ID NO.: 29 and the VL of the reference antibody comprises SEQ. ID NO.: 30, or (e) the VH of the reference antibody comprises SEQ. ID NO.: 31 and the VL of the reference antibody comprises SEQ. ID NO.: 32. In certain aspects, anti-LICAM antibodies, or antigen-binding fragments thereof, specifically bind to the same epitope of L1CAM as a reference antibody comprising the VH complementarity determining region 1 (CDR1), VH CDR2 and VH CDR3, and ΜΛ / / UU JO l¿ VL CDR1, VL CDR2 and VL CDR3, wherein at least one amino acid is in the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the antibody, or antigen-binding fragment thereof, is different from the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the reference antibody (eg, mAb417 antibody), wherein the VH CDR1, VH CDR2, VH CDR3 of the reference antibody comprise the amino acid sequence of SEQ. ID NO.: 2, SEQ. ID NO.: 9 and SEQ. ID NO.: 10, respectively, and the VL CDR1, VL CDR2 and VL CDR3 of the reference antibody comprise the amino acid sequence of SEQ. ID NO.: 6, SEQ. ID NO.: 7 and SEQ. ID NO.: 11, respectively. In certain aspects, the at least one amino acid difference comprises (i) glutamine at residue 5 in CDR2 of VH; (ii) serine at residue 8 in the CDR1 of VL; and / or (iii) proline at residue 8 in CDR3 of VL of the anti-LICAM antibody, or antigen binding fragment thereof. In certain aspects, the at least one amino acid difference comprises (i) alanine, glycine, phenylalanine, tyrosine, threonine, proline, and tryptophan at residues 3 to 9, respectively in the CDR3 of VL; (ii) alanine, glycine, phenylalanine, tyrosine, serine, proline and tryptophan at residues 3 to 9, respectively in the CDR3 of VL or (iii) leucine, valine or histidine, tryptophan or phenylalanine, tyrosine, proline and tryptophan at the residues at 9, respectively in the CDR3 of VL of the antiL1CAM antibody, or antigen-binding fragment thereof. In certain aspects, anti-LICAM antibodies, or antigen-binding fragments thereof, cross-compete for binding to the L1CAM epitope as a reference antibody comprising the VH complementarity determining region 1 (CDR1), VH CDR2 and VH CDR3, and VL CDR1, VL CDR2 and VL CDR3, wherein at least one amino acid in VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the antibody, or antigen-binding fragment thereof, is different from the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the antibody reference (eg mAb417 antibody), (i) wherein the VH CDR1, VH CDR2, VH CDR3 of the reference antibody comprises the amino acid sequence of SEQ. ID NO.: 2, SEO. ID NO.: 9 and SEO. ID NO. : 10, respectively, and the VL CDR1, VL CDR2 and VL CDR3 of the reference antibody comprise the amino acid sequence of SEQ. ID NO.: 6, SEQ. ID NO.: 7 and SEQ. ID NO.: 11, respectively. In certain aspects, the at least one amino acid difference comprises (i) glutamine at residue 5 in CDR2 of VH; (ii) serine at residue 8 in the CDR1 of VL; and / or (iii) proline at residue 8 in CDR3 of VL of the anti-LICAM antibody, or antigen binding fragment thereof. In certain aspects, the at least one amino acid difference comprises (i) alanine, glycine, phenylalanine, tyrosine, threonine, proline, and tryptophan at residues 3 to 9, respectively in the CDR3 of VL; (ii) alanine, glycine, phenylalanine, tyrosine, serine, proline and tryptophan at residues 3 to 9, respectively in the CDR3 of VL or (iii) leucine, valine or histidine, tryptophan or phenylalanine, tyrosine, proline and tryptophan at the residues 4 to 9, respectively in the CDR3 of VL of the anti-LICAM antibody, or antigen-binding fragment thereof. In certain aspects, anti-LICAM antibodies, or antigen-binding fragments thereof, cross-compete for binding to the L1CAM epitope with a control antibody comprising a heavy chain (VH) variable region and a variable region. light chain (VL), wherein: (a) the VH of the reference antibody comprises SEQ. ID NO.: 23 and the VL of the reference antibody comprises SEQ. ID NO.: 24, (b) the VH of the reference antibody comprises SEQ. ID NO.: 25 and the VL of the reference antibody comprises SEQ. ID NO.: 26, (c) the VH of the reference antibody comprises SEQ. ID NO.: 27 and the VL of the reference antibody comprises SEQ. ID NO.: 28, (d) the VH of the reference antibody comprises SEQ. ID NO.: 29 and the VL of the reference antibody comprises SEQ. ID NO.: 30, or (e) the VH of the reference antibody comprises SEQ. ID NO. : 31 and the VL of the reference antibody comprises SEQ. ID NO.: 32. Competing antibodies bind to the same epitope, an overlapping epitope, or to adjacent epitopes (eg, as evidenced by spherical impediment). Whether two antibodies compete with each other to bind to a target can be determined by competition experiments known in the art, such as RIA and EIA. Techniques for determining whether two antibodies bind to the same epitope include, for example, epitope mapping methods, such as X-ray analysis of antigen:antibody complex crystals that provide atomic resolution of the epitope and hydrogen exchange mass spectrometry. / deuterium (HDX-MS), methods that monitor antibody binding to antigen fragments or mutated variations of the antigen, where loss of binding due to a modification of an amino acid residue within the antigen sequence is often considered a indication of an epitope component, computational combinatorial methods for epitope mapping. In certain aspects, an antibody, or antigen-binding fragment thereof, is provided herein that binds to L1CAM (eg, human LIGAN) with 20%, 25%, 30%, 35%, 40% , 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or higher affinity than to another LIGAN family protein, as measured by , p. eg, a ΜΛ / I / UUOO l ¿ immunoassay (eg, ELISA), surface plasmon resonance, BLI (biolayer interferometry), or kinetic exclusion assay. In a specific aspect, provided herein is an antibody, or antigen-binding fragment thereof, that binds to L1CAM (eg, human L1CAM) without cross-reactivity with another L1CAM-family protein as measured by, eg, an immunoassay. In certain aspects, anti-LICAM antibodies are not natural antibodies or are not naturally occurring antibodies. For example, anti-LICAM antibodies have post-translational modifications that are different from naturally occurring antibodies, eg, by having more, less, or a different type of post-translational modification. III. Illustrative anti-LICAM antibodies Particular antibodies that can be used in the methods described herein are antibodies, eg, monoclonal antibodies, having the CDR and / or antibody variable region sequences Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 constructed in Examples 1. and 2, as well as antibodies having at least 80% identity (for example, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about than 97%, at least about 98%, at least about 99%, or about 100% of ΜΛ / I / UUOO l¿identity) with their variable region or CDR sequences. The VH amino acid sequences of Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 are set forth in SEQ. ID NO.: 23, 25, 27, 29 and 31, respectively. The VL amino acid sequences of Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 are set forth in SEQ. ID NO.: 24, 26, 28, 30 and 32, respectively. ΜΛ / / UU JO l Table 2. Variable heavy chain CDR amino acid sequences (according to the Kabat system) VH-CDR1 VH-CDR2 VH-CDR3 Anti-L1CAM Antibody (“Ab612”) RFGMH (SEQ. ID NO.: 2) FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) GRAYGSGSLFDP (SEQ. ID NO.: 4) Anti- L1CAM ("Ab4H5") RFGMH (SEQ. ID NO.: 2) FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) GRAYGSGSLFDP (SEQ. ID NO.: 4) Anti-L1CAM ("Ab2C2") RFGMH (SEQ. ID NO. .: 2) FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) GRAYGSGSLFDP (SEQ. ID NO.: 4) Anti-L1CAM (“Ab4H6”) RFGMH (SEQ. ID NO.: 2) FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) GRAYGSGSLFDP (SEQ. ID NO.: 4) Anti-L1CAM (“Ab5D12”) RFGMH (SEQ. ID NO.: 2) FISNEGSNKYYADSVKG (SEQ. ID NO.: 10) GRAYGSGSLFDP (SEQ. ID NO.: 4) Table 3. Variable light chain CDR amino acid sequences (according to the Kabat system) Antibody VL-CDR1 VL-CDR2 VL-CDR3 Ant¡-L1CAM (“Ab612”) RASRTISSYVN (SEQ. ID NO.: 12) AASNLHS (SEQ. ID NO.: 7) QQSIGRGPVT (SEQ. ID NO.: 13) Anti -L1CAM ("Ab4H5") RASRTISSYVN (SEQ. ID NO.: 12) AASNLHS (SEQ. ID NO.: 7) QQAGFYTPWT (SEQ. ID NO.: 15) Anti-L1CAM (“Ab2C2”) RASRTISSYVN (SEQ. ID NO.: 12) AASNLHS (SEQ. ID NO.: 7) QQAGFYSPWT (SEQ. ID NO.: 17) Anti-L1CAM RASRTISSYVN AASNLHS QQSLHFYPWT (“Ab4H6”) ( SEQ. ID NO.: 12) (SEQ. ID NO.: 7) (SEQ. ID NO.: 19) Anti-L1CAM RASRTISSYVN AASNLHS QQSLVWYPWT (“Ab5D12”) (SEQ. ID NO.: 12) (SEQ. ID NO.: 7) (SEQ. ID NO.: 21) ΜΛ / / UU JO l Table 4A. Variable heavy chain amino acid sequence VH Amino Acid Sequence Antibody (SEQ. ID NO.) Anti-L1CAM (“Ab612”) EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S. (SEQ. ID NO-1HCAM 23) Anti-LCAM ”) EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEC. ID NO.:25) Anti-L1CAM (“Ab2C2”) EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEC. ID NO.: 27) Anti-L1CAM (“Ab4H6”) EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTLY LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEC. ID NO.: 29) Anti-L1CAM (“Ab5D12”) EVQLVESGGG WQPGGSLRL SCAASGFTFS RFGMHWVRQA PGKGLEWVAF ISNEGSNKYY ADSVKGRFTI SRDNSANTL Y LQMNSLRAED TAVYYCARGR AYGSGSLFDP WGQGTLVTVS S (SEQ. ID NO.: 31) Table 4B. Variable Light Chain Amino Acid Sequence Anti-LICAM ("Ab612") VL Amino Acid Sequence Antibody DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ SIGRGPVTFG QGTKLEIK (SEQ. ID NO.: 24") Anti-L15CAM ("Ab4H5CAM") DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ AGFYTPWTFG QGTKLEIK (SEC. ID NO.: 26) Anti-LICAM (“Ab2C2”) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ AGFYSPWTFG QGTKLEIK (SEC. ID NO.: 28) Anti-LICAM (“Ab4H6”) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYC QQSLHFYPWT FG QGTKLEIK (SEC. ID NO.: 30) Ant¡-L1CAM (“Ab5D12”) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYC QQSLVWYPWT FG QGTKLEIK (SEQ. ID NO.: 32) Accordingly, provided herein is an isolated anti-LICAM antibody, or antigen-binding fragment thereof, comprising heavy and light chain variable regions, wherein the heavy chain variable region comprises the amino acid sequence of the SEQ. ID NO.: 23, 25, 27, 29 or 31. In other aspects, the isolated anti-LICAM antibody, or an antigen-binding fragment thereof, comprises the heavy chain variable region CDRs selected from the group consisting of in the SECs. ID NO.: 2, or 4. Also provided is an isolated anti-LICAM antibody, or antigen-binding fragment thereof, comprising heavy and light chain variable regions, wherein the light chain variable region comprises the amino acid sequence of SEQ. ID NO.: 24, 26, 28, 30, or 32. In other aspects, the isolated anti-LICAM antibody, or an antigen-binding fragment thereof, comprises the light chain variable region CDRs selected from the group that consists of SECs. ID NO.: 12, 7, 13, 15, 17, 19 or 21. In certain aspects, the isolated anti-LICAM antibody, or an antigen-binding fragment thereof, comprises the heavy chain variable region CDRs selected from the group consisting of SEQs. ID NO.: 2, 10 or 4 and the CDRs of the light chain variable region selected from the group consisting of SEQ. ID NO.: 12, 7, 13, 15, 17, 19 or 21. Also provided is an isolated anti-LICAM antibody, or antigen-binding fragment thereof, comprising the heavy and light chain variable regions, (i) wherein the heavy chain variable region comprises the amino acid sequence of SEQ . ID NO.: 23 and wherein the light chain variable region comprises the amino acid sequence of SEQ. ID NO.: 24; (ii) wherein the heavy chain variable region comprises the amino acid sequence of SEQ. ID NO.: 25 and wherein the light chain variable region comprises the sequence of ΜΛ / / UU JO l ¿ amino acids of SEQ. ID NO.: 26; (iii) wherein the heavy chain variable region comprises the amino acid sequence of SEQ. ID NO.: 27 and wherein the light chain variable region comprises the amino acid sequence of SEQ. ID NO.: 28; (iv) wherein the heavy chain variable region comprises the amino acid sequence of SEQ. ID NO. : 29 and wherein the light chain variable region comprises the amino acid sequence of SEQ. ID NO.: 30; or (v) wherein the heavy chain variable region comprises the amino acid sequence of SEQ. ID NO.: 31 and wherein the light chain variable region comprises the amino acid sequence of SEQ. ID NO.: 32. Provided herein is an isolated anti-LICAM antibody, or an antigen-binding fragment thereof, comprising a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises a sequence of amino acid which is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98 %, at least about 99%, or about 100% identical to the amino acid sequence indicated as SEQ. ID NO.: 23, 25, 27, 29 or 31. Also provided herein is an isolated anti-LICAM antibody, or antigen-binding fragment thereof, comprising a heavy chain variable region and a light chain variable region, wherein the light chain variable region comprises a sequence of amino acids that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as SEQ. ID NO.: 24, 26, 28, 30 or 32. Provided herein is an isolated anti-LICAM antibody, or antigen-binding fragment thereof, comprising a heavy chain variable region and a light chain variable region, wherein the heavy chain variable region comprises a sequence of amino acid which is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98 %, at least about 99%, or about 100% identical to the amino acid sequence indicated as SEQ. ID NO.: 23, 25, 27, 29 or 31, and wherein the light chain variable region comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90% , at least ΜΛ / I / UUOO l ¿ about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the sequence of amino acids indicated as SEQ. ID NO.: 24, 26, 28, 30 or 32. In some aspects, the isolated anti-LICAM antibody, antigen thereof, comprising (a) light region sequences comprising the respectively; (b) light region sequences comprising the respectively; (c) light region sequences comprising the respectively; (d) light region sequences comprising the respectively; or (e) light region sequences comprising the respectively. The amino acid sequences description provides one or a fragment binding to the heavy chain variable and SEQ. ID NO. : 23 and 24, heavy string variable and SEQ. ID NO. : 25 and 26, heavy string variable and SEQ. ID NO. : 27 and 28, heavy string variable and SEQ. ID NO. : 29 and 30, heavy string variable and SEQ. ID NO. : 31 and 32, os of CDR1, CDR2 and CDR3 of VH for Ab612 antibody, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 are set forth in SEQ. ID NO.: 2, 10 and 4, respectively. The VL CDR1, CDR2 and CDR3 amino acid sequences for Ab612 are set forth in SEQ. ID NO.: 12, 7 and 13, respectively. The VL CDR1, CDR2 and CDR3 amino acid sequences for Ab4H5 are set forth in SEQ. ID NO.: 12, 7 and 15, respectively. The VL CDR1, CDR2 and CDR3 amino acid sequences for Ab2C2 are set forth in SEQ. ID NO.: 12, 7 and 17, respectively. The amino acid sequences of the VL CDR1, CDR2 and CDR3 for Ab4H6 are set forth in SEQ. ID NO.: 12, 7 and 19, respectively. The VL CDR1, CDR2 and CDR3 amino acid sequences for Ab5D12 are set forth in SEQ. ID NO.: 12, 7 and 21, respectively. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, of the disclosure, which specifically binds to human L1CAM, comprises: (a) a VH CDR1 comprising the amino acid sequence of SEQ. ID NO.: 2; and / or (b) a VH CDR2 comprising the amino acid sequence of SEQ. ID NO.: 10; and / or (c) a VH CDR3 comprising the amino acid sequence of SEQ. ID NO.: 4. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, that specifically binds to human L1CAM, comprises: ΜΛ / / UU JO 1 (a) a VL CDR1 comprising the amino acid sequence of SEQ. ID NO.: 12; and / or (b) a VL CDR2 comprising the amino acid sequence of SEQ. ID NO.: 7; and / or (c) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 13. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, which specifically targets human L1CAM, comprises: (a) a VH CDR1 comprising the amino acid sequence of SEQ. ID NO.: 2; (b) a VH CDR2 comprising the amino acid sequence of SEQ. ID NO.: 10; (c) a VH CDR3 comprising the amino acid sequence of SEQ. ID NO.: 4; (d) a VL CDR1 comprising the amino acid sequence of SEQ. ID NO.: 12; (e) a VL CDR2 comprising the amino acid sequence of SEQ. ID NO.: 7; and / or (f) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 13. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, which specifically targets human L1CAM, comprises: (a) a VL CDR1 comprising the sequence from from from of of of of of or one of ΜΛ / / UUOO l SEQ amino acids. ID NO.: 12; and / or (b) a VL CDR2 comprising the amino acid sequence of SEQ. ID NO.: 7; and / or (c) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 15. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, which specifically targets human L1CAM, comprises: (a) a VH CDR1 comprising the amino acid sequence of SEQ. ID NO.: 2; (b) a VH CDR2 comprising the amino acid sequence of SEQ. ID NO.: 10; (c) a VH CDR3 comprising the amino acid sequence of SEQ. ID NO.: 4; (d) a VL CDR1 comprising the amino acid sequence of SEQ. ID NO.: 12; (e) a VL CDR2 comprising the amino acid sequence of SEQ. ID NO.: 7; and / or (f) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 15. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, which specifically targets human L1CAM, comprises: (a) a VL CDR1 comprising the amino acid sequence of SEQ. ID NO.: 12; and / or of of of of of of or binds from (b) a CDR2 of VL comprising the amino acid sequence of SEQ. ID NO.: 7; and / or (c) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 17. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, which specifically targets human L1CAM, comprises: (a) a VH CDR1 comprising the amino acid sequence of SEQ. ID NO.: 2; (b) a VH CDR2 comprising the amino acid sequence of SEQ. ID NO.: 10; (c) a VH CDR3 comprising the amino acid sequence of SEQ. ID NO.: 4; (d) a VL CDR1 comprising the amino acid sequence of SEQ. ID NO.: 12; (e) a VL CDR2 comprising the amino acid sequence of SEQ. ID NO.: 7; and / or (f) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 17. In some aspects, the anti-LICAM antibody, antigen-binding fragment thereof, which specifically targets human L1CAM, comprises: (a) a VL CDR1 comprising the amino acid sequence of SEQ. ID NO.: 12; and / or (b) a VL CDR2 comprising the sequence of of or of of of of or of ΜΛ / I / UUOO l ¿ amino acids of SEQ. ID NO.: 7; and / or (c) a VL CDR3 comprising the amino acid sequence of SEQ. ID NO.: 19. ΜΛ / / UU JO i In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof that specifically binds to human L1CAM, comprises: a CDR1 of VH comprising the amino acid of SEQ. ID NO.: 2; (b) a CDR2 of VH comprising the amino acid sequence of SEQ. ID NO.: 10; a CDR3 of VH comprising the amino acid sequence of SEQ. ID NO.: 4; (d) a CDR1 of VL comprising the amino acid sequence of SEQ. ID NO.: 12; a CDR2 of VL comprising the amino acid sequence of SEQ. ID NO.: 7; I CDR3 of VL comprising the amino acid of SEQ. ID NO.: 21. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, that specifically binds to human L1CAM, comprises a heavy chain (HC) and a light chain (LC), where the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 38 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID 100 NO.: 39. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, that specifically binds to human L1CAM, comprises a heavy chain (HC) and a light chain (LC), where the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO. : 40 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 41. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, that specifically binds to human L1CAM, comprises a heavy chain (HC) and a light chain (LC), where the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 42 and the LC of the antibody, or antigen-binding fragment thereof, comprising SEQ. ID NO.: 43. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, that specifically binds to human L1CAM, comprises a heavy chain (HC) and a light chain (LC), where the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 44 and the LC of the antibody, or antigen-binding fragment thereof, of the latter, comprises the VIA / / UU JO l ¿ SEQ. ID NO.: 45. 101 In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, that specifically binds to human L1CAM, comprises a heavy chain (HC) and a light chain (LC), where the HC of the antibody, or antigen-binding fragment thereof, comprises SEQ. ID NO.: 46 and the LC of the antibody, or antigen-binding fragment thereof, of the latter, comprises SEQ. ID NO.: 47. ΜΛ / I / UUOO l¿ Table 5A. heavy chain amino acid sequence Anticuerpo Secuencia de aminoácidos de cadena pesada (SEC. ID NO.) Anti-LICAM (Ab612) EVQLVESGGGWQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVA FISNEGSNKYYADSVKGRFTISRDNSANTLYLQMNSLRAEDTAVYYCA RGRAYGSGSLFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSWTVP SSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVWDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRWSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH EALHNHYTQKSLSLSPGK (SEC. ID NO.:38) Anti-LICAM (Ab4H5) EVQLVESGGGWQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVA FISNEGSNKYYADSVKGRFTISRDNSANTLYLQMNSLRAEDTAVYYCA RGRAYGSGSLFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSWTVP SSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVWDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRWSVLTVLHQDWLNGKEYKCKVSNKALPAPIE 102 KTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH EALHNHYTQKSLSLSPGK (SEC. ID NO.:40) Anti-LICAM (Ab2C2) EVQLVESGGGWQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVA ElSNEGSNKYYADSVKGRFTISRDNSANTLYLQMNSLRAEDTAVYYCA RGRAYGSGSLFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSWTVP SSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVWDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRWSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH EALHNHYTQKSLSLSPGK (SEC. ID NO.:42) Anti-LICAM (Ab4H6) EVQLVESGGGWQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVA ElSNEGSNKYYADSVKGRFTISRDNSANTLYLQMNSLRAEDTAVYYCA RGRAYGSGSLFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSWTVP SSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVWDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRWSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQ VYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH EALHNHYTQKSLSLSPGK (SEC. ID NO.:44) Anti-LICAM (Ab5D12) EVQLVESGGGWQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVA FISNEGSNKYYADSVKGRFTISRDNSANTLYLQMNSLRAEDTAVYYCA RGRAYGSGSLFDPWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAA LGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSWTVP ΙνΙΛ / I / UUOO / ¿ 103 SSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCPPCPAPELLGG PSVFLFPPKPKDTLMISRTPEVTCVWDVSHEDPEVKFNWYVDGVEVH NAKTKPREEQYNSTYRWSVLTVLHQDWLNGKEYKCKVSNKALPAPIE KTISKAKGQPREPQVYTLPPSRDELTKNQVSLTCLVKGFYPSDIAVEW ESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH EALHNHYTQKSLSLSPGK (SEC. ID NO.:46) ΜΛ / I / UUOO l¿ Table 5B. light chain amino acid sequence Anticuerpo Secuencia de aminoácidos de cadena ligera (SEC. ID NO.) Anti-LICAM (Ab612) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ SIGRGPVTFGQ GTKLEIKRTVAAPSVFIFPPSDEQLKSGTASWCLLNNFYPREAKVQW KVDNALQ SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSS PVTKSFN RGEC (SEC. ID NO.: 39) Anti-LICAM (Ab4H5 ) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ AGFYTPWTFG QGTKLEIK TVAAPSVFIFPPSDEQLKSGTASWCLLNNFYPREAKVQWKVDNAL QSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLS SPVTKSFN RGEC (SEC. ID NO.: 41) Anti-LICAM (Ab2C2) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYCQQ AGFYSPWTFG QGTKLEIK RTVAAPSVFIFPPSDEQLKSGTASWCLLNNFYPREAKVQWKVDNA LQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGL 104 SSPVTKS FNRGEC (SEC. ID NO.: 43) Anti-LICAM (Ab4H6) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYC QQSLHFYPWT FG QGTKLEIK RTVAAPSVFIFPPSDEQLKSGTASWCLLNNFYPREAKVQWKVDNA LQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGL SSPVTKS FNRGEC (SEC. ID NO.: 45) Anti-LICAM (Ab5D12) DIQL TQSPSS LSASVGDRVT ITCRASRTIS SYVNWYRQRP GKAPESLIYA ASNLHSGVPS RFSGSGSGTD FTLTISSLQP EDFATYYC QQSLVWYPWT FG QGTKLEIK RTVAAPSVFI FPPSDEQLKSGTASWCLLNNFYPREAKVQWKVDNA LQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGL SSPVTKS FNRGEC (SEC. ID NO.: 20) ΜΛ / / UU JO l A VH domain, or one or more CDRs thereof, described herein, can be linked to a constant domain to form a heavy chain, eg, a full-length heavy chain. Similarly, a VL domain, or one or more CDRs thereof, described herein, can be linked to a constant domain to form a light chain, eg, a full-length light chain. A full length heavy chain and a full length light chain are combined to form a full length antibody. Accordingly, in specific aspects, there is provided herein an antibody comprising a 105 light chain and a heavy chain of antibody, eg, a separate light chain and heavy chain. With respect to the light chain, in a specific aspect, the light chain of an antibody described herein is a kappa light chain. In another specific aspect, the light chain of an antibody described herein is a lambda light chain. In yet another specific aspect, the light chain of an antibody described herein is a human kappa light chain or a human lambda light chain. In a particular aspect, an antibody described herein that specifically binds to an L1CAM polypeptide (eg, human L1CAM), comprises a light chain comprising any VL or VL CDR amino acid sequence described herein, and wherein the light chain constant region comprises the amino acid sequence of a human kappa light chain constant region. In a particular aspect, an antibody described herein that specifically binds to an L1CAM polypeptide (eg, human L1CAM) comprises a light chain comprising VL or VL CDR amino acid sequences described herein, and wherein the light chain constant region comprises the amino acid sequence of a human lambda light chain constant region. Non-limiting examples of human constant region sequences have been described in the art, for example, see US Patent No. 5,693,780 and Kabat 106 EA et al., (1991) mentioned above. With respect to the heavy chain, in some aspects, the heavy chain of an antibody described herein may be an alpha (a), delta (δ), epsilon (ε), gamma (γ), or mu (μ) heavy chain. . In another specific aspect, the heavy chain of an antibody described herein may comprise a human alpha (a), delta (δ), epsilon (ε), gamma (γ) or mu (μ) heavy chain. In one aspect, an antibody described herein that specifically binds to L1CAM (eg, human L1CAM), comprises a heavy chain comprising a VH or VH CDR amino acid sequence described herein, and wherein the heavy chain constant region comprises the amino acid sequence of a human gamma (γ) heavy chain constant region. In another aspect, an antibody described herein, which specifically binds to L1CAM (eg, human L1CAM), comprises a heavy chain comprising a VH or VH CDR amino acid sequence described herein, and wherein the heavy chain constant region comprises the amino acid of a human heavy chain as described herein or known in the art. Non-limiting examples of human constant region sequences have been described in the art, eg see US Patent No. 5,693,780 and Kabat EA et al., (1991) mentioned ΜΛ / / UUOO f ¿ above. 107 In some aspects, an antibody described herein that specifically binds L1CAM (eg, human L1CAM) comprises a VL domain and a VH domain comprising the VH or VH CDRs and the described VL or VL CDRs. herein, and wherein the constant regions comprise the amino acid sequences of the constant regions of an IgG, IgE, IgM, IgD, IgA or IgY immunoglobulin molecule, or an IgG, IgE, IgM, IgD, IgA immunoglobulin molecule or human IgY. In another specific aspect, an antibody described herein that specifically binds to L1CAM (eg, human L1CAM) comprises a VL domain and a VH domain comprising the amino acid sequences described herein, and wherein the constant regions comprise the amino acid sequences of the constant regions of an immunoglobulin molecule IgG, IgE, IgM, IgD, IgA, or IgY, any subclass (for example, IgG1, IgG2, IgG3, IgG4, IgAl, and IgA2) of the constant region immunoglobulin. In some aspects, constant regions comprise the amino acid sequences of the constant regions of a human IgG, which are naturally occurring, including subclasses (eg, IgGl, IgG2, IgG3, or IgG4) and allotypes (eg, Glm , G2m, G3m and nG4m) and their variants. See, for example, Vidarsson G. et al. Front Immunol. 5:520 (published online Oct 20, 2014) ; and Jefferis R. and Lefranc MP, mAbs 1:4, 1-7 (2009). In In some aspects, constant regions comprise the amino acid sequences of the constant regions of a human IgG1, IgG2, IgG3, or IgG4, or variants thereof. In certain aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein, does not have Fe effector functions, eg, complement-dependent cytotoxicity (CDC) and / or antibody-dependent cellular phagocytosis ( ADCP). Effector functions are mediated by the Fe region and the residues closest to the hinge region in the CH2 domain of the Fe region are responsible for the effector functions of antibodies as it contains a largely overlapping binding site for receptors. Clq (complement) and IgG-Fc (FcyR) in effector cells of the innate immune system. In addition, IgG2 and IgG4 antibodies have lower levels of Fe effector functions than IgG1 and IgG3 antibodies. The effector functions of an antibody can be reduced or prevented by different approaches known in the art, including (1) using antibody fragments that lack the Fe region (for example, as a Fab, F(ab')2, Fv single chain (scFv) or an sdAb consisting of a VH or VL monomeric domain); (2) generate aglycosylated antibodies, which can be generated, for example, by removal or alteration of the residue to which the sugar is attached, removal of 109 sugars enzymatically, production of the antibody in cells cultured in the presence of a glycosylation inhibitor, or expression of the antibody in cells incapable of glycosylating proteins (eg, bacterial host cells, see, eg, US publication .#20120100140); (3) employing Fc regions from an IgG subclass that have reduced effector function (for example, an Fc region of IgG2 or IgG4 antibodies or a chimeric Fc region comprising a CH2 domain of IgG2 or IgG4 antibodies, see, for For example, US Publication No. 20120100140 and Lau C. et al J. Immunol. 191:4769-4777 (2013)); and (4) generating an Fe region with mutations that produce reduced or no Fe functions. See, for example, US Publication No. 20120100140 and US and PCT applications cited therein and An et al., mAbs 1:6, 572-579 (2009). Thus, in some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described herein is a Fab, a Fab', an F(ab')2, an Fv, a long-chain Fv single (scFv) or an sdAb consisting of a VH or VL monomeric domain. Such antibody fragments are known in the art and have been described above. In some aspects, the anti-LICAM antibody, or antigen-binding fragment thereof, described in the ΜΛ / / UUOO f ¿ 110 present comprises an Fe region with little or no Fe effector function. In some aspects, the constant regions comprise the amino acid sequences of the Fe region of a human IgG2 or IgG4, in some aspects, the anti-LICAM antibody is of an IgG2 / IgG4 isotype. In some aspects, the anti-LICAM antibody comprises a chimeric Fc region comprising a CH2 domain from an IgG antibody of the IgG4 isotype and a CH3 domain from an IgG antibody of the IgGl isotype, or a chimeric Fc region comprising an IgG2 hinge region and an IgG4 CH2 region, or an Fe region with mutations that produce reduced or no Fe functions. Fe regions with reduced or no Fe effector function include those known in the art. See, for example, Lau C. et al. J. Immunol. 191:4769-4777 (2013); An et al., mAbs 1:6, 572-579 (2009); and US Publication No. 20120100140 and US Patents and Publications and PCT Publications cited therein. One of ordinary skill in the art can easily prepare the Fe regions with reduced or no Fe effector function as well. IV. nucleic acid molecules Another aspect described herein relates to one or more nucleic acid molecules encoding any of the antibodies or antigen-binding fragments thereof described herein. The nucleic acids may be present in whole cells, in a used cell or in a ΜΛ / / UU JO f ¿ 111 substantially pure or partially purified form. A nucleic acid is isolated or rendered substantially pure when it is purified from other cellular components or other contaminants, eg, other nucleic acids (eg, other chromosomal DNA, eg, chromosomal DNA that is bound to DNA isolated in nature ) or cellular proteins, by standard techniques, including alkaline / SDS treatment, CsCl banding, column chromatography, restriction enzymes, agarose gel electrophoresis, and others known in the art. See, F. Ausubel, et al., ed. (1987) Current Protocols in Molecular Biology, Greene Publishing and Wiley Interscience, New York. A nucleic acid described herein may be, for example, DNA or RNA and may or may not contain intronic sequences. In certain aspects, the nucleic acid is a cDNA molecule. The nucleic acids described herein can be obtained using standard molecular biology techniques. For antibodies expressed by hybridomas (eg, hybridomas prepared from transgenic mice carrying human immunoglobulin genes as described further below), cDNAs encoding the heavy and light chains of the antibody carried by the hybridoma can be obtained by standard PCR amplification techniques or cDNA cloning. For the 112 antibodies obtained from an immunoglobulin library (eg, using phage display techniques), nucleic acid encoding the antibody can be recovered from the library. Certain nucleic acid molecules described herein are those encoding the VH and VL sequences of the monoclonal antibody Ab612, Ab4H5, Ab2C2, Ab4H6, Ab5D12. Illustrative DNA sequences encoding the VH sequence of Ab612, Ab4H5, Ab2C2, Ab4H6, Ab5D12 are set forth in SEQ. ID NO.: 8, 14, 16, 18 or 22. Illustrative DNA sequences encoding the VL sequences of Ab612, Ab4H5, Ab2C2, Ab4H6, Ab5D12 are set forth in SEQ. ID NO.: 33, 34, 35, 36 and 37, respectively. ΜΛ / I / UUOO l¿ Table 6: Sequence of Variable Heavy Chain Polynucleotides Anticuerpo Secuencia de polinucleótidos de cadena pesada variable (SEC. ID NO.) Anti-L1CAM (“Ab612”) gaggtgcagctggtggagagcggcggcggcgtggtgcagcccggcggcagcctgagactgagctgcgccgc cagcggcttcaccttcagcagattcggcatgcactgggtgagacaggcccccggcaagggcctggagtgggtg gccttcatcagcaacgagggcagcaacaagtactacgccgacagcgtgaagggcagattcaccatcagcag agacaacagcgccaacaccctgtacctgcagatgaacagcctgagagccgaggacaccgccgtgtactactg cgccagaggcagagcctacggcagcggcagcctgttcgacccctggggccagggcaccctggtgaccgtga gcagc (SEC. ID NO.: 8) Anti-LICAM (“Ab4H5”) gaggtgcagctggtggagagcggcggcggcgtggtgcagcccggcggcagcctgagactgagctgcgccgc cagcggcttcaccttcagcagattcggcatgcactgggtgagacaggcccccggcaagggcctggagtgggtg gccttcatcagcaacgagggcagcaacaagtactacgccgacagcgtgaagggcagattcaccatcagcag 113 agacaacagcgccaacaccctgtacctgcagatgaacagcctgagagccgaggacaccgccgtgtactactg cgccagaggcagagcctacggcagcggcagcctgttcgacccctggggccagggcaccctggtgaccgtga gcagc (SEC. ID NO.: 14) 5 Anti-L1CAM (“Ab2C2”) gaggtgcagctggtggagagcggcggcggcgtggtgcagcccggcggcagcctgagactgagctgcgccgc cagcggcttcaccttcagcagattcggcatgcactgggtgagacaggcccccggcaagggcctggagtgggtg gccttcatcagcaacgagggcagcaacaagtactacgccgacagcgtgaagggcagattcaccatcagcag agacaacagcgccaacaccctgtacctgcagatgaacagcctgagagccgaggacaccgccgtgtactactg cgccagaggcagagcctacggcagcggcagcctgttcgacccctggggccagggcaccctggtgaccgtga gcagc (SEC. ID NO.: 16) 10 15 Anti-LICAM (“Ab4H6”) gaggtgcagctggtggagagcggcggcggcgtggtgcagcccggcggcagcctgagactgagctgcgccgc cagcggcttcaccttcagcagattcggcatgcactgggtgagacaggcccccggcaagggcctggagtgggtg gccttcatcagcaacgagggcagcaacaagtactacgccgacagcgtgaagggcagattcaccatcagcag agacaacagcgccaacaccctgtacctgcagatgaacagcctgagagccgaggacaccgccgtgtactactg cgccagaggcagagcctacggcagcggcagcctgttcgacccctggggccagggcaccctggtgaccgtga gcagc (SEQ. ID NO.: 18) 20 Anti -LICAM (“Ab5D12”) gaggtgcagctggtggagagcggcggcggcgtggtgcagcccggcggcagcctgagactgagctgcgccgc cagcggcttcaccttcagcagattcggcatgcactgggtgagacaggcccccggcaagggcctggagtgggtg gccttcatcagcaacgagggcagcaacaagtactacgccgacagcgtgaagggcagattcaccatcagcag agacaacagcgccaacaccctgtacctgcagatgaacagcctgagagccgaggacaccgccgtgtactactg cgccagaggcagagcctacggcagcggcagcctgttcgacccctggggccagggcaccctggtgaccgtga gcagc (SEC. ID NO.: 22) Tabla 7: variable 114 Secuencia de polinucleótidos de cadena ligera Anticuerpo Secuencia de polinucleótidos de cadena ligera variable (SEC. ID NO.) 5 10 Anti-LICAM (“Ab612”) GACATCCAGCTGACCCAGAGCCCCAGCAGCCTGAGCGCCAGCGTGGGCGA CAGAGTGACCATCACCTGCAGAGCCAGCAGAACCATCAGCAGCTACGTGAA CTGGTACAGACAGAGACCCGGCAAGGCCCCCGAGAGCCTGATCTACGCCG CCAGCAACCTGCACAGCGGCGTGCCCAGCAGATTTAGCGGCAGCGGCAGC GGCACCGACTTCACCCTGACCATCAGCAGCCTGCAGCCCGAGGACTTCGCC ACCTACTACTGCCAGCAGAGCATCGGCAGAGGCCCCGTGACCTTCGGCCAG GGCACCAAGCTGGAGATCAAG (SEC. ID NO.: 33) 15 Anti-LICAM (“Ab4H5”) GACATCCAGCTGACCCAGAGCCCCAGCAGCCTGAGCGCCAGCGTGGGCGA CAGAGTGACCATCACCTGCAGAGCCAGCAGAACCATCAGCAGCTACGTGAA CTGGTACAGACAGAGACCCGGCAAGGCCCCCGAGAGCCTGATCTACGCCG CCAGCAACCTGCACAGCGGCGTGCCCAGCAGATTTAGCGGCAGCGGCAGC GGCACCGACTTCACCCTGACCATCAGCAGCCTGCAGCCCGAGGACTTCGCC ACCTACTACTGCCAGCAGGCCGGCTTCTACACCCCCTGGACCTTCGGCCAG GGCACCAAGCTGGAGATCAAG (SEC. ID NO.: 34) 20 Anti-L1CAM (“Ab2C2”) GACATCCAGCTGACCCAGAGCCCCAGCAGCCTGAGCGCCAGCGTGGGCGA CAGAGTGACCATCACCTGCAGAGCCAGCA GAACCATCAGCAGCTACGTGAA CTGGTACAGACAGAGACCCGGCAAGGCCCCCGAGAGCCTGATCTACGCCG CCAGCAACCTGCACAGCGGCGTGCCCAGCAGATTTAGCGGCAGCGGCAGC GGCACCGACTTCACCCTGACCATCAGCAGCCTGCAGCCCGAGGACTTCGCC ACCTACTACTGCCAGCAGGCCGGCTTCTACTCCCCCTGGACCTTCGGCCAG GGCACCAAGCTGGAGATCAAG (SEC. ID NO.: 35) Anti-L1CAM (“Ab4H6”) GACATCCAGCTGACCCAGAGCCCCAGCAGCCTGAGCGCCAGCGTGGGCGA CAGAGTGACCATCACCTGCAGAGCCAGCAGAACCATCAGCAGCTACGTGAA CTGGTACAGACAGAGAGACCCGGCAAGGCCCCGAGAGCCTGATCTACGCCG CCAGCAACCTGCACAGCGGCGTGCCCGGCAGTAGCCCGGCAGC ΙνΙΛ / / UU JO / ¿ 115 GGCACCGACTTCACCCTGACCATCAGCAGCCTGCAGCCCGAGGACTTCGCC ACCTACTACTGCCAGCAGTCCCTGCACTTCTACCCCTGGACCTTCGGCCAG GGCACCAAGCTGGAGATCAAG (SEC. ID NO.: 36) Anti-LICAM (“Ab5D12”) GACATCCAGCTGACCCAGAGCCCCAGCAGCCTGAGCGCCAGCGTGGGCGA CAGAGTGACCATCACCTGCAGAGCCAGCAGAACCATCAGCAGCTACGTGAA CTGGTACAGACAGAGACCCGGCAAGGCCCCCGAGAGCCTGATCTACGCCG CCAGCAACCTGCACAGCGGCGTGCCCAGCAGATTTAGCGGCAGCGGCAGC GGCACCGACTTCACCCTGACCATCAGCAGCCTGCAGCCCGAGGACTTCGCC ACCTACTACTGCCAGCAGTCCCTGGTGTGGTACCCCTGGACCTTCGGCCAG GGCACCAAGCTGGAGATCAAG (SEC. ID NO.: 37) A method of preparing an anti-LICAM antibody as described herein may comprise expressing the heavy chain and light chains in a cell line comprising the nucleotide sequences encoding the heavy and light chains with a signal peptide. Host cells comprising these nucleotide sequences are included herein. Once the DNA fragments encoding the VH and VL segments are obtained, these DNA fragments can be further manipulated by standard recombinant DNA techniques, for example, to convert variable region genes into antibody chain genes. full length, in Fab fragment genes or in an scFv gene. In these manipulations, a DNA fragment encoding VL or VH is operatively linked to another DNA fragment encoding another protein, such as a 116 antibody constant region or a flexible linker. The term operably linked, as used in this context, is intended to mean that the two DNA fragments are joined in such a way that the amino acid sequences encoded by the two DNA fragments remain in frame. Isolated DNA encoding the VH region can be converted to a full-length heavy chain gene by operably linking the VH-encoding DNA to another DNA molecule encoding heavy chain constant regions (hinge, CH1, CH2, and / or CH3). Human heavy chain constant region gene sequences are known in the art (see, for example, Kabat, E.A., et al., (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242) and DNA fragments spanning these regions can be obtained by standard PCR amplification. The heavy chain constant region may be an IgG1, IgG2, IgG3, IgG4, IgA, IgE, IgM or IgD constant region, eg, an IgG2 and / or IgG4 constant region. For a Fab fragment heavy chain gene, the DNA encoding VH can be operably linked to another DNA molecule encoding only the heavy chain CH1 constant region. Isolated DNA encoding the VL region can 117 can be converted into a full-length light chain gene (as well as a Fab light chain gene) by operatively linking the DNA encoding VL to another DNA molecule encoding the light chain constant region, CL. Human light chain constant region gene sequences are known in the art (see, for example, Kabat, E.A., et al., (1991) Sequences of Proteins of Immunological Interest, Fifth Edition, U.S. Department of Health and Human Services, NIH Publication No. 91-3242) and DNA fragments spanning these regions can be obtained by standard PCR amplification. The light chain constant region may be a kappa or lambda constant region. To create an scFv gene, the DNA fragments encoding VH and VL are operably linked to another fragment encoding a flexible linker, for example, encoding the amino acid sequence (Gly4-Ser)3, such that the sequences of VH and VL can be expressed as a single chain protein, that is, the VL and VH regions joined by the flexible linker (see, for example, Bird et al., (1988) Science 242:423-426; Huston et al. ., (1988) Proc. Nati. Acad. Sci. USA 85:5879-5883; McCafferty et al., (1990) Nature 348:552-554). In some aspects, the present disclosure provides a vector comprising a nucleic acid molecule ΜΛ / / UUOO f ¿ 118 isolate comprising a nucleotide sequence encoding an antibody or antigen-binding fragment thereof. In other aspects, the vectors can be used for gene therapy. Vectors suitable for the description include expression vectors, viral vectors and plasmid vectors. In one aspect, the vector is a viral vector. As used herein, an expression vector refers to any nucleic acid construct that contains the elements necessary for the transcription and translation of an inserted coding sequence, or in the case of an RNA viral vector, the elements necessary for replication and translation, when introduced into a suitable host cell. Expression vectors can include plasmids, phagemids, viruses, and derivatives thereof. Expression vectors of the disclosure may include polynucleotides encoding the antibody, or antigen-binding fragment thereof, described herein. In one aspect, the coding sequences for the antibody, or antigen-binding fragment thereof, are operatively linked to an expression control sequence. As used herein, two nucleic acid sequences are operatively linked when they are covalently linked to allow each component nucleic acid sequence to retain its ΜΛ / / UUOO l 119 functionality. A coding sequence and a gene expression control sequence are said to be operably linked when they are covalently linked to place the expression or transcription and / or translation of the coding sequence under the influence or control of the expression control sequence. genetic. Two DNA sequences are said to be operatively linked if induction of a promoter in the 5' gene expression sequence results in transcription of the coding sequence and if the nature of the linkage between the two DNA sequences (1) it does not introduce a frameshift mutation, (2) it does not interfere with the ability of the promoter region to direct transcription of the coding sequence, nor (3) it interferes with the ability of the corresponding RNA transcript to be translated into a protein. Thus, a gene expression sequence would be operably linked to a coding nucleic acid sequence if the gene expression sequence were capable of effecting transcription of that coding nucleic acid sequence in such a way that the resulting transcript is translated into the desired antibody, or antigen-binding fragment thereof. Viral vectors include, but are not limited to, nucleic acid sequences from the following viruses: retroviruses, such as Moloney murine leukemia virus, 120 Harvey murine sarcoma virus, murine mammary tumor virus and Rous sarcoma virus; lentiviruses; adenovirus, adeno-associated virus; SV40-like virus; polyomavirus; Epstein-Barr virus; papilloma virus; herpes virus; vaccinia virus; polio virus and RNA virus such as a retrovirus. Other vectors known in the art may be used. Certain viral vectors are based on non-cytopathic eukaryotic viruses in which non-essential genes have been replaced by the gene of interest. Non-cytopathic viruses include retroviruses, whose life cycle involves reverse transcription of genomic viral RNA into DNA with subsequent proviral integration into host cellular DNA. Retroviruses have been approved for human gene therapy trials. Those retroviruses that lack replication (ie, capable of directing the synthesis of the desired proteins, but unable to make an infectious particle) are most useful. Genetically altered retroviral expression vectors have general utility for high-efficiency transduction of genes in vivo. Standard protocols for producing non-replicating retroviruses (including the steps of incorporating foreign genetic material into a plasmid, transfecting a packaging cell line with plasmids, producing recombinant retroviruses by the packaging cell line, collecting viral particles from the culture medium 121 cellular and infection of target cells with viral particles) are provided in Kriegler, M., Gene Transfer and Expression, A Laboratory Manual, W.H. Freeman Co., New York (1990) and Murry, E. J., Methods in Molecular Biology, Vol. 7, Humana Press, Inc., Cliffton, N.J. (1991). In one aspect, the virus is an adeno-associated virus, a double-stranded DNA virus. Adeno-associated virus can be genetically engineered to be non-replicating and is capable of infecting a wide variety of species and cell types. In addition, it has such advantages as thermal and lipid solvent stability; high transduction frequencies in cells of various lineages, including hematopoietic cells; and lack of inhibition of superinfection, allowing for multiple sets of transductions. Apparently, adeno-associated virus can integrate into human cellular DNA in a site-specific manner, thus minimizing the possibility of insertional mutagenesis and inserted gene expression variability characteristic of retroviral infection. In addition, wild-type adeno-associated virus infections have been followed in tissue culture for more than 100 passages in the absence of selective pressure, implying that adeno-associated virus genomic integration is a relatively stable event. Adeno-associated virus can also function extrachromosomal. 122 In other aspects, the vector is derived from lentiviruses. In certain aspects, the vector is a recombinant lentivirus vector capable of infecting non-dividing cells. The lentiviral genome and proviral DNA commonly have the three genes found in retroviruses: gag, pol, and env, which are flanked by two long terminal repeat (LTR) sequences. The gag gene encodes the internal structural proteins (matrix, capsid, and nucleocapsid); the pol gene encodes RNA-directed DNA polymerase (reverse transcriptase), a protease, and an integrase; and the env gene encodes the viral membrane glycoproteins. The 5' and 3' LTRs serve to promote virion RNA transcription and polyadenylation. The LTR contains all the cis-acting sequences necessary for viral replication. Lentiviruses have additional genes including vif, vpr, tat, rev, vpu, nef, and vpx (in HIV-I, HIV-2, and / or SIV). Adjacent to the 5' LTR are sequences necessary for reverse transcription of the genome (the tRNA primer binding site) and for efficient packaging of viral RNA into particles (the Psi site). If the sequences necessary for packaging (or packaging of retroviral RNA into infectious virions) are missing from the viral genome, the cis defect prevents packaging of the virus. ΜΛ / / UU JO l 123 genomic RNA. However, the resulting mutation is still capable of directing the synthesis of all virion proteins. The disclosure provides a method of producing a recombinant lentivirus capable of infecting a non-dividing cell, comprising transfecting a suitable host cell with two or more vectors carrying the packaging functions, namely gag, pol and env, as well as also rev and tat. As described herein below, vectors lacking a functional tat gene are suitable for certain applications. Thus, for example, a first vector can provide a nucleic acid encoding a viral gag and a viral pol and another vector can provide a nucleic acid encoding a viral env to produce a packaging cell. Introducing a vector delivering a heterologous gene, identified herein as a transfer vector, into that packaging cell generates a producer cell that releases infectious viral particles carrying the foreign gene of interest. In accordance with the above vector configuration and foreign genes, the second vector can provide a nucleic acid encoding a viral envelope (env) gene. The env gene can be derived from almost any suitable virus, including retroviruses. In ΜΛ / / UU JO l¿ In some respects, the env protein is an amphotropic envelope protein that allows for transduction of cells from humans and other species. Examples of retroviral derived env genes include, but are not limited to: Moloney murine leukemia virus (MoMuLV or MMLV), Harvey murine sarcoma virus (HaMuSV or HSV), murine mammary tumor virus (MuMTV or MMTV), gibbon leukemia virus (GaLV or GALV), human immunodeficiency virus (HIV) and Rous sarcoma virus (RSV). Other env genes such as the vesicular stomatitis virus (VSV) G protein (VSV G) of hepatitis and influenza viruses may also be used. The vector providing the viral env nucleic acid sequence is operably associated with regulatory sequences described elsewhere herein. Examples of lentiviral vectors are described in WO9931251, W09712622, W09817815, W09817816 and WO9818934, which are incorporated herein by reference in their entirety. Other vectors include plasmid vectors. Plasmid vectors have been widely described in the art and are known to those skilled in the art. See, for example, Sambrook et al., Molecular Cloning: A Laboratory Manual, Second Edition, Cold Spring Harbor Laboratory Press, 1989. In recent years, it has been discovered that vectors ΜΛ / / UUOO f ¿ 125 plasmids are particularly advantageous for delivering genes to cells in vivo due to their inability to replicate within or integrate with a host genome. However, these plasmids, having a promoter compatible with the host cell, can express a peptide from a gene operably encoded within the plasmid. Some commonly used plasmids available from commercial vendors include pBR322, pUC18, pUC19, various pcDNA plasmids, pRC / CMV, various pCMV plasmids, pSV40, and pBlueScript. Additional examples of specific plasmids include pcDNA3.1, catalog number V79020; pcDNA3.1 / hygro, catalog number V87020; pcDNA4 / myc-His, catalog number V86320 and pBudCE4.1, catalog number V53220, all from Invitrogen (Carlsbad, CA.). Other plasmids are known to those skilled in the art. In addition, plasmids can be custom designed using standard molecular biology techniques to remove and / or add specific DNA fragments. V. Antibody Production Antibodies, or fragments thereof, that immunospecifically bind to L1CAM (eg, human LIGAN) can be produced by any method known in the art for the synthesis of antibodies, for example, by chemical synthesis or by expression techniques. ΜΛ / / UU JO f ¿ 126 recombinant. The methods described herein employ, unless otherwise indicated, standard techniques in molecular biology, microbiology, genetic analysis, recombinant DNA, organic chemistry, biochemistry, PCR, oligonucleotide synthesis and modification, nucleic acid hybridization, and related fields. within the knowledge of the art. These techniques are described, for example, in the references cited herein and fully explained in the literature. See, for example, Maniatis T et al., (1982) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press; Sambrook J et al., (1989), Molecular Cloning: A Laboratory Manual, Second Edition, Cold Spring Harbor Laboratory Press; Sambrook J et al., (2001) Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY; Ausubel FM et al., Current Protocols in Molecular Biology, John Wiley & Sons (1987 and annual updates); Current Protocols in Immunology, John Wiley & Sons (1987 and annual updates) Gait (ed.) (1984) Oligonucleotide Synthesis: A Practical Approach, IRL Press; Eckstein (ed.) (1991) Oligonucleotides and Analogues: A Practical Approach, IRL Press; Birren B et al., (eds.) (1999) Genome Analysis: A Laboratory Manual, Cold Spring Harbor Laboratory Press. In a specific aspect, an antibody described herein is an antibody (eg, antibody ΜΛ / / UU JO f ¿ 127 monoloclonal) prepared, expressed, created, or isolated by any means involving creation, eg, by synthesis, genetic modification of DNA sequences. In certain aspects, the antibody comprises sequences (eg, DNA sequences or amino acid sequences) that do not occur naturally in the germline repertoire of antibodies of an animal or mammal (eg, human) in vivo. In a certain aspect, provided herein is a method of preparing an antibody, or antigen-binding fragment thereof, that immunospecifically binds to L1CAM (eg, human L1CAM), comprising culturing a cell or host cell described at the moment. In a certain aspect, provided herein is a method of making an antibody, or antigen-binding fragment thereof, that immunospecifically binds to L1CAM (eg, human L1CAM), comprising expressing (eg, recombinant expression ) the antibody, or antigen-binding fragment thereof, using a cell or host cell described herein (eg, a cell or host cell comprising polynucleotides encoding an antibody described herein). In a particular aspect, the cell is an isolated cell. In a particular aspect, the exogenous polynucleotides were introduced into the cell. In a particular aspect, the method comprises ΜΛ / I / UU JO (¿ 128 furthermore the step of purifying the antibody, or antigen-binding fragment thereof, obtained from the host cell or cell. Methods for producing polyclonal antibodies are known in the art (see, for example, Chapter 11 in: Short Protocols in Molecular Biology, (2002) 5.aed., Ausubel FM et al., Eds., John Wiley and Sons, NY) Monoclonal antibodies can be prepared using a wide variety of techniques known in practice, including the use of hybridoma, recombinant, and phage display technologies, or a combination of these. For example, monoclonal antibodies can be produced using hybridoma techniques, including those known in the art and described, for example, in Harlow E & Lane D, Antibodies: A Laboratory Manual, (Coid Spring Harbor Laboratory Press, 2nd ed. 1988 ); Hammerling GJ et al., in: Monoclonal Antibodies and T-Cell Hybridomas 563-681 (Elsevier, N.Y., 1981). The term monoclonal antibody, as used herein, is not limited to antibodies produced by hybridoma technology. For example, monoclonal antibodies can be produced recombinantly from host cells that exogenously express an antibody described herein or a fragment thereof, eg, light chain and / or heavy chain of the antibody. ΜΛ / / UU JO f ¿ 129 In specific aspects, a monoclonal antibody, as used herein, is an antibody produced by a single cell (eg, hybridoma or host cell that produces a recombinant antibody), wherein the antibody immunospecifically binds to L1CAM (eg, , human L1CAM) as determined, for example, by ELISA or other antigen binding or competitive binding assay known in the art or in the Examples provided herein. In particular aspects, the monoclonal antibody can be a chimeric antibody or a humanized antibody. In certain aspects, a monoclonal antibody is a monovalent antibody or a multivalent (eg, bivalent) antibody. In particular aspects, a monoclonal antibody is a monospecific or multispecific (eg, bispecific) antibody. The monoclonal antibodies described herein can be prepared, for example, by the hybridoma method as described in Kohler G & Milstein C (1975) Nature 256: 495 or can, for example, be isolated from phage libraries using the techniques described. in the present, for example. Other methods for the preparation of clonal cell lines and monoclonal antibodies expressed therewith are known in the art (see, eg, Chapter 11 in: Short Protocols in Molecular Biology, (2002) 5.aed., Ausubel EM et al., mentioned above). Methods for producing and screening for antibodies Specific 130 through the use of hybridoma technology are common and known in the art. For example, in the hybridoma method, a mouse or other suitable host animal, such as a sheep, goat, rabbit, rat, hamster, or macaque monkey, is immunized to obtain lymphocytes that produce or are capable of producing antibodies. that specifically bind to the protein (eg, human LIGAN) used for immunization. Alternatively, lymphocytes can be immunized in vitro. The lymphocytes are then fused with myeloma cells using a suitable fusion agent, such as polyethylene glycol, to form a hybridoma cell (Goding JW (Ed), Monoclonal Antibodies: Principles and Practice, pp. 59-103 (Academic Press, 1986)). Additionally, a RIMMS (repetitive multiple immunization site) technique can be used to immunize an animal (Kilpatrick KE et al., (1997) Hybridoma 16:381-9, which is incorporated herein in its entirety by reference). In some aspects, mice (or other animals, such as chickens, rats, monkeys, donkeys, pigs, sheep, hamsters, or dogs) can be immunized with an antigen (eg, LIGAN, like human LIGAN) and, a Once an immune response is detected, eg, antibodies specific for the antigen are detected in the mouse serum, the spleen is removed from the mouse and the splenocytes are isolated. Then the z / Qenn / Lznz / q / Yi 131 splenocytes are fused by known techniques with any suitable myeloma cell, eg, cells of the SP20 cell line available from the American Type Culture Collection (ATCC) (Manassas, VA), to form hybridomas. Hybridomas are selected and cloned by limited dilution. In certain aspects, lymph nodes from immunized mice are removed and fused with NSO myeloma cells. The hybridoma cells thus prepared are grown in a suitable medium, preferably with one or more substances that inhibit the growth or survival of the original unfused myeloma cells. For example, if the parent myeloma cells lack the enzyme hypoxanthine guanine phosphoribosyltransferase (HGPRT or HPRT), culture medium for hybridomas will commonly include hypoxanthine, aminopterin, and thymidine (HAT medium), substances that prevent growth of HGPRT-deficient cells. Specific aspects employ myeloma cells that fuse efficiently, support stable high-level production of antibody by the selected antibody-producing cells, and are sensitive to a medium such as HAT medium. Among these myeloma cell lines are murine myeloma lines, such as the NSO cell line or those derived from MOPC-21 mouse tumors. 132 and MPC-11, available from Salk Institute Cell Distribution Center, San Diego, CA, USA and SP-2 or X63-Ag8.653 cells available from American Type Culture Collection, Rockville, MD, USA. Human myeloma and mouse-human heteromyeloma cell lines have also been described for the production of human monoclonal antibodies (Kozbor D (1984) J Immunol 133: 3001-5; Brodeur et al., Monoclonal Antibody Production Techniques and Applications, pp. 51-63 (Marcel Dekker, Inc., New York, 1987)). The culture medium in which the hybridoma cells are grown is assayed for producing monoclonal antibodies directed against L1CAM (eg, human L1CAM). The binding specificity of the monoclonal antibodies produced by the hybridoma cells is determined using methods known in the art, for example, immunoprecipitation or by an in vitro binding assay, such as a radioimmunoassay (RIA) or a linked immunosorbent assay. enzymes (ELISA). After identification of hybridoma cells that produce antibodies of the desired specificity, affinity, and / or activity, clones can be subcloned using limiting dilution procedures and grown using standard methods (Goding JW (Ed), Monoclonal Antibodies: Principles and Practice, mentioned z / Qenn / Lznz / q / Yi 133 above). Suitable culture medium for this purpose includes, for example, D-MEM or RPMI 1640 medium. In addition, hybridoma cells can be grown in vivo as ascites tumors in an animal. The monoclonal antibodies secreted by the subclones are suitably separated from the culture medium, ascites fluid, or serum by standard immunoglobulin purification procedures, such as, for example, protein A-Sepharose, hydroxylapatite chromatography, gel electrophoresis, dialysis or affinity chromatography. The antibodies described herein include antibody fragments that recognize specific L1CAM (eg, human L1CAM) and can be generated by any method known to those skilled in the art. For example, the Fab and F(ab')2 fragments described herein can be produced by proteolytic cleavage of immunoglobulin molecules, using enzymes such as papain (to produce Fab fragments) or pepsin (to produce F(ab')2 fragments). ) . A Fab fragment corresponds to one of two identical arms of an antibody molecule and contains the complete light chain paired with the heavy chain VH and CH1 domains. An F(ab')2 fragment contains the two antigen-binding arms of an antibody molecule linked by disulfide bonds at the hinge region. z / Qenn / Lznz / q / Yi 134 In one aspect, to generate complete antibodies, PCR primers that include VH or VL nucleotide sequences, a restriction site, and a flanking sequence to protect the restriction site can be used to amplify the VH or VL sequences from from a mold, p. g., scFv clones. Using cloning techniques known to those skilled in the art, PCR-amplified VH domains can be cloned into vectors expressing a VH constant region and PCR-amplified VL domains can be cloned into vectors expressing a VH constant region. VL constant, e.g. eg, human kappa or lambda constant regions. The VH and VL domains can also be cloned into a vector expressing the necessary constant regions. Heavy chain conversion vectors and light chain conversion vectors are then co-transfected into cell lines to generate stable or transient cell lines expressing full-length antibodies, e.g. g ., IgG, using techniques known to those skilled in the art. A chimeric antibody is a molecule in which different antibody fragments are derived from different immunoglobulin molecules. For example, a chimeric antibody may contain a variable region from a non-human animal (eg, mouse, rat, or chicken) monoclonal antibody fused to a constant region from a z / Qenn / Lznz / q / Yi antibody. 135 human. Methods for producing chimeric antibodies are known in the art. See, for example, Morrison SL (1985) Science 229: 1202-7; Oi VT & Morrison SL (1986) BioTechniques 4: 214-221; Gillies SD et al., (1989) J Immunol Methods 125: 191-202; and US Patent Nos. 5,807,715, 4,816,567, 4,816,397, and 6,331,415. A humanized antibody can bind to a predetermined antigen and comprises a framework region having substantially the amino acid sequence of a human immunoglobulin and CDRs having substantially the amino acid sequence of a non-human immunoglobulin (eg, a murine immunoglobulin or of chicken). In particular aspects, a humanized antibody also comprises at least one fragment of an immunoglobulin (Fe) constant region, typically that of a human immunoglobulin. The antibody may also include the CH1, hinge, CH2, CH3, and CH4 regions of the heavy chain. A humanized antibody can be selected from any class of immunoglobulins, including IgM, IgG, IgD, IgA, and IgE, and any isotype, including IgG1, IgG2, IgG3, and IgG4. Humanized antibodies can be produced using a variety of techniques known in the art, including, but not limited to, CDR grafting (European Patent No. EP 239400; International Publication No. WO 91 / 09967; and US Patents 5,225,539, 5,530,101, and 5,585,089), z / Qenn / Lznz / q / Yi 136 coating or surface restoration (European patents no. EP 592106 and EP 519596; Padlan EA (1991) Mol Immunol 28(4 / 5): 489-498; Studnicka GM et al., (1994) Prot Engineering 7(6 ): 805-814 and Roguska MA et al., (1994) PNAS 91: 969-973), chain shuffling (US Patent No. 5,565,332), and techniques described in, for example, the patent US Patent No. 6,407,213, US Patent No. 5,766,886, International Publication No. WO 93 / 17105; Tan P et al., (2002) J Immunol 169: 1119-25; Caldas C et al., (2000) Proteln Eng. 13(5): 353-60; Morea V et al., (2000) Methods 20(3) : 267-79; Baca M et al., (1997) J Biol Chem 272(16): 10678-84; Roguska MA et al., (1996) Proteln Eng 9(10) : 895 904; Couto JR et al., (1995) Cancer Res. 55 (23 Supp): 5973s-5977s; Couto JR et al., (1995) Cancer Res 55(8): 1717-22; Sandhu JS (1994) Gene 150(2): 409-10 and Pedersen JT et al., (1994) J Mol Biol 235(3): 959-73. See also US Application Publication No. 2005 / 0042664 AI (February 24, 2005), which is incorporated herein in its entirety by reference. Methods for producing multispecific antibodies (eg, bispecific antibodies) have been described. See, for example, US Patent Nos. 7,951,917; 7,183,076; 8,227,577; 5,837,242; 5,989,830; 5,869,620; 6,132,992 and 8,586,713. Single domain antibodies, eg zjQenn / Lznz / q / Yi 137 antibodies lacking light chains, can be produced by methods known in the art. See Riechmann L & Muyldermans S (1999) J Immunol 231: 25-38; Nuttall SD et al., (2000) Curr Pharm Biotechnol 1(3): 253-263; Muyldermans S, (2001) J Biotechnol 74(4): 277-302; US patent #6,005,079; and International Publication Nos. WO 94 / 04678, WO 94 / 25591 and WO 01 / 44301. In addition, antibodies that immunospecifically bind to an L1CAM antigen can, in turn, be used to generate anti-idiotype antibodies that mimic an antigen using techniques known to those skilled in the art. (See, for example, Greenspan NS & Bona CA (1989) FASEB J 7(5): 437-444; and Nissinoff A (1991) J Immunol 147(8): 2429-2438). In particular aspects, an antibody described herein that binds to the same epitope of L1CAM (eg, human L1CAM) as an anti-LICAM antibody described herein is a human antibody or an antigen-binding fragment thereof. . In particular aspects, an antibody described herein, which competitively (eg, in a dose-dependent manner) blocks the antibodies described herein (eg, Ab612, Ab4H5, Ab2C2, Ab4H6, and Ab5D12) to that do not bind to L1CAM (eg, human L1CAM), is a human antibody or an antigen-binding fragment thereof. z / Qenn / Lznz / q / Yi 138 Human antibodies can be produced using any method known in the art. For example, transgenic mice that cannot express functional endogenous immunoglobulins, but can express human immunoglobulin genes, can be used. In particular, human heavy and light chain immunoglobulin gene complexes can be introduced randomly or by homologous recombination into mouse embryonic stem cells. Alternatively, the human variable region, constant region, and diversity region can be introduced into mouse embryonic stem cells in addition to the human heavy and light chain genes. Mouse heavy and light chain immunoglobulin genes can be rendered separately or simultaneously infunctional with the introduction of human immunoglobulin loci by homologous recombination. In particular, homozygous deletion of the JH region prevents the production of endogenous antibodies. The modified embryonic stem cells are expanded and microinjected into blasts to produce chimeric mice. The chimeric mice are then crossed to produce homozygous offspring that express human antibodies. Transgenic mice are immunized in the traditional manner with a selected antigen, e.g. eg, all or a fragment of an antigen (eg, L1CAM). Monoclonal antibodies directed against the antigen are z / Qenn / Lznz / q / Yi 139 can be obtained from immunized and transgenic mice using conventional hybridoma technology. Human immunoglobulin transgenes found in transgenic mice are rearranged during B-lymphocyte differentiation and subsequently undergo class switching and somatic mutation. Therefore, using this technique, it is possible to produce therapeutically useful IgG, IgA, IgM and IgE antibodies. For a summary of this technology for the production of human antibodies, see Lonberg N & Huszar D (1995) Int Rev Immunol 13 :65-93. For a detailed description of this human antibody and human monoclonal antibody production technology and protocols for the production of the antibodies see, for example, International Publication Nos. WO 98 / 24893, WO 96 / 34096 and WO 96 / 33735 and US Patent Nos. 5,413,923, 5, 625,126, 5, 633,425, 5, 569, 825, 5, 661, 016, 5, 545, 806, 5, 814,318, and 5,939, 598. Examples of mice that can produce human antibodies include XENOMOUSE™ (Abgenix, Inc.; US Patent Nos. 6,075,181 and 6,150,184), HUAB-MOUSE” (Mederex, Inc. / Gen Pharm; US Patent Nos. 5,545,806 and 5,569,825), TRANS CHROMO MOUSE (Kirin) and KM MOUSE (Medarex / Kirin). Human antibodies that specifically bind to L1CAM (eg, human L1CAM) can be produced by a variety of methods known in the art, including z / Qenn / Lznz / q / Yi 140 phage display methods described above, using antibody libraries derived from human immunoglobulin sequences. See also US Patent Nos. 4,444,887, 4,716,111, and 5,885,793; and International Publication Nos. WO 98 / 46645, WO 98 / 50433, WO 98 / 24893, WO 98 / 16654, WO 96 / 34096, WO 96 / 33735, and WO 91 / 10741. In some aspects, human antibodies can be produced through the use of mouse-human hybridomas. For example, Epstein-Barr virus (EBV)-transformed human peripheral blood lymphocytes can be fused with mouse myeloma cells to produce mouse-human hybridomas that secrete human monoclonal antibodies, and these mouse-human hybridomas can be assay to determine which secrete human monoclonal antibodies that immunospecifically bind to a target antigen (eg, L1CAM, such as human L1CAM). Methods are known and described in the art, see, for example, Shinmoto H et al., (2004) Cytotechnology 46: 19-23; Naganawa Y et al., (2005) Human Antibodies 14: 27-31. SAW. γ cell vectors In certain aspects, provided herein are cells (eg, host cells) with expression (eg, recombinantly) of antibodies described herein (or an antigen-binding fragment thereof) that are specifically bind LICAM (eg, human L1CAM) and z / Qenn / Lznz / q / Yi 141 polynucleotides and related expression vectors. Provided herein are vectors (eg, expression vectors) comprising polynucleotides comprising nucleotide sequences encoding anti-LICAM antibodies or a fragment for recombinant expression in host cells, e.g. g ., mammalian cells. Also provided herein are host cells comprising the vectors for recombinant expression of anti-LICAM antibodies described herein (eg, human or humanized antibody). In a particular aspect, provided herein are methods of producing an antibody described herein, comprising expressing the antibody from a host cell. Recombinant expression of an antibody described herein (eg, a full-length antibody, heavy and / or light chain antibody, or a single chain antibody described herein) that specifically binds to L1CAM (eg, human L1CAM) involves the construction of an expression vector containing a polynucleotide encoding the antibody. Once a polynucleotide encoding an antibody molecule, an antibody heavy and / or light chain, or fragment thereof (eg, heavy and / or light chain variable domains) has been obtained, the vector can be produced. for the production of the antibody molecule using technology ΜΛ / / UUOO l 142 of recombinant DNA using methods known in the art. Thus, described herein are methods for preparing a protein by expressing a polynucleotide containing an antibody, or antibody fragment (eg, light chain and / or heavy chain), encoding sequences of nucleotides. Methods known to those skilled in the art can be used to construct expression vectors containing antibody or antibody fragment coding sequences (eg, heavy chain or light chain) and appropriate transcriptional and translational control signals. These methods include, for example, in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination. Also provided are replicable vectors comprising a nucleotide sequence encoding an antibody molecule described herein, an antibody heavy chain or light chain, an antibody heavy or light chain variable domain or fragment thereof, or a Heavy or light chain CDR operatively linked to a promoter. Vectors, for example, can include the nucleotide sequence encoding the constant region of the antibody molecule (see, for example, International Publication Nos. WO 86 / 05807 and WO 89 / 01036 and US Pat. US No. 5, 122, 464) and antibody variable domains can be cloned into the vector for expression of z / Qrnn / Lznz / q / Yi 143 the complete heavy chain, the complete light chain or both the complete heavy chain and the complete light chain. An expression vector can be transferred into a cell (eg, host cell) by standard techniques and the resulting cells can be cultured by standard techniques to produce an antibody described herein (eg, an antibody comprising the VH and / or VL, or one or more of the VH and / or VL CDRs, of Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12) or a fragment thereof. Thus, provided herein are host cells that contain a polynucleotide encoding an antibody described herein or fragments thereof, or a heavy or light chain thereof, or fragment thereof, or a single chain antibody described herein. herein, operatively linked to a promoter for expression of the sequences in the host cell. In certain aspects, for the expression of double chain antibodies, vectors encoding both the heavy and light chains, individually, can be expressed together in the host cell for expression of the complete immunoglobulin molecule, as described details below. In certain aspects, a host cell contains a vector comprising a polynucleotide encoding both the heavy chain and light chain of an antibody described herein, or a fragment thereof. In aspects z / Qenn / Lznz / q / Yi 144 specific, a host cell contains two distinct vectors, a first vector comprising a polynucleotide encoding a heavy chain or heavy chain variable region of an antibody described herein, or a fragment thereof, and a second vector comprising a polynucleotide encoding a light chain or light chain variable region of an antibody described herein, or a fragment thereof. In other aspects, a first host cell comprises a first vector comprising a polynucleotide encoding a heavy chain or heavy chain variable region of an antibody described herein, or fragment thereof, and a second host cell comprises a second vector. comprising a polynucleotide encoding a light chain or light chain variable region of an antibody described herein. In specific aspects, a heavy chain / heavy chain variable region expressed by a first cell is associated with a light chain / light chain variable region of a second cell to form an anti-LICAM antibody described herein or a ligation fragment. to its antigen. In certain aspects, a host cell population is provided herein comprising the first host cell and the second host cell. In a particular aspect, a population of vectors is provided herein comprising a first vector that z / Qenn / Lznz / q / Yi 145 comprises a polynucleotide encoding a light chain / light chain variable region of an anti-LICAM antibody described herein and a second vector comprising a polynucleotide encoding a heavy chain / heavy chain variable region of an anti-LICAM antibody described herein. A variety of host expression vector systems can be used to express the antibody molecules described herein. Host expression systems represent vehicles by which the coding sequences of interest can be produced and subsequently purified, but they also represent cells that, when transformed or transfected with the appropriate nucleotide coding sequences, can express a described antibody molecule. in the present in situ. These include, but are not limited to, microorganisms such as bacteria (eg, E. coli and B. subtilis) transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing antibody coding sequences; yeast (eg, Saccharomyces Pichia) transformed with recombinant yeast expression vectors containing antibody coding sequences; insect cell systems infected with recombinant virus expression vectors (eg baculovirus) containing z / Qenn / Lznz / q / Yi sequences 146 encoding antibodies; plant cell systems (eg, green algae such as Chlamydomonas reinhardtii) infected with recombinant virus expression vectors (eg, cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV ( for its acronym in English)) or transformed with recombinant plasmid expression vectors (eg, Ti plasmid) containing antibody coding sequences; or mammalian cell systems (eg COS (eg COSI or COS), CHO, BHK, MDCK, HEK 293, NSO, PER.C6, VERO, CRL7030, HsS78Bst, HeLa, NIH 3T3, HEK-293T cells , HepG2, SP210, Rl.l, B-W, L-M, BSC1, BSC40, YB / 20, SP2 / 0, Sf9, human lymphoblastoids, NSO, bow melanoma, HT-1080, PERC.6 and BMT10) harboring constructs of recombinant expression containing promoters derived from the genome of mammalian cells (eg, metallothionein promoter) or from mammalian viruses (eg, the adenovirus late promoter; the vaccinia virus 7.5K promoter). In a specific aspect, the cells for expression of the antibodies described herein, or an antigen-binding fragment thereof, are CHO cells, eg, CHO cells from CHO GS SYSTEM™ (Lonza). In a particular aspect, the cells for expressing antibodies described herein are human cells, eg, human z / Qenn / Lznz / q / Yi cell lines. In a specific aspect, a vector of 147 mammalian expression is POPTIVEC™ or pcDNA3.3. In a particular aspect, bacterial cells such as Escherichia coli, or eukaryotic cells (eg, mammalian cells), especially for full length recombinant antibody molecule expression, are used for expression of a recombinant antibody molecule. For example, mammalian cells, such as Chinese hamster ovary (CHO) cells, together with a vector such as the human cytomegalovirus major intermediate early gene promoter element, are an efficient expression system for antibodies (Foecking MK & Hofstetter H (1986) Gene 45: 101-5 and Cockett MI et al., (1990) Blotechnology 8(7): 662-7). In certain aspects, the antibodies described herein are produced by CHO cells or NSO cells. In a specific aspect, the expression of nucleotide sequences encoding antibodies described herein that bind immunospecifically to L1CAM (eg, human L1CAM) is regulated by a constitutive promoter, inducible promoter, or tissue-specific promoter. In bacterial systems, various expression vectors can be advantageously selected depending on the intended use of the antibody molecule being expressed. For example, when a large amount of the antibody must be produced, for the generation of pharmaceutical compositions from a molecule of z / Qenn / Lznz / q / Yi 148 antibody, vectors that direct the expression of high levels of fusion protein products that are easily purified may be convenient. Such vectors include, but are not limited to, the E. coli expression vector pUR278 (Ruether U & Mueller-Hill B (1983) EMBO J 2: 1791-1794), into which the antibody coding sequence can be ligated individually in-frame the vector with the lac Z coding region such that a fusion protein is produced; pIN vectors (Inouye S & Inouye M (1985) Nuc Acids Res 13: 3101-3109; Van Heeke G & Schuster SM (1989) J Biol Chem 24: 5503-5509); and the like. For example, pGEX vectors can also be used to express foreign polypeptides as glutathione 5-transferase (GST) fusion proteins. In general, such fusion proteins are soluble and can be readily purified from used cells by adsorption and binding to a matrix of agarose-glutathione microspheres, followed by elution in the presence of free glutathione. pGEX vectors are designed to include thrombin or factor Xa protease cleavage sites so that the cloned target gene product can be released from the GST moiety. In an insect system, Autographa californica nuclear polyhedrosis virus (AcNPV) can be used, for example, as a vector to express foreign genes. The virus grows in Spodoptera z / Qenn / Lznz / q / Yi cells 149 frugiperda. The antibody coding sequence can be individually cloned into non-essential regions (eg, the polyhedrin gene) of the virus and placed under the control of an AcNPV promoter (eg, the polyhedrin promoter). In mammalian host cells, a variety of virus-based expression systems can be used. In cases where an adenovirus is used as the expression vector, the antibody coding sequence of interest can be ligated to an adenovirus transcriptional / translational control complex, e.g. eg, the late promoter and tripartite leader sequence. This chimeric gene can then be inserted into the adenovirus genome by recombination in vitro or in vivo. Insertion into a non-essential region of the viral genome (eg, the El or E3 region) will result in a recombinant virus that is viable and capable of expressing the antibody molecule in infected hosts (for example, see Logan J & Shenk T (1984) PNAS 81(12): 3655-9). Specific initiation signals may also be required for efficient translation of inserted antibody coding sequences. These signals include the ATG initiation codon and adjacent sequences. Additionally, the initiation codon must be in frame with the reading frame of the desired coding sequence to ensure translation of the entire insert. These z / Qenn / Lznz / q / Yi codons 150 initiation and control signals of exogenous translation can have various origins, both natural and synthetic. The efficiency of expression can be enhanced by the inclusion of appropriate transcriptional enhancer elements and transcriptional terminators, etc. (see, for example, Bitter G et al., (1987) Methods Enzymol. 153: 516-544). Additionally, a host cell strain may be chosen that modulates the expression of the inserted sequences or that modifies and processes the gene product in the specific manner desired. Such modifications (eg glycosylation) and processing (eg cleavage) of protein products may be important for the function of the protein. Different host cells have characteristic and specific mechanisms for the post-translational processing and modification of proteins and gene products. Appropriate cell lines or host systems can be chosen to ensure correct modification and processing of the expressed foreign protein. For this purpose, eukaryotic host cells that possess the cellular machinery for the correct processing of the major transcription, glycosylation, and phosphorylation of the gene product can be used. Mammalian host cells include, but are not limited to, CHO, SKOV-3, B16-F1, NCI-H522, VERO, BHK, Hela, MDCK, 151 ΗΕΚ 293, NIH 3Τ3, W138, ΒΤ483, Hs578T, ΗΤΒ2, ΒΤ20 and T47D, NSO (a murine myeloma cell line that does not endogenously produce any immunoglobulin chains), CRL7030, COS (eg, COS 1 or COS) , PER.C6, VERO, HsS78Bst, HEK-293T, HepG2, SP210, R1. 1, B-W, L-M, BSC1, BSC40, YB / 20, BMT10 and HsS78Bst. In certain aspects, the anti-LICAM antibodies described herein are produced in mammalian cells, such as CHO cells. In a specific aspect, the antibodies described herein, or antigen-binding fragments thereof, have reduced or no fucose content. Such antibodies can be produced using techniques known to one skilled in the art. For example, antibodies can be expressed in cells deficient or unable to fucosylate. In a specific example, cell lines with a knockout of both 1,6-fucosyltransferase alleles can be used to produce antibodies or antigen-binding fragments thereof with lower fucose content. The POTELLIGENT® system (Lonza) is an example of a system that can be used to produce antibodies, or antigen-binding fragments thereof, with lower fucose content. For long-term, high-yield production of recombinant proteins, stable expression cells can be generated. For example, you can design ΜΛ / / UUOO l 152 genetically engineered cell lines that stably express an anti-LICAM antibody described herein, or an antigen-binding fragment thereof. In specific aspects, a cell provided herein stably expresses a light chain / light chain variable domain and a heavy chain / heavy chain variable domain that associate to form an antibody described herein, or a ligation fragment. to its antigen. In certain aspects, instead of using expression vectors that contain viral origins of replication, host cells can be transformed with DNA controlled by appropriate expression control elements (eg, promoter, enhancer, sequences, transcription terminators, polyadenylation sites, etc.) and a selectable marker. After introducing the foreign DNA / polynucleotide, the genetically modified cells can be allowed to grow for 1-2 days in enriched medium, and then switched to selective medium. The selectable marker on the recombinant plasmid confers resistance to selection and allows cells to stably integrate the plasmid into their chromosomes and grow to form foci that can, in turn, be cloned and expanded into cell lines. This method can be used to advantage to genetically engineer cell lines that express an anti-LICAM antibody described herein, or 153 an antibody-binding fragment of this. These genetically modified cell lines may be particularly useful for screening and evaluating compositions that directly or indirectly interact with the antibody molecule. A variety of selection systems can be used, including, but not limited to, herpes simplex virus thymidine kinase genes (Wigler M et al., (1977) Cell 11(1): 223-32), hypoxanthine guanine phosphoribosyltransferase (Szybalska EH & Szybalski W (1962) PNAS 48(12): 2026-2034) and adenine phosphoribosyltransferase (Lowy I et al., (1980) Cell 22(3): 817-23), which can be used in cells tk, hgprt, or aprt, respectively. Furthermore, resistance to antimetabolites can be used as the basis of selection for the following genes: dhfr, which confers resistance to methotrexate (Wigler M et al., (1980) PNAS 77(6): 3567-70; O'Hare K et al., (1981) PNAS 78: 1527-31); gpt, which confers resistance to mycophenolic acid (Mulligan RC & Berg P (1981) PNAS 78(4): 2072-6); neo, which confers resistance to the aminoglycoside G-418 (Wu GY & Wu OH (1991) Biotherapy 3: 87-95; Tolstoshev P (1993) Ann Rev Pharmacol Toxicol 32: 573-596; Mulligan RC (1993) Science 260: 926 -932; and Morgan RA & Anderson WF (1993) Ann Rev Biochem 62: 191-217; Nabel GJ & Feigner PL (1993) Trends Biotechnol 11(5): 211-5); and hygro, which confers resistance to hygromycin (Santerre RF et 154 al., (1984) Gene 30(1-3): 147-56). Recombinant DNA technology methods commonly known in the art can be routinely applied to select the desired recombinant clone and the methods are described, for example, in Ausubel FM et al., (eds.), Current Protocols in Molecular Biology , John Wiley & Sons, NY (1993); Kriegler M, Gene Transfer and Expression, A Laboratory Manual, Stockton Press, NY (1990); and in Chapters 12 and 13, Dracopoli NC et al., (eds.), Current Protocols in Human Genetics, John Wiley & Sons, NY (1994); Colbere-Garapin F et al., (1981) J Mol Biol 150: 1-14, which are incorporated in their entireties herein by reference. In some aspects, the antibody, or antigen-binding fragment thereof, of the present disclosure may be expressed in an immune cell, eg, a T cell and / or NK cell. In some aspects, the antibody, or antigen-binding fragment thereof, can be expressed as a chimeric antigen receptor (CAR). A CAR-T cell is a T lymphocyte that expresses a chimeric antigen receptor. The phrase chimeric antigen receptor (CAR), as used herein, refers to a recombinant fusion protein having an antigen-specific extracellular domain (or ectodomain) coupled to an intracellular domain that directs the cell to carry perform a specialized function ΜΛ / / UU JO f ¿ 155 after binding an antigen to the extracellular domain. Chimeric antigen receptors are distinguished from other antigen-binding agents by their ability to bind MHC-independent antigens and transduce activation signals via their intracellular domain. In some aspects, the antigen-specific extracellular domain of a chimeric antigen receptor specifically recognizes and binds an antigen, ie, L1CAM. A suitable L1CAM-specific extracellular domain for use in a CAR of the present disclosure may be any antigen-binding polypeptide, a wide variety of which are known in the art. In some cases, the antigen binding domain is a single chain Fv (scFv) or Fab. In other aspects, the antigen-binding fragment useful for a CAR of the present disclosure includes an antigen-binding fragment described elsewhere herein. In some aspects, the transmembrane domain useful for a CAR is linked to the extracellular domain and may include a naturally occurring transmembrane domain. In other aspects, the transmembrane domain useful for a CAR may be derived from the alpha chain, beta chain, or zeta chain of the T cell receptor, CD28, CD3 8, CD45, CD4, CD5, CDS, CD9, CD16, CD22, CD33, CD37, CD64, CD80, CD86, CD134, CD154, CD8, or any other known in the art. ΜΛ / / UU JO l 156 The term intracellular domain refers to the part of a CAR that transduces the signal of effector function upon binding of an antigen to the extracellular domain and directs the T lymphocyte to carry out a specialized function. In one aspect, an intracellular domain for a CAR comprises a tyrosine-based immunoreceptor activation motif (ITAM) activation motif. In some aspects, the ITAM is derived from CD3 zeta (ζ, zeta), FcR gamma, FcR beta, CD3 gamma, CD3 delta, CD3 epsilon, CDS, CD22, CD79a, CD79b, CD66d, 4-1 BB, DAP-1 0 , 0X40 or Fe [epsilon] RI [gamma]. In some aspects, the CAR of the present disclosure further comprises a costimulatory domain that can bind to the intracellular domain. The costimulatory domain in a CAR construct can signal and activate cells as part of an intracellular portion of the CAR. In some aspects, the costimulatory domain is derived from CD27, CD28, 4-1BB, 0X40, CD30, CD40, PD-1, ICOS, lymphocyte function-associated antigen 1 (LFA-1), CD7, LIGHT, NKG2C, or B7- H3. In other aspects, a CAR of the present disclosure further comprises a linker. A short oligopeptide or linker polypeptide may be present between the transmembrane domain and the intracellular domain. In some aspects, the linker is not limited to a length 157 particular provided that the intracellular domain of CAR is capable of inducing activation of T lymphocytes when the extracellular domain is bound to antigen, ie, L1CAM. In some aspects, the linker comprises the (Gly4Ser)3 linker. In other aspects, the present disclosure includes a polynucleotide encoding the CAR of the present disclosure or a vector comprising the polynucleotide. As used herein, the term "T lymphocyte" is a lymphocyte derived from the thymus and related to the immune response of the cell. T cells include CD4+ T cells (helper T cells, TH cells), CD8+ T cells (cytotoxic T cells, CTL), memory T cells, regulatory T cells (Tregs), or natural killer T cells. In some aspects, the T cell into which a CAR is introduced is a CD8 + T cell. VII. Immunoconjugates, antibody derivatives and diagnostics The anti-LICAM antibodies described herein can be used for diagnostic purposes, including sample analysis and in vivo imaging, and for this purpose the antibody (or binding fragment thereof) can be conjugated to a suitable detectable agent. , to form an immunoconjugate. For diagnostic purposes, agents ΜΛ / / UU JO f ¿ Suitable 158 are obnoxious markers including radioisotopes, for whole body imaging, and radioisotopes, enzymes, fluorescent and other antibody markers suitable for sample analysis. Objectionable markers that can be bound to any of the anti-LICAM antibodies described herein can be any of several types currently used in the field of in vitro diagnostics, including particle markers including metallic colloidal solutions such as colloidal gold, isotopes such as I125o Te presented, for example, with a peptide chelating agent of the N2S2, N3S, or N4 type, chromophores including fluorescent labels, luminescent labels, phosphorescent labels, and the like, as well as enzyme labels that convert a given substrate to a detectable label, and label tags. polynucleotides that are revealed after amplification, such as by polymerase chain reaction. Suitable enzyme labels include horseradish peroxidase, alkaline phosphatase, and the like. For example, the marker can be the enzyme alkaline phosphatase, detected by measuring the presence or formation of chemiluminescence after conversion of 1,2-dioxetane substrates such as adamantyl methoxy phosphoryloxy phenyl dioxetane (AMPPD), 3-(4-(methoxyspiro ΜΛ / / UUOO f ¿ 159 {1,2-dioxetane-3,2'-(5'-chloro)tricyclo{3.3.1.1 3,7} decan}-4-yl) disodium phenyl phosphate (CSPD), as well as CDP and CDP-STAR® or other luminescent substrates known to those skilled in the art, for example, the suitable lanthanide chelates such as terbium(III) and europium(III). The means of detection is determined by the selected marker. The appearance of the marker or its reaction products can be achieved with the naked eye, in the case the marker is particulate and accumulates at suitable levels, or through the use of instruments such as a spectrophotometer, luminometer, fluorimeter and the like, all in accordance with standard practice. In some aspects, the conjugation methods result in bonds that are substantially (or nearly so) non-immunogenic, for example, peptide (ie, amide), sulfide, (hindered), disulfide, hydrazone, and ether bonds. These bindings are almost non-immunogenic and show reasonable stability in serum (see, for example, Senter, PD, Curr. Opin. Chem. Biol. 13 (2009) 235-244; WO 2009 / 059278; WO 95 / 17886). . Depending on the biochemical nature of the moiety and the antibody, different conjugation strategies can be employed. In case the remainder is of natural or recombinant origin between 50 and 500 amino acids, there are standard procedures in textbooks that ΜΛ / / UU JO f ¿ 160 describe the chemistry for the synthesis of protein conjugates, which can be readily followed by one skilled in the art (see, for example, Hackenberger, C. P. R., and Schwarzer, D., Angew. Chem. Int. Ed. Engl. M (2008) 10030-10074). In some aspects, the reaction of a maleinimide moiety with a cysteine ​​residue within the antibody or moiety is used. This is an especially suitable coupling chemistry in case, for example, a Fab or Fab' fragment of an antibody is used. Alternatively, in some aspects, coupling to the C-terminus of the antibody or moiety is performed. Modification of the C-terminus of a protein, eg of a Fab fragment, can be performed as described (Sunbul, M. and Yin, J., Org. Biomol. Chem. 7 (2009) 3361-3371). In general, the site-specific reaction and covalent coupling are based on the transformation of a natural amino acid into an amino acid with a reactivity orthogonal to the reactivity of the other functional groups present. For example, a specific cysteine ​​within a rare sequence context can be enzymatically converted to an aldehyde (see Frese, M.A., and Dierks, T., ChemBioChem. 10 (2009) 425-427). It is also possible to obtain a desired amino acid modification using the specific enzymatic reactivity of certain enzymes with a natural amino acid in a given sequence context (see, for example, 161 Taki, M. et al., Prot. Eng. Des. Sel. 17 (2004) 119-126; Gautier, A. et al. Chem. Blol. 15 (2008) 128-136; and protease-catalyzed formation of C—N bonds is used by Bordusa, F., Highlights in Bioorganic Chemistry (2004) 389-403). Site-specific reaction and covalent coupling can also be achieved by selective reaction of terminal amino acids with appropriate modifying reagents. The reactivity of an N-terminal cisterna with benzonitriles (see Ren, H. et al., Angew. Chem. Int. Ed. Engl. 48 (2009) 9658-9662) can be used to achieve site-specific covalent coupling. Natural chemical ligation may also depend on C-terminal cisternae residues (Taylor, E. Vogel; Imperial!, B, Nucleic Aclds and Molecular Biology (2009), 22 (Protein Engineering), 65-96). Document US6437095 B1 describes a conjugation method that is based on the faster reaction of a cisternae in a stretch of negatively charged amino acids with a cisterna located in a stretch of positively charged amino acids. The moiety can also be a synthetic peptide or a peptide mimetic. In case a polypeptide is chemically synthesized, amino acids with orthogonal chemical reactivity can be incorporated during synthesis (see, for example, ΜΛ / / UUOO f ¿ 162 example, de Graaf, A.J. et al., Bloconjug. Chem. 20 (2009) 1281-1295). Since a wide variety of orthogonal functional groups are at play and can be introduced into a synthetic peptide, conjugation of the peptide to a linker is standard chemistry. To obtain a monolabeled polypeptide, the conjugate with 1:1 stoichiometry can be separated by chromatography from other conjugation by-products. This procedure can be facilitated by using a dye-labeled binding pair member and a charged linker. By using this type of highly negatively charged, labeled binding pair member, monoconjugated polypeptides are easily separated from unlabelled polypeptides and polypeptides carrying more than one carrier, since the difference in charge and molecular weight can be used. for separation. The fluorescent dye can be useful to purify the complex from unbound components, such as a labeled monovalent binder. In some aspects, the moiety bound to an anti-LICAM antibody is selected from the group consisting of a binding moiety, a labeling moiety, and a biologically active moiety. The anti-LICAM antibodies described herein can also be conjugated to a therapeutic agent to form an immunoconjugate, such as an antibody-drug conjugate (ADC). The ΜΛ / I / UU JO (¿ Suitable therapeutic agents include antimetabolites, alkylating agents, DNA minor groove binding agents, DNA intercalators, DNA crosslinkers, histone deacetylase inhibitors, nuclear export inhibitors, proteasome inhibitors, topoisomerase I or II inhibitors, heat shock proteins, tyrosine kinase inhibitors, antibiotics, and antimitotic agents. In the ADC, the antibody and therapeutic agent are preferably conjugated via a cleavable linker such as a peptidyl, disulfide or hydrazone linker. ADCs can be prepared as described in US Patent Nos. 7,087,600; 6,989,452; and 7,129,261; PCT Publications WO 02 / 096910; WO 07 / 038658; WO 07 / 051081; WO 07 / 059404; WO 08 / 083312; and WO 08 / 103693; US Patent Publications 20060024317; 20060004081; and 20060247295. In some aspects, the therapeutic agent is selected from the group consisting of a cytotoxin, a non-cytotoxic drug, a radioactive agent, a second antibody, an enzyme, an antineoplastic agent, and any combination of these. In some aspects, the immunoconjugate comprises an anti-LICAM antibody and a cytotoxin. The cytotoxin can be selected from any cytotoxin known in the art. In some aspects, the cytotoxin is selected from the group consisting of dolastatin, monomethyl auristatin E ΜΛ / I / UUOO l¿ 164 (ΜΜΑΕ), maytansine, duocarmycin, calicheamicin, pyrrolobenzodiazepine, duocarmycin, centanamycin, SN38, doxorubicin, a derivative thereof, a synthetic analog thereof, and any combination thereof. In certain aspects, the immunoconjugate comprises an anti-LICAM antibody and cytotoxin A. In other aspects, the immunoconjugate comprises an anti-LICAM antibody and a non-cytotoxic drug. In some aspects, the immunoconjugate comprises an anti-LICAM antibody and a radioactive agent. In some aspects, the radioactive agent is a radionucleotide. In certain aspects, the radioactive agent comprises radioactive iodine. In particular aspects, the radioactive agent comprises 131-iodo. In other aspects, the radioactive agent comprises the radioactive isotope yttrium-90. In some aspects, the immunoconjugate comprises an anti-LICAM antibody and a second antibody. In certain aspects, the immunoconjugate comprises an anti-LICAM antibody and an enzyme. In some aspects, the enzyme comprises glucose oxidase. In some aspects, the enzyme comprises a peroxidase. In some aspects, the enzyme comprises myeloperoxidase. In some aspects, the enzyme comprises glucose oxidase. In some aspects, the enzyme comprises horseradish peroxidase. In certain aspects, the immunoconjugate comprises an anti-LICAM antibody and an antineoplastic agent. The agent ΜΛ / I / UUOO l¿ The antineoplastic agent can be any agent known in the art. In some aspects, the antineoplastic agent is epirubicin. In some aspects, the antineoplastic agent is a superantigen. In certain aspects, the superantigen is staphylococcal enterotoxin A (SEA / E-120; stafenatox). Anti-LICAM antibodies, eg, those described herein, can also be used to detect L1CAM, such as human L1CAM, eg, human L1CAM on the surface of a cell or soluble L1CAM in serum. The antibodies can be used, for example, in an ELISA assay or in flow cytometry. In some aspects, an anti-LICAM antibody is contacted with cells or serum for a suitable time for specific binding to occur, and then a reagent, eg, an antibody that detects the anti-LICAM antibody, is added. Example tests are provided in the Examples. Illustrative methods for detecting L1CAM, eg, surface expressed L1CAM or soluble L1CAM (sLICAM) in a sample (serum) comprise (i) contacting a sample with an anti-LICAM antibody, for a time sufficient to allow the specific binding of the anti-LICAM antibody to L1CAM in the sample, and (2) contacting the sample with a detection reagent, eg, an antibody, that specifically binds the anti-LICAM antibody, such as to the Fe region of the anti-LICAM antibody, in order to detect L1CAM at the ΜΛ / / UU JO f ¿ 166 that binds the anti-LICAM antibody. Washing steps may be included after incubation with the antibody and / or detection reagent. Anti-LICAM antibodies for use in these methods do not have to be linked to a marker or detection agents, as a separate detection agent can be used. Other uses of anti-LICAM antibodies, eg, as monotherapy or combination therapy, are provided elsewhere herein, eg, in the section relating to combination treatments. VIII. bispecific molecules The anti-LICAM antibodies described herein can be used to form bispecific molecules. An anti-LICAM antibody, or antigen-binding portions thereof, can be derivatized or linked to another functional molecule, eg, another peptide or protein (eg, another antibody or ligand for a receptor) to generate a bispecific molecule that binds to at least two different binding sites or target molecules. For example, an anti-LICAM antibody can bind to an antibody or scFv that specifically binds to proteins that can be used as potential targets for combination treatments. In fact, the antibody described herein can be derived from or bind to more than one different functional molecule to generate multispecific molecules that bind to more than two ΜΛ / / UU JO l 167 different binding sites and / or target molecules; Multispecific molecules are also intended to be encompassed by the term bispecific molecule as used herein. To create a bispecific molecule described herein, an antibody described herein can be operatively linked (eg, by chemical coupling, gene fusion, non-covalent association, or otherwise) to one or more binding molecules, such as another binding antibody, antibody fragment, peptide or mimetic, such that a bispecific molecule is produced. Accordingly, bispecific molecules are provided herein comprising at least a first binding specificity for L1CAM and a second binding specificity for a second epitope target. In some aspects described herein where the bispecific molecule is multispecific, the molecule may further include a third binding specificity. In some aspects, the bispecific molecules described herein comprise as binding specificity at least one antibody, or an antibody fragment thereof, including, for example, a Fab, Fab', F(ab')2, Fv or a single chain Fv (scFv). The antibody can also be a light chain or heavy chain dimer, or any minimal fragment thereof, such as an Fv or single chain construct as described in Ladner et al., patent. 168 US #4,946,778. The bispecific molecules described herein can be prepared by conjugation of constituent binding specificities using methods known in the art. For example, each bispecific molecule binding specificity can be generated separately and then conjugated to each other. When the binding specificities are proteins or peptides, it is possible to use a variety of coupling or crosslinking agents for covalent conjugation. See, for example, Karpovsky et al. (1984) J. Exp. Med. 160: 1686; Liu, MA et al. (1985) Proc. nati. Acad. Sel. USA 82:8648. Other methods include those described in Paulus (1985) Behring Ins. Mitt. #78, 118-132; Brennan et al. (1985) Science 229:81-83), and Glennie et al. (1987) J. Immunol. 139: 2367-2375). Some conjugating agents are SATA and sulfo-SMCC, both available from Pierce Chemical Co. (Rockford, IL). IX. compositions Further provided herein are compositions, e.g., a pharmaceutical composition, containing an anti-LICAM antibody, or a combination thereof, or a combination with antibodies against other targets, or antigen-binding part(s) thereof, described herein, formulated together with a pharmaceutically acceptable carrier. Such compositions may include an antibody or a VIA / / UU JO f ¿ 169 combination of antibodies (eg, two or more different), or immunoconjugates or bispecific molecules that are described herein. For example, a pharmaceutical composition described herein may comprise a combination of antibodies (either immunoconjugates or bispecific) that bind to different epitopes on the target antigen or that have complementary activities. The pharmaceutical compositions described herein can also be administered in combination therapy, ie, combined with other agents. For example, the combination therapy may include an anti-LICAM antibody described herein combined with at least one other anti-cancer and / or immunomodulatory agent, eg, T-lymphocyte stimulating (eg, activator) agent. Examples of Therapeutic agents that can be used in combination therapy are described in greater detail below in the section on uses of the anti-LICAM antibodies described herein. In some aspects, the composition of the invention further comprises a thickening agent. A thickening agent can be selected from the group consisting of NaCl, mannitol, glycine, alanine, and any combination of these. In other aspects, the composition of the invention comprises a stabilizing agent. The stabilizing agent may be selected from the group consisting of sucrose, trehalose, 170 raffinose, arginine; or any combination of these. In other aspects, the composition of the invention comprises a surfactant. The surfactant can be selected from the group consisting of polysorbate 80 (PS80), polysorbate 20 (PS20) and any combination of these. In certain aspects, the composition further comprises a chelating agent. The chelating agent may be selected from the group consisting of diethylenetriaminepentaacetic acid (DTPA), ethylenediaminetetraacetic acid, nitrilotriacetic acid, and any combination thereof. In other aspects, the composition comprises a third antibody. In some aspects, the third antibody is any antibody described herein. In one aspect, the composition further comprises NaCl, mannitol, pentetic acid (DTPA), sucrose, PS80, and any combination of these. As used herein, "pharmaceutically acceptable carrier" includes any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like that are physiologically compatible. In some aspects, the carrier is suitable for intravenous, intramuscular, subcutaneous, parenteral, spinal, or epidermal administration (eg, by injection or infusion). a choice of 171 subcutaneous injection is based on Halozyme Therapeutics' ENHANZE® drug delivery technology, which involves a co-formulation of an Ab with the recombinant human hyaluronidase enzyme (rHuPH20) that eliminates traditional limitations on the volume of biologics and drugs that they can be administered subcutaneously due to the extracellular matrix (US Patent No. 7,767, 429). Depending on the route of administration, the active compound, ie, an antibody, immunoconjugate, or bispecific molecule, may be coated with a material to protect the compound from acids and other natural conditions that can inactivate the compound. The pharmaceuticals described herein may include one or more pharmaceutically acceptable salts. A pharmaceutically acceptable salt refers to a salt that retains the desired biological activity of the parent compound and does not impart any unwanted toxicological effects (see, for example, Berge, S.M., et al. (1977) J. Pharm. Sel. 66: 1-19, a pharmaceutical composition described herein can also include a pharmaceutically acceptable antioxidant. These compositions may also contain adjuvants such as preservatives, wetting agents, emulsifying agents, and dispersing agents. The prevention of the presence of microorganisms can be guaranteed by 172 sterilization procedures, noted above, and by including various antibacterial and antifungal agents, for example, paraben, chlorobutanol, phenol, sorbic acid, and the like. It may also be desirable to include isotonic agents, such as sugars, sodium chloride, and the like, in the compositions. In addition, prolonged absorption of the injectable dosage form can be produced by including agents that delay absorption, such as aluminum monostearate and gelatin. Pharmaceutically acceptable carriers include sterile aqueous solutions or dispersions and sterile powders for extemporaneous preparation of sterile injectable solutions or dispersions. The use of media and agents for pharmaceutically active substances is known in the art. Except insofar as any conventional media or agent is incompatible with the active compound, its use in the pharmaceutical compositions described herein is contemplated. A pharmaceutical composition may comprise a preservative or may be devoid of preservatives. Supplementary active compounds can be incorporated into the compositions. Normally, therapeutic compositions must be sterile and stable under the conditions of manufacture and storage. The composition can be formulated as a solution, microemulsion, liposome, or other ordered structure. ΜΛ / / UUOO l 173 suitable for high drug concentration. The carrier can be a solvent or dispersion medium containing, for example, water, ethanol, polyol (for example, glycerol, propylene glycol, and liquid polyethylene glycol, and the like), and suitable mixtures thereof. It is possible to maintain proper fluidity, for example, by using a coating, such as lecithin, by maintaining the necessary particle size in the case of dispersions, and by using surfactants. In many cases, the compositions can include isotonic agents, for example, sugars, polyols such as mannitol, sorbitol, or sodium chloride in the composition. Prolonged absorption of pharmaceutical compositions can be brought about by the inclusion in the composition of an agent that delays absorption, for example, monostearate salts and gelatin. Sterile injectable solutions can be prepared by incorporating the active compound in the required amount in a suitable solvent with an ingredient or combination of ingredients listed above, as necessary, followed by sterilization and microfiltration. In general, dispersions are prepared by incorporating the active compound into a sterile vehicle with a basic dispersion medium and the necessary other ingredients mentioned herein. In the case of sterile powders for the preparation of solutions 174 sterile injectables, some methods of preparation are vacuum drying and freeze-drying (lyophilization) which provide a powder of the active ingredient plus any desired additional ingredients from a previously filtered solution of these under sterile conditions. For the administration of an anti-LICAM antibody, for example, described herein, the dose ranges from about 0.0001 to 100 mg / kg. In some methods, two or more monoclonal antibodies with different binding specificities are administered simultaneously, in which case the dosage of each antibody administered is within the indicated ranges. The antibody is usually administered on multiple occasions. An antibody can be administered as a sustained release formulation, in which case less frequent administration is needed. Dosage and frequency may vary depending on the half-life of the antibody in the patient. In general, human antibodies show the longest half-life, followed by humanized antibodies, chimeric antibodies, and non-human antibodies. The dosage and frequency of administration may vary depending on whether the treatment is prophylactic or therapeutic. In prophylactic applications, a relatively low dosage is administered at intervals 175 relatively infrequent over a long period of time. Some patients continue to receive treatment for the rest of their lives. In therapeutic applications, a relatively high dosage at relatively short dosing intervals is sometimes needed until disease progression is slowed or terminated, and until the patient shows partial or complete improvement of disease symptoms. Subsequently, the patient may be administered a prophylactic regimen. A therapeutically effective dosage of an anti-LICAM antibody described herein may result in a decrease in the severity of disease symptoms, an increase in the frequency and duration of symptom-free periods of disease, or a prevention of disease symptoms. impairment or disability due to illness. In the context of cancer, a therapeutically effective dose may result in increased survival, eg, overall survival, and / or prevention of further deterioration of physical symptoms associated with cancer. Symptoms of cancer are known in the art and include, for example, unusual characteristics of a mole, a change in the appearance of a mole, including asymmetry, border, color, and / or diameter, a newly pigmented area of ​​skin, an abnormal mole, darkened area under the fingernails, lumps on 176 breast changes, nipple changes, breast cysts, breast pain, death, weight loss, weakness, excessive fatigue, difficulty eating, loss of appetite, chronic cough, worsening shortness of breath, cough with blood, blood in urine, blood in stool, nausea, vomiting, liver metastases, lung metastases, bone metastases, abdominal fullness, abdominal distension, fluid in the peritoneal cavity, vaginal bleeding, constipation, abdominal distension , colon perforation, acute peritonitis (infection, fever, pain), pain, vomiting blood, profuse sweating, fever, high blood pressure, anemia, diarrhoea, jaundice, dizziness, chills, muscle spasms, colon metastases, colon metastases lungs, bladder metastases, liver metastases, bone metastases, kidney metastases and pancreas metastases, difficulty in swallowing and the like. A therapeutically effective dose can prevent or delay the onset of cancer, as may be desired when early or preliminary signs of the disease are present. Laboratory tests used in the diagnosis of cancer include chemistry (including measurement of L1CAM levels), hematology, serology, and radiology. Therefore, any clinical or biochemical assay that controls any of the 177 above to determine whether a particular treatment is a therapeutically effective dose for treating cancer. A person skilled in the art will be able to determine amounts based on factors such as the size of the subject, the severity of the subject's symptoms, and the particular composition or route of administration selected. A composition described herein can be administered by one or more routes of administration using one or more of a variety of methods known in the art. As will be appreciated by those skilled in the art, the route and / or mode of administration will vary depending on the desired results. The routes of administration of the anti-LICAM antibodies described herein may include intravenous, intramuscular, intradermal, intraperitoneal, subcutaneous, spinal, or other parenteral routes of administration, eg, by injection or infusion. The phrase parenteral administration, as used herein, means modes of administration other than enteral and topical administration, generally by injection, and includes, but is not limited to, intravenous, intramuscular, intraarterial, intrathecal, intracapsular, intraorbital injection and infusion. , intracardiac, intradermal, intraperitoneal, transtracheal, subcutaneous, subcuticular, intraarticular, subcapsular, subarachnoid, intraspinal, epidural, and intrasternal. 178 Alternatively, an antibody described herein could potentially be administered via a non-parenteral route, such as a topical, epidermal, or mucosal route of administration, eg, intranasal, oral, vaginal, rectal, sublingual, or topical. X.Kits Kits are provided herein comprising one or more antibodies described herein, or antigen-binding fragments thereof, bispecific molecules, or immunoconjugates thereof. In a specific aspect, provided herein is a pharmaceutical pack or kit comprising one or more containers filled with one or more of the ingredients of the pharmaceutical compositions described herein, such as one or more antibodies provided herein, or an antigen-binding fragment thereof, optionally instructions for use. In some aspects, the kits contain a pharmaceutical composition described herein and any prophylactic or therapeutic agent, such as those described herein. XI. uses and methods Certain aspects of the present disclosure relate to the method of treating a subject, comprising administering to the subject an anti-LICAM antibody described herein, a polynucleotide encoding the anti-LICAM antibody, a vector comprising the polynucleotide, a 179 host cell comprising the polynucleotide, an immunoconjugate comprising an anti-LICAM antibody, or any combination of these. Certain aspects of the present disclosure relate to a method of treating a cancer in a subject in need thereof, comprising administering to the subject an effective dose of a composition described herein (eg, an antibody, polynucleotide, vector, host cell , immunoconjugate, or pharmaceutical composition). In other aspects, the present disclosure relates to a method of inhibiting the release of L1CAM by a tumor cell in a subject in need thereof, comprising administering to the subject an effective dose of a composition described herein. In other aspects, the present disclosure relates to a method of reducing serum L1CAM release and / or retaining L1CAM on the cell surface in a subject in need thereof, comprising administering to the subject an effective dose of a composition described in the present. In other aspects, the present disclosure relates to a method of killing a tumor cell in a subject in need thereof, comprising administering to the subject an effective dose of a composition described herein. In other aspects, the present description relates to a method of reducing the size of a tumor in a subject in need thereof, comprising ΜΛ / I / UU JO l¿ 180 administering to the subject an effective dose of a composition described herein. In other aspects, the present disclosure relates to inhibiting the metastasis of a tumor in a subject in need thereof, which comprises administering to the subject an effective dose of a composition described herein. In some aspects, the subject is a human being. The compositions of the present disclosure can be administered using any pharmaceutically acceptable route. In some aspects, the composition (eg, antibody, polynucleotide, vector, host cell, immunoconjugate, or pharmaceutical composition) is administered intravenously, intraperitoneally, intramuscularly, intraarterially, intrathecally, intralymphatically, intralesionally, intracapsularly, intraorbitally, intracardiacally, intradermally, transtracheal, subcutaneous, subcuticular, intraarticular, subcapsular, subarachnoid, intraspinal, epidural, intrasternal, topical, epidermal, mucosal, or any combination of these. In some aspects, the composition is administered intravenously. In some aspects, the composition is administered subcutaneously. In certain aspects, the method reduces the size of a cancer, eg, the size of a tumor, in the subject. In some aspects, the size of the cancer is reduced by at least about 5%, at least about 10%, at least about 15%, at least about 20%, at least about 25%, at least about 30%, at least 181 about 35%, at least about 40%, at least about 45%, at least about 50%, at least about 60%, at least about 70%, at least about 80% or at least about 90%. In some aspects, the method increases the overall survival of the subject. In some aspects, overall survival is increased relative to the average overall survival of a subject who has the same cancer, but is treated with a different therapy. In certain aspects, overall survival is increased by at least about 10%, at least about 20%, at least about 25%, at least about 50%, at least about 2-fold, at least about 3-fold, at least around 5 times. In some aspects, overall survival is increased from at least about 1 month, at least about 2 months, at least about 3 months, at least about 4 months, at least about 5 months, at least about 6 months , at least about 7 months, at least about 8 months, at least about 9 months, at least about 10 months, at least about 1 month, at least about 12 months, at least about 15 months, at least about 18 months, at least about 21 months, at least about 2 years, at least about 3 years, at least about 4 years, at least about 5 years, or at least about 10 years. 182 In some aspects, the method increases the progression free survival of the subject. In some aspects, overall survival is increased relative to the average progression free survival of a subject who has the same cancer, but is treated with a different therapy. In certain aspects, progression-free survival is increased by at least about 10%, at least about 20%, at least about 25%, at least about 50%, at least about 2-fold, at least about 3-fold times, at least about 5 times. In some aspects, overall survival is increased from at least about 1 month, at least about 2 months, at least about 3 months, at least about 4 months, at least about 5 months, at least about 6 months , at least about 7 months, at least about 8 months, at least about 9 months, at least about 10 months, at least about 1 month, at least about 12 months, at least about 15 months, at least about 18 months, at least about 21 months, at least about 2 years, at least about 3 years, at least about 4 years, at least about 5 years, or at least about 10 years. In some respects, the method increases the subject's objective response rate. In certain aspects, the method induces a complete response in the subject. In some ΜΛ / / UUOO l 183 aspects, the method induces a partial response in the subject. In some aspects, the method comprises administering an anti-LICAM antibody (or a polynucleotide, vector, host cell, or immunoconjugate) described herein and a second therapy. In some aspects, the second therapy is administered before the anti-LICAM antibody. In some aspects, the second therapy is administered after the anti-LICAM antibody. In some aspects, the second therapy is administered at the same time as the anti-LICAM antibody. In certain aspects, the anti-LICAM antibody and the second therapy are administered separately. In other aspects, the anti-LICAM antibody and the second therapy are administered in a single formulation. The second therapy can be any other therapy known in the art. In some aspects, the second therapy comprises an immunotherapy. In some aspects, the second therapy comprises a chemotherapy. In some aspects, the second therapy comprises radiation therapy. In some aspects, the second therapy comprises a surgical intervention. In some aspects, the second therapy comprises administering a second therapeutic agent. Anti-LICAM antibodies can enhance the immune response to cancer cells in a cancer patient. Methods are provided herein for treating ΜΛ / / UU JO l¿ 184 a subject having cancer, comprising administering to the subject an anti-LICAM antibody described herein, such that the subject is treated, for example, so as to inhibit or reduce the growth of cancerous tumors and / or have a regression of the tumors and / or that prolonged survival is achieved. An anti-LICAM antibody alone can be used to inhibit the growth of cancerous tumors. Alternatively, an anti-LICAM antibody can be used in conjunction with another agent, eg, another immunogenic agent, a standard cancer treatment, or another antibody, as described below. Accordingly, provided herein are methods of treating cancer, eg, by inhibiting the growth of tumor cells, in a subject, comprising administering to the subject a therapeutically effective amount of an anti-LICAM antibody described herein. Cancers whose growth can be inhibited using the antibodies of the disclosure include cancers that normally respond to immunotherapy and those that do not normally respond to immunotherapy. Cancers that can be treated also include L1CAM-positive cancers. The cancers can be solid tumor cancers or hematologic malignancies (liquid tumors). Non-limiting examples of cancers for treatment include bile duct cancer, carcinoma 185 Squamous cell lung cancer, small cell lung cancer, non-small cell lung cancer, squamous non-small cell lung cancer (NSCLC), non-squamous NSCLC, gastrointestinal cancer, renal cancer (eg, clear cell cancer) , ovarian cancer, liver cancer, colorectal cancer, endometrial cancer, kidney cancer (for example, renal cell carcinoma (RCC)), prostate cancer (for example, hormonal adenocarcinoma of the prostate). refractory), thyroid cancer, neuroblastoma, pharyngeal cancer, laryngeal cancer, oral cancer, connective tissue cancer, Hodgkin lymphoma, lymphoma, multiple myeloma, pancreatic cancer, glioblastoma (glioblastoma multiforme), cervical cancer, breast cancer stomach, bladder cancer, hepatoma, breast cancer, colon adenocarcinoma and head and neck cancer (or carcinoma), gastric cancer, germ cell tumor, pediatric sarcoma, nasal killer cell lymphoma, mela noma (for example, metastatic malignant melanoma, such as cutaneous or infraocular malignant melanoma), bone cancer, skin cancer, cancer of the uterus, cancer of the anal region, cancer of the testicles, carcinoma of the fallopian tubes, carcinoma of the endometrium, carcinoma of the cervix, carcinoma of the vagina, carcinoma of the vulva, cancer of the esophagus, cancer of the small intestine, cancer of the endocrine system, cancer of the parathyroid gland, cancer of the 186 adrenal gland, soft tissue sarcoma, urethral cancer, penile cancer, rectal cancer, childhood solid tumors, ureteral cancer, renal pelvic carcinoma, central nervous system (CNS) neoplasm, lymphoma CNS primary, tumor angiogenesis, spinal axis tumor, brain cancer, brainstem glioma, pituitary adenoma, Kaposi's sarcoma, epidermoid cancer, squamous cell cancer, environmentally induced cancers, including asbestos-induced, cancers related to viruses or cancers of viral origin (eg, human papillomavirus (tumors related to or originating from HPV)); and combinations of cancers. In some aspects, an anti-LICAM antibody is administered to patients who have cancer that has exhibited an inadequate response to, or progressed during, prior treatment, for example, prior treatment with an immuno-oncology drug or immunotherapy, or patients who have cancer that is refractory or resistant, intrinsically refractory or resistant, or where resistant or refractory status is acquired. For example, subjects who do not respond or do not respond sufficiently to a first therapy or who see disease progression after treatment can be treated by administration of an anti-LICAM antibody alone or in combination. ΜΛ / I / UUOO l¿ 187 combination with another therapy. In some aspects, an anti-LICAM antibody is administered to patients who have not previously received (ie, been treated with) an immuno-oncology agent. In some aspects, a method of treating cancer in a subject comprises first determining whether the subject is L1CAM-positive, eg, has L1CAM-expressing tumor cells, and if the subject has L1CAM-positive cancer, administering to the subject an anti-LICAM antibody. , for example, described herein. A method of treating a subject having cancer with an anti-LICAM antibody may comprise administering, to a subject having cancer cells expressing L1CAM, a therapeutically effective amount of an L1CAM antibody. Also provided herein are methods of predicting whether a subject will respond to treatment with an anti-LICAM antibody, wherein the methods comprise determining the level of L1CAM in the patient's cancer cells, and whether the subject's cancer cells are L1CAM positive, then the subject is likely to respond to treatment with an L1CAM antibody. An anti-LICAM antibody can be administered with a reference standard treatment. An anti-LICAM antibody can be administered as maintenance therapy, eg, a therapy that is intended to prevent the occurrence or recurrence of tumors. 188 An anti-LICAM antibody may be given with other treatment, for example, radiation, surgery, or chemotherapy. For example, adjuvant therapy with anti-LICAM antibodies may be given when there is a risk that micrometastases may be present and / or to reduce the risk of relapse. An anti-LICAM antibody, eg, an anti-LICAM antibody described herein, can be combined with a vaccination protocol. Many experimental strategies for vaccination against tumors have been devised (see Rosenberg, S., 2000, Development of Cancer Vaccines, ASCO Educational Book Spring: 60-62; Logothetis, C, 2000, ASCO Educational Book Spring: 300-302; Khayat, D. 2000, ASCO Educational Book Spring: 414-428, Foon, K. 2000, ASCO Educational Book Spring: 730-738, see also Restifo, N. and Sznol, M., Cancer Vaccines, Chapter 61, pp. 3023-3043 in DeVita et al (eds.), 1997, Cancer: Principles and Practice of Oncology, Fifth Edition). Administration of an anti-LICAM antibody can also be combined with standard cancer treatments (eg, surgery, radiation, and chemotherapy). Administration of an anti-LICAM antibody can be effectively combined with chemotherapeutic regimens. In these cases, it may be possible to reduce the dose of the chemotherapeutic reagent administered (Mokyr 189 et al. (1998) Cancer Research 58: 5301-5304). Practice of the present disclosure will use, unless otherwise indicated, standard techniques of cell biology, cell culture, molecular biology, transgenic biology, microbiology, recombinant DNA, and immunology, which are within the skill of the art. Those techniques are fully explained in the literature. See, for example, Sambrook et al., ed. (1989) Molecular Cloning A Laboratory Manual (2nd ed.; Cold Spring Harbor Laboratory Press); Sambrook et al., ed. (1992) Molecular Cloning: A Laboratory Manual, (Coid Springs Harbor Laboratory, NY); D. N. Glover ed., (1985) DNA Cloning, Volume I and II; Gait, ed. (1984) Oligonucleotide Synthesis; Mullis et al., US Patent No. 4,683,195; Hames and Higgins, eds. (1984) Nucleic Acid Hybridization; Hames and Higgins, eds. (1984) Transcription And Translation; Freshney (1987) Culture Of Animal Cells (Alan R. Liss, Inc.); Immobilized Cells And Enzymes (IRL Press) (1986); Perbal (1984) A Practical Guide To Molecular Cloning; the treatise, Methods In Enzymology (Academic Press, Inc., N.Y.); Miller and Callos eds. (1987) Gene Transfer Vectors For Mammalian Cells, (Coid Spring Harbor Laboratory); Wu et al., eds., Methods In Enzymology, vols. 154 and 155; Mayer and Walker, eds. (1987) Immunochemical Methods In Cell And Molecular Biology (Academic Press, London); Weir Blackwell, eds., (1986) Handbook Of Experimental ΜΛ / / UU JO f ¿ 190 Immunology, volumes I-IV; Manipulating the Mouse Embryo, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y., (1986)); Crooks, Antisense drug Technology: Principles, strategies and applications, 2.aed. CRC Press (2007) and in Ausubel et al. (1989) Current Protocols in Molecular Biology (John Wiley and Sons, Baltimore, Md.). The following examples are offered by way of illustration and not by way of limitation. EXAMPLES The following experimental methods and details are mentioned in the examples that follow. Example 1. Construction of Ab612 by site-directed mutagenesis Human antibody Ab417 binding to mammalian (eg, human and mouse) L1CAM, and a method of preparing the same, are described in US Patent No. 9,777,060 and International Publication No. WO2014 / 077648, which are incorporated herein by reference. To improve the biophysical properties of the Ab417 antibody, the effects of the respective amino acids constituting the variable region of the Ab417 antibody on the binding ability of the Ab417 antibody were examined. DNA was synthesized to have the R16G, D54E, K76A, and P88A mutations in the heavy chain variable region of the 191 Ab417 antibody, and recombined with the gene encoding the CH1 domain of human Cyl by polymerase chain reaction (PCR). The resulting PCR product was subjected to 1.5% agarose gel electrophoresis. Bands containing DNA were excised and purified using the PCR purification kit (GeneAll®). Both ends of the purified DNAs were digested with restriction enzymes Ncol and Apal (New England Biolabs), and subcloned into the Ncol and Apal sites of a modified version (full-length pKRIBB-GIII) of the vector pKRIBB-FabD (ref) from phage display human Fab, carrying the full length of Gene III. The resulting recombinant phagemid was named full length pKRIBB-GIII-Fd612. DNA was synthesized to carry the I31S and V95P mutations in the light chain variable region of the Ab417 antibody and recombined with the gene encoding human Ck by PCR. The resulting PCR product was subjected to 1.5% agarose gel electrophoresis. Bands containing DNA were excised and purified using the PCR purification kit (GeneAll®). Both ends of the purified DNAs were digested with the restriction enzyme BstXI (New England Biolabs) and subcloned into the BstXI sites of the full-length pKRIBB-GIII-Fd612. The resulting recombinant phagemid was named full length pKRIBB-GIII-Fab612. For this, the antibody comprising the mutations R16G, D54E, ΜΛ / / UU JO f ¿ 192 Κ7 6Α and Ρ88Α in the heavy chain variable region and the I31S and V95P mutations in the light chain variable region of antibody Ab417 was designated the Ab612 antibody. Example 2. Construction of a Phage Displayed Ab612 Variant Fab Library To improve the affinity and biophysical properties of the Ab612 antibody prepared in Example 1, five LCDR3 sites of Ab612 were randomized by TRIM (trinucleotide mutagenesis, ELLA biotech, Germany). Fragment A containing the sequence from FR1 to FR3 of Ab612 was synthesized. Fragment B (5'-TTT AAT TTC CAC TTT AGT TOO CTG CCC GAA CGT CCA CGG X17 X15 X15 X13 X15 TTG CTG ACA ATA ATA GGT GGC AAA ATC TTC-3') was synthesized, containing the sequence FR3 to FR4 of Ab612 with random LCDR3. X represents the number of amino acids; X17 is 17 amino acids, X15 and X13 are 15 amino acids and 13 amino acids, respectively. Fragments A and B were assembled by recombinant PCR with Phusion high fidelity DNA polymerase (Thermo Fisher Scientific). The resulting PCR products were purified using the PCR purification kit (GeneAll®), digested with the restriction enzyme BstXI (New England Biolabs) and ligated with the BstXI-digested expression vector pKRIBB-GIII-Fab612 complete with vector 1:3 to insert the molar ratio. DNA was electroporated into competent E. coli TG1. the library 193 Ab612 variant Fab produced 5.92 x 108 colonies. To isolate monoclonal antibodies that recognize human L1CAM, human L1CAM was used as the antigen in the first, second, and third rounds of screening. After the three rounds of screening, 470 colonies were randomly selected and separately inoculated into 96-well plates, and then cultured in 300 μΐ of 2 x YT / carbenicillin / glucose at 37°C for 8 h. Subsequently, 30 μΐ of the cells were seeded in each well containing 1 ml of 2x YT / carbenicillin / glucose medium and cultured for 2 h until reaching an OD600 of 0.5. Cells were infected with KM13 helper phage at multiplicity of infection (MOI) 20 without shaking at 37°C for 30 min and then incubated with shaking for 30 min. Infected cells were resuspended in 2xYT / carbenicillin / kanamycin after centrifugation at 2900 x g for 10 min and cultured at 30 °C for 12 h. The supernatant containing Fab phage from the 470 colonies was subjected to indirect and quantitative ELISA. Among them, 41 clones binding human L1CAM with high activity were selected and their plasmid DNAs were isolated and sequenced. As a result, all 32 clones were found to be different from each other. To test the binding ability of the 32 unique clones to human L1CAM, an indirect ELISA was performed. 194 As a result, 4 clones were found to show the highest antigen binding ability (ie, Ab4H5, Ab2C2, Ab4H6 and Ab5D12). Example 3. Conversion of Fab to IgGl and production To convert the Fab to full-length IgGl with codon-optimized sequence for mammalian cells, the heavy and light chain variable regions with leader sequences were amplified by PCR and subcloned into the EcoRI and Apal sites (New England Biolabs) and the BsiWI sites. and HindIII (New England Biolabs), respectively, in the mammalian IgGl expression plasmid vector pdCMV-dhfr-Ab612. HEK293F cells were grown and transfected with the IgGl expression plasmid using ExpiFectamin (Thermo Fisher Scientific) according to ExpiCHO protocols. 7-14 days post-transfection, the cell culture supernatants were centrifuged and filtered using a bottle top filter (0.22 µm PES, Sartorius), and the productivity of the respective mutant was compared to that of the existing Ab417 antibody by ELISA as follows. described below in Example 5. As shown in Table 8, the variant antibodies showed a productivity that is 1.25-1.44 times higher than Ab417. Ab612 was increased 1.44-fold, while Ab4H5, Ab2C2, Ab4H6, and Ab5D12 were increased 1.25, 1.26, 1.36, and 1.26-fold, respectively. ΜΛ / / UUOO f ¿ 195 Table 8. Productivity of antibodies Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 compared to Ab417 Antibody Productivity (mg / L) Anti-LICAM (Ab417) 52 Anti-LICAM (Ab612) 75 Anti-LICAM (Ab4H5) 65 Anti-LICAM (Ab2C2) 66 Anti-LICAM (Ab4H6) 71 Anti-LICAM (Ab5D12) 66 Example 4. Purification of Ab417 Variant Antibodies The plasmid DNAs of the expression vectors of these antibodies were obtained in a large amount and expressed in ExpiCHO cells in the same manner as in Examples 1-3, respectively. The cell cultures were centrifuged to collect the supernatants. Supernatants were filtered using a bottle top filter (0.22 pm PES, Sartorius) and purified by affinity chromatography. The respective supernatants were applied to a column packed with protein A-coupled beads (Amicogen) and the antibodies were eluted to protein A using 0.1 M sodium-citric acid solution. 196 (pH 3.2). Next, 1.0 M Tris solution (pH 8.0) was immediately added to the eluted antibodies for neutralization. Purified IgG1 was stored in buffer (Napi 10 mM 5% sorbitol 0.01% tween 20) after dialysis using a PD-10 column with sephadex G-25 (GE Healthcare). The concentration of the purified antibody was determined with a Nanodrop (Thermo Fisher Scientific, Nanodrop 2000) based on the molar extinction coefficient. Purified antibodies were subjected to 10% SDS-PAGE and Coomassie staining to confirm that each of the heavy and light chains were expressed and assembled as full length IgG. Example 5. Characterization of Ab417 variant antibodies The affinities of the purified antibodies for human LIGAN were measured by competitive ELISA. Human LIGAN was prepared at a density of 1x10 -7 M and serially diluted to 1x10-12M using 0.1% PBA buffer (PBS containing 0.1% BSA). The respective antibodies were prepared by diluting them in 0.1% PBA buffer to particular concentrations based on their binding capacity. The diluted antigens and antibodies were reacted with each other in the same volume ratio at 37°C for 3 hours. 96-well plates (MaxiSorp, Nunc) were coated using the purified human LIGAN which were diluted in a buffered solution. 197 (15 mM Na2C03, 34.84 mM NaHCO3, pH 9.6) at a concentration of 100 ng / well, at 4 °C overnight. The next day, Difeo skim milk (BD) was dissolved in a 0.05% PBS-T buffer solution to a concentration of 2%, and 200 ul was added to each well, followed by incubation at 37 °C for 1 hour. The wells were washed twice with 0.05% PBS-T buffered solution. Then, 100 ul of the antigen / antibody reagent was added and reacted for 3 hours and allowed to react at room temperature for 1 hour. The wells were washed three times with 0.05% PBS-T buffer to remove non-antigen-bound antibodies. As a secondary antibody, goat anti-human IgG(Fc) HRP (invitrogen, 1 / 10000) which specifically recognizes the Fe region of the human antibody was added and allowed to react at 37°C for 1 hour. Wells were washed four times with 0.05% PBS-T buffer to remove remaining secondary antibodies. To examine the affinity according to color development, 100 ul of a solution (BD OptEIA, BD) containing TMB as a substrate for the HRP enzyme (which was covalently linked to the secondary antibody) was added to each well and incubated at room temperature. for 5 minutes. Finally, 50 ul of 2.5 M HSO solution was added to each well to terminate the enzymatic reaction. After the completion of the reaction, the 198 absorbance at 450 nm (VERSAmax microplate reader, Molecular Devices). The results are shown in Table 9. The affinity of Ab417 for human L1CAM was 5x10-10 M, the affinity of Ab612 was 2.6 x 10-10 M, the affinity of the Ab4H5 mutant was 6 x 10-11 M, the affinity of Ab2C2 mutant was 5 x 10-11 M, Ab4H6 mutant affinity was 6 x 10-11 M, Ab5D12 mutant affinity was 1.2 x 10-10 M. Ab417 variant antibodies showed binding affinity around 2- 10-fold higher for human L1CAM than the Ab417 antibody. Table 9. Affinity (K) of Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 antibodies for human L1CAM compared to Ab417 ΜΛ / I / UUOO l¿ Antibody Affinity (K) M Anti-LICAM (Ab417) 5 x 10~10 Anti-LICAM (Ab612) 2.6 x 10~10 Anti-LICAM (Ab4H5) 6 x 10-11 Anti-LICAM (Ab2C2) 5 x 1011 Anti- LICAM (Ab4H6) 6 x ΙΟ11 Anti-LICAM (Ab5D12) 1.2 x 10~10 199 Example 6. Analysis of the antigen binding specificity of Ab417 variants To examine whether the variant antibodies selectively bind to human and mouse LIGAN, flow cytometry was performed using various cell types. In this regard, as a comparative antibody, the antibody Ab417 which binds to human L1CAM and mouse L1CAM was used. CHO-DG44 cells (ATCC #PTA-3356) known not to express human LIGAN were cultured and used as a negative control. In addition, cells expressing human LIGAN, human ovarian carcinoma, SKOV3 (ATCC #HTB-77) and human non-small cell lung carcinoma, NCI-H522 (AYCC #CRL-5810) were cultured. As mouse LIGAN-expressing cells, a melanoma cell line, B16F1 (ATCC No. CRL-6323), was cultured. Cultured cells were harvested using 0.05% trypsin or dissociation buffer (GIBCO) for CHO-DG44 cells, resuspended in 1% PBA solution, and placed on ice for 20 min. The cells were then added to a round bottom polystyrene test tube (Falcon) at a density of 4 x 105 cells per tube. Purified antibodies were diluted in PBA solution to a concentration of 10 ug / ml, and 100 ul was added to each tube and mixed well. The tubes were placed at 4 °C for 1 hour. The secondary antibody that specifically binds to the Fe region of the 200 Human IgG and is covalently linked with FITC (Sigma) to each tube at a ratio of 1:2000. The plate was wrapped with aluminum foil to block the light and it was left to react at 4 °C for 1 hour. A PI staining reagent (propidium iodide, Sigma) was added at a ratio of 1:200 to assess cell viability. After completion of all reactions, fluorescent signals of FITC and PI were detected in the cells. Figure 1A shows that variant antibodies do not bind L1CAM negative cells (ie CHO-DG44). Figures IB-ID show that the variant antibodies bind to L1CAM-positive human cells, NCI-H522 (Figure IB), SKOV3 (Figure 1C) and L1CAM-positive mouse cells, B16F1 (Figure ID). The variant antibodies specifically bind to the B166F1 mouse melanoma cell line, suggesting that the Ab417 variants of the present invention specifically bind to both human and mouse L1CAM. Example 7. Quality measurement of Ab417 variants purified by SEC-HPLC HPLC grade UPLC solvents and PBS were purchased from Fisher Scientific (Fair Lawn, NJ, USA) and GIBCO (St. Louis, MO, USA), respectively. Size exclusion chromatography was used for the separation of antibody samples with a high resolution Biosuit SEC column or (7.5 x 300 mm, 250A particle size). Samples are z / Qenn / Lznz / q / Yi 201 separated using PBS pH 7.4 with isocratic flow. For the experiments, the Waters® e2695 separations module was used, and the 2489 UV / Vis detector controlled the absorbance at 280 nm. Size-exclusion high-performance liquid chromatography (SEC-HPLC) analysis showed that the variant antibodies exhibited a monomer peak (Figures 2B-2F), although Ab417 had high molecular weight aggregates and low molecular weight fragments with a broad beak (Figure 2A). Example 8. Affinity analysis of Ab417 variants for human L1CAM The affinities of Ab417 and Ab417 variants for human L1CAM were examined by BLI using Octet RED384 (ForteBio). For affinity analysis, antibodies were diluted with a PBA solution prepared by adding 0.1% BSA to PBS. Human L1CAM was serially diluted with PBA to a concentration of 50, 25, 12.5, 6.25, 3.125, 1.5625, 0.78125, or 0 nM, then 200 ul of diluted L1CAM was added to an opaque 96-well plate to prevent transmission of light. The AHC (Anti-Human IgG Fe Capture) Sensor Chip was used to analyze the binding kinetics of antibodies to antigens by examining changes in refractive index that occur as antibody and antigen associate and dissociate while transfer sensor chip to PBA solution, antibody, z / Qenn / Lznz / q / Yi solution 202 PBA, antigen and PBA solution in this order. Table 10 shows that the affinity (Kd) of Ab417 for human L1CAM was around 0.2 nM, the affinity of Ab612 was 0.1 nM, the affinity of Ab4H5 was 8 pM, the affinity of Ab2C2H was out of range, the Ab4H6 affinity was 0.07 nM and Ab5D12 affinity was 0.09 nM. The higher affinity of the variants compared to Ab417 (eg, up to 25-fold) was due to the slower rate of dissociation. Table 10. Affinity (Kd) of Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 antibodies for human L1CAM compared to Ab417 z i ornn / L7n7 / q / yl Antigen antibody KO (m) Kohíws) χλ2 Comp ra2comp hthsl AB417 3.596+05 9.456*05 0 2376 0.9938 1.056*10 3.136+05 3.286*05 0.1235 0.997 AMHS 8726-12 3 636+05 2.956-06 0.209 0.209 0.209 12 3 446+05 <1.06-07 0.3084 0.9933 M4H6 L416-11 3.736+05 2.776-05 0.2228 0.9943 &606-11 4.116+05 3.946-05 0.2524 0.9936 Example 9. Isoelectric Point (IP) Analysis of Ab417 Variants The Sciex PA800 plus instrument with a neutral coated capillary (Sciex PN 477441) was used to perform capillary isoelectric focusing (cIEF) of Ab417 and its mutants. All experiments were carried out in triplicate. The values ​​of P1 of the respective materials 203 were determined using 32 Karat software. Table 11 shows that Ab417 antibody pI was 9.62, Ab612 pI was 9.25, Ab4H5 pI was 8.96, Ab2C2 pI was 8.96, Ab4H6 pI was 9.03 and the pI value of Ab5D12 was 9.04. Table 11. Pl value of Ab612, Ab4H5, Ab2C2, Ab4H6 and Ab5D12 compared to Ab417 1 Qrnn / L7h7 / q / Yl· Antibody Pl Value Anti-LICAM (Ab417) 9.62 Anti-LICAM (Ab612) 9.25 Anti-LICAM (Ab4H5) 8.96 Anti-LICAM (Ab2C2) 8.96 Anti-LICAM (Ab4H6) 9.03 Anti-LICAM (Ab5D12) 9.04 Example 10 Analysis of the inhibitory effect on tumor growth of Ab417 variants To investigate the antitumor effect of the Ab612 antibody, male Balb / c nude mice were transplanted with the cholangiocarcinoma cell line of human origin Choi-CK. Constructed Choi-Ck tumor tissue (3x3x3 mm3) was inoculated on the back of the mice. after the volume 204 tumor reached 100 mm3 (n=8 per group), it was injected i.v. Ab417 antibody at a dose of 10 mg / kg, Ab612 antibody at a dose of 10 mg / kg, control hFc antibody at a dose of 3.3 mg / kg, and negative control (PBS) or (vehicle) three times a week for 3 weeks. Tumor volume, mouse body weight and tumor weight were measured and are shown in Figures 1A-1C, respectively. Figures 3A and 3C show that the Ab612-treated groups showed a mean tumor volume of 311 mm3 and a tumor weight of 0.20 g, while the AÓ417-treated groups showed a mean tumor volume of 387 mm3 and a tumor weight of 0.41 g. Sham control mice showed a mean tumor volume of 1096 mm3 and a tumor weight of 0.93 g. The result indicates that Ab612 (tumor growth inhibition rate (RI) 78.2%) exhibited 1.4-fold higher tumor growth inhibition compared to Ab417 (IR 55.5%), based on tumor weight (Figure 3C). Figure 3D shows the images of tumors from each group of eight mice sacrificed after the end of the experiment as described in Figures 3A-3C. The size of cancerous tissues removed from eight mice treated with Ab612 antibody is smaller than those treated with Ab417 antibody. Anti-cancer effect of Ab612 antibody appears to work well in vivo, enhancing tumor microenvironment (TME) to z / Qenn / Lznz / q / Yi 205 through the infiltration of antibodies into the cancerous tissue or the environment of aggression based on immune cells. Therefore, the group treated with the Ab612 antibody described herein showed a significant inhibitory effect on tumor growth, compared with the group administered the negative control. In addition, no loss of body weight was observed in the mice during the administration and no toxicity was observed from the administration of the antibody. The foregoing description of the specific aspects will fully disclose the general nature of the invention so that others, applying knowledge in the art, can readily modify and / or adapt the specific aspects to various applications, without undue experimentation and without departing from the concept. overview of the present invention. Therefore, adaptations and modifications are intended to be within the meaning and spectrum of equivalents of the aspects described, based on the information and guidelines presented herein. It is to be understood that the phraseology or terminology used herein is for the purpose of description and not limitation, such that those skilled in the art will interpret the terminology or phraseology of the present description in light of the information and guidelines of the z / Qenn / Lznz / q / Yi 206 present . Other aspects of the invention will be apparent to those skilled in the art from the description and practice of the invention described herein. It is intended that the description and examples be regarded as exemplary only, and that the following claims indicate a true scope and spirit of the invention. All publications, patents, and patent applications described herein are incorporated by this reference to the same extent as if each individual publication, patent, or patent application were specifically and individually indicated as incorporated by this reference. It is noted that as of this date, the best method known to the applicant for putting said invention into practice is the one that is clear from the present description of the invention.

Claims

1. An isolated antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to the same epitope of the L1 cell adhesion molecule (L1CAM) as a reference antibody comprising a heavy chain variable region (HV) and a light chain variable region (LV), wherein: (a) the HV of the reference antibody comprises SEC. ID NO.: 23 and the LV of the reference antibody comprises SEC. ID NO.: 24, (b) the HV of the reference antibody comprises SEC. ID NO.: 25 and the LV of the reference antibody comprises SEC. ID NO.: 26, (c) the HV of the reference antibody comprises SEC. ID NO.: 27 and the LV of the reference antibody comprises SEC. ID NO.: 28, (d) the HV of the reference antibody comprises SEC. ID NO.: 29 and the LV of the reference antibody comprises SEC. ID NO.: 30, or (e) the VH of the reference antibody comprises SEC. ID NO.: 31 and the VL of the reference antibody comprises SEC. ID NO.: 32.

208. z / Government / Sales / q / Yi 208.

2. The antibody, or antigen-binding fragment thereof, according to claim 1, characterized in that it comprises the complementarity-determining region of VH 1 (CDR1), VH CDR2 and VH CDR3, and VL CDR1, VL CDR2 and VL CDR3, wherein at least one amino acid in the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2 and / or VL CDR3 of the antibody, or antigen-binding fragment thereof, is different from the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2 and / or VL CDR3 of the mAb417 antibody, and wherein the VH CDR1 of the mAb417 antibody comprises RFGMH (SEC. ID NO.: 2); The VH CDR2 of the mAb417 antibody comprises FISNDGSNKYYADSVKG (SEC. ID NO.: 9); the VH CDR3 of the mAb417 antibody comprises GRAYGSGSLFDP (SEC. ID NO.: 10); the VL CDR1 of the mAb417 antibody comprises RASRTISIYVN (SEC. ID NO.: 6); the VL CDR2 of the mAb417 antibody comprises AASNLHS (SEC. ID NO.: 7); and the VL CDR3 of the mAb417 antibody comprises QQSIGRGWT (SEC.ID NO.: 11).

3. An isolated antibody, or antigen-binding fragment thereof, characterized in that it cross-competes for binding to an epitope of the L1 cell adhesion molecule z / Qenn / Lznz / q / Yi 209 (L1CAM) with a reference antibody comprising a heavy chain variable region (HV) and a light chain variable region (LV), wherein: (a) the HV of the reference antibody comprises SEC. ID NO.: 23 and the LV of the reference antibody comprises SEC. ID NO.: 24, (b) the HV of the reference antibody comprises SEC. ID NO.: 25 and the LV of the reference antibody comprises SEC. ID NO.: 26, (c) the HV of the reference antibody comprises SEC. ID NO.: 27 and the LV of the reference antibody comprises SEC. ID NO.: 28, (d) the HV of the reference antibody comprises SEC. ID NO.: 29 and the VL of the reference antibody comprises SEC. ID NO.: 30, or (e) the VH of the reference antibody comprises SEC. ID NO.: 31 and the VL of the reference antibody comprises the SEC. ID NO.: 32, wherein the antibody, or antigen-binding fragment thereof, comprises the complementarity-determining region of VH1 (CDR1), VH CDR2 and VH CDR3, and VL CDR1, VL CDR2 and VL CDR3, wherein at least one amino acid in the VH CDR1, VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of the antibody, or antigen-binding fragment thereof, is different from the VH CDR1, z / Qenn / Lznz / q / Yi 210 VH CDR2, VH CDR3, VL CDR1, VL CDR2, and / or VL CDR3 of antibody mAb 417, and wherein the VH CDR1 of antibody mAb417 comprises RFGMH (SEC. ID NO.: 2); the VH CDR2 of the mAb417 antibody comprises FISNDGSNKYYADSVKG (SEC. ID NO.: 9); the VH CDR3 of the mAb417 antibody comprises GRAYGSGSLFDP (SEC. ID NO.: 10); the VL CDR1 of the mAb417 antibody comprises RASRTISIYVN (SEC. ID NO.: 6); the VL CDR2 of the mAb417 antibody comprises AASNLHS (SEC. ID NO.: 7) ; and the VH CDR3 of the mAb417 antibody comprises QQSIGRGWT (SEC. ID NO.: 11).

4. The antibody, or antigen-binding fragment thereof, according to claim 2 or 3, characterized in that the at least one amino acid difference is in the VH CDR2 of the antibody, or antigen-binding fragment thereof, and wherein the VH CDR2 of the antibody, or antigen-binding fragment thereof, comprises glutamine in residue 5.

5. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 4, characterized in that the at least one amino acid difference is in the VL CDR1 of the antibody, or antigen-binding fragment 211 thereof, and wherein the VL CDR1 of the antibody, or antigen-binding fragment thereof, comprises serine in residue 8.

6. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 5, characterized in that the at least one amino acid difference is in the VL CDR3 of the antibody, or antigen-binding fragment thereof, and wherein the VL CDR3 of the antibody, or antigen-binding fragment thereof, comprises proline in residue 8.

7. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 6, characterized in that the at least one amino acid difference is in the VL CDR3 of the antibody, or antigen-binding fragment thereof, and wherein the VL CDR3 of the antibody, or antigen-binding fragment thereof, comprises alanine, glycine, phenylalanine, tyrosine, threonine, proline, and tryptophan in residues 3 to 9, respectively.

8. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 7, characterized in that the at least one amino acid difference is in the VL CDR3 of the antibody, or antigen-binding fragment thereof, and wherein the VL CDR3 of the antibody, or antigen-binding fragment thereof, comprises alanine, glycine, phenylalanine, tyrosine, serine, proline, and tryptophan at residues 3 to 9, respectively.

9. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 8, characterized in that the at least one amino acid difference is in the VL CDR3 of the antibody, or antigen-binding fragment thereof, and wherein the VL CDR3 of the antibody, or antigen-binding fragment thereof, comprises leucine, histidine, phenylalanine, tyrosine, proline, and tryptophan in residues 4 to 9, respectively.

10. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 9, characterized in that the at least one amino acid difference is in the VL CDR3 of the antibody, or antigen-binding fragment thereof, and wherein the VL CDR3 of the antibody, or antigen-binding fragment thereof, comprises leucine, valine, tryptophan, tyrosine, proline, and tryptophan in residues 4 to 9, respectively.

11. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 10, characterized in that it comprises SEC. ID NO.: 13, SEC. ID NO.: 15, SEC. ID NO.: 17, SEC. ID NO.: 19 or SEC. ID NO.:

21.

12. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 11, characterized in that the VH CDR1 of the antibody, or the antigen-binding fragment thereof, comprises RFGMH (SEC. ID NO.: 2).

13. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 12, characterized in that the VH CDR2 of the antibody, or antigen-binding fragment thereof, comprises FISNEGSNKYYADSVKG (SEC. ID NO.: 10).

14. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 13, characterized in that the VH CDR3 of the antibody, or antigen-binding fragment thereof, comprises GRAYGSGSLFDP (SEC. ID NO.: 4).

15. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 14, characterized in that the CDR1 of VL comprises RASRTISSYVN (SEC. ID NO.: 12).

16. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 15, characterized in that the CDR2 of VL comprises AASNLHS (SEC. ID NO.: 7).

17. The antibody, or antigen-binding fragment thereof, according to any of claims 2 to 16, characterized in that the CDR3 of VL comprises QQSIGRGPVT SEC. ID NO.:

13.

18. The antibody, or antigen-binding fragment of 214 this, according to any of claims 1 to 17, characterized in that it comprises a heavy chain CDR1, CDR2 and CDR3 and a light chain CDR1, CDR2 and CDR3, wherein the light chain CDR3 comprises QQSIGRGPVT (SEC. ID NO.:13).

19. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 17, characterized in that it comprises a heavy chain CDR1, CDR2 and CDR3 and a light chain CDR1, CDR2 and CDR3, wherein the light chain CDR3 comprises QQAGFYTPWT (SEC. ID NO.:15).

20. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 17, characterized in that it comprises a heavy chain CDR1, CDR2 and CDR3 and a light chain CDR1, CDR2 and CDR3, wherein the light chain CDR3 comprises QQAGFYSPWT (SEC. ID NO.:17).

21. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 17, characterized in that it comprises a heavy chain CDR1, CDR2 and CDR3 and a light chain CDR1, CDR2 and CDR3, wherein the light chain CDR3 comprises QQSLHFYPWT (SEC. ID NO.:19).

22. The antibody, or antigen-binding fragment thereof, according to any of claims 1 215 to 17, characterized in that it comprises a heavy chain CDR1, CDR2 and CDR3 and a light chain CDR1, CDR2 and CDR3, wherein the light chain CDR3 comprises QQSLVWYPWT (SEC. ID NO.:21).

23. The antibody, or antigen-binding fragment thereof, according to any one of claims 1 to 22, wherein the antibody, or antigen-binding fragment thereof, is characterized in that it has one or more features selected from the group consisting of: (a) the antibody, or antigen-binding fragment thereof, exhibits improved productivity; (b) the antibody, or antigen-binding fragment thereof, exhibits improved affinity as measured by the equilibrium dissociation constant (Kd); (c) the antibody, or antigen-binding fragment thereof, exhibits an improved PI value; (d) the antibody, or antigen-binding fragment thereof, exhibits improved affinity as measured by the association constant (K); or (e) any combination thereof.

24. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 23, characterized in that it exhibits improved productivity compared to the mAb417 antibody. 25.The antibody, or antigen-binding fragment of 216, according to claim 24, characterized in that the enhanced productivity is at least 55 mg / L, at least 56 mg / L, at least 57 mg / L, at least 58 mg / L, at least mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L, at least about mg / L at least around mg / L at least around mg / L at least around 85 mg / L when expressed as in example 3.

26. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 25, characterized in that it exhibits an improved Kd compared to the mAb417 antibody.

27. The antibody, or antigen-binding fragment thereof, according to claim 26, characterized in that the improved Kd is less than 2.6 x 10⁻¹⁰ M, less than 2.5 x 10⁻¹⁰ M, less than 2.0 x 10⁻¹⁰ M, less than 1.5 x 10⁻¹⁰ M, less than 1.0 x 10⁻¹⁰ M, less than 9 x 10⁻¹¹ M, less than 8 x 10⁻¹¹ M, less than 7 x 10⁻¹¹ M, less than 6 x 10⁻¹¹ M, less than 5 x 10⁻¹¹ M, less than 4 x 10⁻¹¹ M, less than 3 x 10⁻⁹ M, less than 2 x 10⁻¹¹ M, less than 1 x 10⁻¹¹ M, less than 9 x 10⁻¹² M, less than 8 X 10~12 M, less than 7 X 10~12 M, less than 6 10-13 M, or less than 8 X ΙΟ-13 M.

28. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 27, characterized in that it exhibits an improved affinity (K) compared to the mAb417 antibody.

29. The antibody, or antigen-binding fragment thereof, according to claim 28, characterized in that the enhanced affinity (K) is less than 5 x 10⁻¹⁰ M, less than 4 x 10⁻¹⁰ M, less than 3 x 10⁻¹⁰ M, less than 2 x 10⁻¹⁰ M, less than 1.0 x 10⁻¹⁰ M, less than 9 x 10⁻¹¹ M, less than 8 x 10⁻¹¹ M, less than 7 x 10⁻¹¹ M, less than 6 x 10⁻¹¹ M, less than 5 x 10⁻¹¹ M, less than 4 x 10⁻¹¹ M, less than 3 x 10⁻¹¹ M, less than 2 x 10⁻¹¹ M, less than 1 x 10⁻¹¹ M, less than 9 x 10⁻¹² M, less than 8 x 10~12 M, less than 7 X 10~12 M, less than 6 X 10~12 M, less than 5 X 10~12 M, less than 4 X 10~13 M. ΜΛ / / UUOO l 218 30. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 29, characterized in that it exhibits an improved PI value compared to the mAb417 antibody.

31. The antibody, or antigen-binding fragment thereof, according to claim 30, characterized in that the improved PI value is less than 9.6, less than 9.5, less than 9.4, less than 9.3, less than 9.2, less than 9.1, less than 9.0, less than 8.9, less than 8.8, less than 8.7, less than 8.6, less than 8.5, less than 8.4, less than 8.3, less than 8.2, less than 8.1, less than 8.0, less than 7.9, less than 7.8, less than 7.7, or less than 7.

6.

32. An isolated antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to L1CAM, wherein the antibody, or antigen-binding fragment thereof, comprises a VH CDR1, CDR2 and CDR3 and a VL CDR1, CDR2 and CDR3; wherein the VH CDR1, CDR2 and CDR3 comprise RFGMH (SEC. ID NO.: 2), FISNEGSNKYYADSVKG (SEC. ID NO.: 10), and GRAYGSGSLFDP (SEC. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2 and CDR3 comprise RASRTISSYVN (SEC. ID NO.: 12), AASNLHS (SEC. ID NO.: 7), and QQSIGRGPVT (SEC. ID NO.: 13), respectively.

33. An isolated antibody, or antigen-binding fragment thereof, specifically binding to L1CAM, characterized in that it comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein the VH CDR1, CDR2 and CDR3 comprise RFGMH (SEC. ID NO.: 2), FISNEGSNKYYADSVKG (SEC. ID NO.: 10), and GRAYGSGSLFDP (SEC. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2 and CDR3 comprise RASRTISSYVN (SEC. ID NO.: 12), AASNLHS (SEC. ID NO.: 7), and QQAGFYSPWT (SEC. ID NO.: 17), respectively.

34. An isolated antibody, or antigen-binding fragment thereof, specifically binding to L1CAM, characterized in that it comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein the VH CDR1, CDR2, and CDR3 comprise RFGMH (SEC. ID NO.: 2), FISNEGSNKYYADSVKG (SEC. ID NO.: 10), and GRAYGSGSLFDP (SEC. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2, and CDR3 comprise RASRTISSYVN (SEC. ID NO.: 12), AASNLHS (SEC. ID NO.: 7), and QQAGFYTPWT (SEC. ID NO.: 17), respectively.

35. An isolated antibody, or antigen-binding fragment thereof, that binds specifically to L1CAM, characterized in that it comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein the VH CDR1, CDR2, and CDR3 comprise RFGMH (SEC. ID NO.: 2), FISNEGSNKYYADSVKG (SEC. ID NO.: 10), and 220GRAYGSGSLFDP (SEC. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2, and CDR3 comprise RASRTISSYVN (SEC. ID NO.: 12), AASNLHS (SEC. ID NO.: 7), and QQSLHFYPWT (SEC. ID NO.: 19), respectively.

36. An isolated antibody, or antigen-binding fragment thereof, that binds specifically to L1CAM, characterized in that it comprises a VH CDR1, CDR2, CDR3 and a VL CDR1, CDR2, CDR3; wherein the VH CDR1, CDR2, and CDR3 comprise RFGMH (SEC. ID NO.: 2), FISNEGSNKYYADSVKG (SEC. ID NO.: 10), and GRAYGSGSLFDP (SEC. ID NO.: 4), respectively; and wherein the VL CDR1, CDR2, and CDR3 comprise RASRTISSYVN (SEC. ID NO.: 12), AASNLHS (SEC. ID NO.: 7), and QQSLVWYPWT (SEC. ID NO.: 19), respectively.

37. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 36, characterized in that the VH comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as EVQLVESGGG WQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVAFISNEGSNKYYADSVKGRFTISR DNSANTLYLQMNSLRAEDTAVYYCARGRAYGSGSLFDPWGQGTLVTVSS (SEC. ID zi ornn / L7n7 / q / yl 221 NO.: 23).

38. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 37, characterized in that the VL comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as DIQLTQSPSS z / Qenn / Lznz / q / Yi LSASVGDRVTITCRASRTISSYVNWYRQRPGKAPESLIYAASNLHSGVPSRFSGSGSGTDF TLTISSLQPEDFATYYCQQSIGRGPVTFGQGTKLEIK (SEC. ID NO.: 24).

39. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 38, characterized in that the VH comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as EVQLVESGGG WQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVAFISNEGSNKYYADSVKGRFTISR DNSANTLYLQMNSLRAEDTAVYYCARGRAYGSGSLFDPWGQGTLVTVSS (SEC. ID NO.: 27).

40. The antibody, or antigen-binding fragment 222 east, according to any of claims 1 to 39, characterized in that the VL comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as DIQLTQSPSS z / Qenn / Lznz / q / Yi LSASVGDRVTITCRASRTISSYVNWYRQRPGKAPESLIYAASNLHSGVPSRFSGSGSGTDF TLTISSLQPEDFATYYCQQAGFYSPWTFGQGTKLEIK (SEC. ID NO.: 28).

41. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 40, characterized in that the VH comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as EVQLVESGGG WQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVAFISNEGSNKYYADSVKGRFTISR DNSANTLYLQMNSLRAEDTAVYYCARGRAYGSGSLFDPWGQGTLVTVSS (SEC. ID NO.: 25).

42. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 41, characterized in that the VL comprises a sequence of 223 amino acids that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as DIQLTQSPSS z / Qenn / Lznz / q / Yi LSASVGDRVTITCRASRTISSYVNWYRQRPGKAPESLIYAASNLHSGVPSRFSGSGSGTDF TLTISSLQPEDFATYYCQQAGFYTPWTFGQGTKLEIK (SEC. ID NO.: 26).

43. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 42, characterized in that the VH comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as EVQLVESGGG WQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVAFISNEGSNKYYADSVKGRFTISR DNSANTLYLQMNSLRAEDTAVYYCARGRAYGSGSLFDPWGQGTLVTVSS (SEC. ID NO. : 2 9).

44. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 43, characterized in that the VL comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as z / Qenn / Lznz / q / Yi DIQLTQSPSSLSASVGDRVTITCRASRTISSYVNWYRQRPGKAPESLIYAASNLHSGVPSR FSGSGSGTDFTLTISSLQPEDFATYYCQQSLHFYPWTFGQGTKLEIK (SEC. ID NO.: 30).

45. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 44, characterized in that the VH comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as EVQLVESGGGWQPGGSLRLSCAASGFTFSRFGMHWVRQAPGKGLEWVAFISNEGSNKYYAD SVKGRFTISRDNSANTLYLQMNSLRAEDTAVYYCARGRAYGSGSLFDPWGQGTLVTVSS (SEC. ID NO.: 31).

46. ​​The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 45, characterized in that the VL comprises an amino acid sequence that is at least about 80%, at least about 85%, at least about 90%, at least about 95%, at least about 96%, at least about 97%, at least about 98%, at least about 99%, or about 100% identical to the amino acid sequence indicated as DIQLTQSPSS LSASVGDRVTITCRASRTISSYVNWYRQRPGKAPESLIYAASNLHSGVPSRFSGSGSGTDF TLTISSLQPEDFATYYC QQSLVWYPWTFGQGTKLEIK (SEC. ID NO.: 32).

47. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 46, characterized in that the VH of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 23 and the VL of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

24.

48. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 46, characterized in that the VH of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 25 and the VL of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

26.

49. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 46, characterized in that the VH of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 27 and the VL of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

28.

50. The antibody, or antigen-binding fragment thereof, according to any of claims 1 z / Qenn / Lznz / q / Yi 226 to 46, characterized in that the VH of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 29 and the VL of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

30.

51. The antibody, or antigen-binding fragment thereof, according to any of claims 1 to 46, characterized in that the VH of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 31 and the VL of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

32.

52. An antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to L1CAM, comprising a heavy chain (HC) and a light chain (LC) wherein the HC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 38 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

39.

53. An antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to L1CAM, comprising a heavy chain (HC) and a light chain (LC) wherein the HC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 40 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

41.

54. An antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to L1CAM, comprising a heavy chain (HC) and a light chain (LC) wherein the HC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 42 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

43.

55. An antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to L1CAM, comprising a heavy chain (HC) and a light chain (LC) wherein the HC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 44 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

45.

56. An antibody, or antigen-binding fragment thereof, characterized in that it binds specifically to L1CAM, comprising a heavy chain (HC) and a light chain (LC) wherein the HC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.: 46 and the LC of the antibody, or antigen-binding fragment thereof, comprises SEC. ID NO.:

20.

57. The antibody according to any one of claims 1 to 56, characterized in that it is selected from the group consisting of IgG1, IgG2, IgG3, IgG4, a variant thereof, and any combination thereof.

58. The antibody according to any of claims 1 to 57, characterized in that it is a chimeric antibody, a human antibody, or a humanized antibody.

59. The antibody according to any of claims 1 to 56, characterized in that it comprises a Fab, a Fab', an F(ab')2, an Fv or a single-chain Fv (scFv).

60. A nucleic acid characterized in that it encodes the antibody according to any of claims 1 to 59.

61. A vector characterized in that it comprises the nucleic acid according to claim 60.

62. A host cell characterized in that it comprises the vector according to claim 61.

63. The host cell according to claim 63, characterized in that it is selected from the group consisting of a cell of E. coli, Pseudomonas, Bacillus, Streptomyces, yeast, CHO, YB / 20, NSO, PER-C6, HEK-293T, NIH-3T3, HeLa, BHK, Hep G2, SP2 / 0, Rl.l, BW, LM, COS 1, COS 7, BSC1, BSC40, BMT10, plant cell, insect cell and a human cell in tissue culture.

64. An immunoconjugate characterized in that it comprises the antibody, or antigen-binding fragment thereof, according to any of claims 1 to 59, linked to an agent. z / Qenn / Lznz / q / Yi 229 65. A bispecific or multispecific antibody comprising the antibody, or the antigen-binding fragment thereof, according to any of claims 1 to 59, and an antibody, or antigen-binding fragment thereof, characterized in that it binds to an antigen.

66. A composition characterized in that it comprises the antibody according to any of claims 1 to 59, the nucleic acid according to claim 60, the vector according to claim 61, the cell according to claim 62 or 63, the immunoconjugate according to claim 64 or the bispecific or multispecific antibody according to claim 65, and a carrier.

67. A kit characterized in that it comprises the antibody according to any of claims 1 to 59, the nucleic acid according to claim 60, the vector according to claim 61, the cell according to claim 62 or 63, the immunoconjugate according to claim 64 or the bispecific or multispecific antibody according to claim 65 and instructions for use.

68. An immune cell characterized in that it comprises the nucleic acid according to claim 60 or the vector according to claim 61.

69. The immune cell according to claim 68, characterized in that it is a T lymphocyte or an NK cell.

70. The immune cell according to claim 68 or 69, characterized in that it comprises a chimeric antigen receptor comprising the antibody, or antigen-binding fragment thereof, according to any one of claims 1 to 59.

71. A method for producing an antibody, or an antigen-binding fragment thereof, characterized in that it binds specifically to a human L1CAM protein, comprising culturing the cell according to claim 62 or 63 under suitable conditions and isolating the antibody.

72. A method for treating a disease or condition in a subject in need thereof, characterized in that it comprises administering to the subject the antibody according to any one of claims 1 to 59, the nucleic acid according to claim 60, the vector according to claim 61, the cell according to claim 62 or 63, the immunoconjugate according to claim 64, the bispecific or multispecific antibody according to claim 65, the composition according to claim 66, or the immune cell according to any one of claims 68 to 70.

73. The method according to claim 72, characterized in that the disease or condition comprises a tumor.

74. The method according to claim 72 or 73, characterized in that the tumor comprises a bile duct cancer, a melanoma, pancreatic cancer, chyloma, breast cancer, lymphoma, lung cancer, kidney cancer, prostate cancer, fibrosarcoma, colon adenocarcinoma, liver cancer, or ovarian cancer.

75. The method according to claim 74, characterized in that the tumor is biliary tract cancer.

76. The method according to any of claims 72 to 75, characterized in that the antibody, nucleic acid, vector, cell, immunoconjugate, bispecific or multispecific antibody, composition or immune cell suppresses tumor growth.

77. The method according to any of claims 72 to 76, characterized in that the antibody, nucleic acid, vector, cell, immunoconjugate, composition or immune cell enhances the infiltration of immune cells into the tumor.

78. The method in accordance with any of claims 72 to 77, characterized in that it comprises administering an additional therapeutic agent.

79. The method according to claim 78, characterized in that the additional therapeutic agent comprises chemotherapy, immunotherapy, radiotherapy, or combinations thereof.

80. The method according to claim 79, characterized in that the additional therapeutic agent is an immune checkpoint inhibitor.