Anti-TL1a antibodies for treating inflammatory dermatologic diseases and related methods

Abstract

Aspects of the disclosure relate to a method for treating inflammatory dermatologic diseases in a subject involves administering an anti-TLIA antibody that is modified for half-life extension. In some embodiments, administration of the anti-TLIA antibody leads to improvements in inflammation, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced and / or lesions compared to no treatment. In some embodiments, the inflammatory dermatologic diseases include eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo and pemphigus. The anti-TLIA antibody treatment is shown to be as effective as TNF inhibitor treatment and can be administered at disease onset or prior to full symptomology. The method is applicable to humans, non-human primates, and rat models of inflammatory dermatologic disease.

Description

Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 ANTI-TL1A ANTIBODIES FOR TREATING INFLAMMATORY DERMATOLOGIC DISEASES AND RELATED METHODSCROSS REFERENCE TO RELATED APPLICATION

[0001] This application claims the benefit of and priority to U. S. Provisional Application No.63 / 744,328, filed on January' 12, 2025 and U. S. Provisional Application No. 63 / 757,709, filed on February 12, 2025. the entire content of each of which are incorporated herein by reference.REFERENCE TO SEQUENCE LISTING

[0002] The instant application contains a Sequence Listing which has been submitted electronically in XML file format and is hereby incorporated by reference in its entirety. Said XML copy, created on January 8, 2026, is named 220703-011801_PCT_SL.xml and is 2,012,910 bytes in size.TECHNICAL FIELD

[0003] Aspects of the present disclosure relate to anti-TLl A antibodies for the treatment of inflammatory dermatologic diseases, and methods of treatment with such antibodies.BACKGROUND

[0004] Inflammatory dermatologic diseases, such as eczema, psoriasis, psoriasis vulgaris, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo, scleroderma, dermatomyositis, and pemphigus, are chronic inflammatory conditions that primarily affect the immune system and skin, causing an immune system response, inflammation, disrupted skin barrier, redness, pain, swelling, itching, often the development of lesions such as plaques, rashes, or blisters. A disrupted skin barrier impairs the skin’s natural protective function, which can lead to moisture loss, and vulnerability to infections and irritants. These diseases may also lead to inflammation of joint, the kidneys, or the cardiovascular system. Psoriasis and eczema, in particular, are prevalent forms of inflammatory dermatologic diseases that affect inflammatory dermatologic diseases millions of people worldwide, significantly impacting their quality of life. Current treatments may not be effective for all patients and can have significant side effects, highlighting the need for new therapeutic approaches.

[0005] These inflammatory dermatologic diseases often require long-term management, where treatment usually focuses on reducing inflammation, preventing flare-ups, and controlling itching. The development of biologic therapies has revolutionized the treatment landscape for inflammatory dermatologic diseases, offering targeted approaches that ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 specifically modulate the immune response. The development of biologic disease-modifying anti-inflammatory dermatologic therapeutics have improved patient care by providing additional options to induce disease remission. Biologies treating eczema include IL -4 and IL-13 inhibitors (e.g.. dupilumab). Biologies treating psoriasis or psoriasis vulgaris include TNF inhibitors (e.g., etanercept, adalimumab, and infliximab) which target Tumor Necrosis Factor (TNF); IL-12 and IL-23 inhibitors (e.g., ustekinumab, guselkumab); IL-17 inhibitors (e.g., secukinumab, ixekizumab, and brodalumab); and phosphodiesterase-4 inhibitor (e.g., apremilast). Biologies treating scleroderma include those targeting CD20 on B cells (e.g., rituximab); IL-6 (e.g., tocilizumab); and B-cell Activating Factor (BAFF) inhibitor (e.g., belimumab). Despite these advances, there remains a substantial unmet need for therapies that provide beter efficacy, safety, and convenience for patients. The complexify of the immune system and the variability in patient responses to existing treatments necessitate ongoing research and innovation. Current biologic treatments, such as TNF and IL-6 inhibitors, increase the risk of serious infection, require frequent drug administration and are ineffective in a subset of patients. Therefore, the development of additional biologic treatments against novel disease targets with favorable safety and dosing profiles could improve patient care and open the door to combination therapies to treat patients with inflammatory dermatologic diseases.SUMMARY

[0006] Aspects of the disclosure relate to methods for treating inflammation of the skin and / or skin fibrosis in a subject in need thereof by administering an inhibitor of TL1A binding to its receptor, hereinafter “a TL1 A inhibitor,” such as an anti-TLl A antibody. In some embodiments, the method comprises treating inflammatory dermatologic diseases in a subject in need thereof by administering a TL1A inhibitor, such as an anti-TLIA antibody. Its administration may lead to improvements in slowing or reduction of lesion size, skin color normalization, and alleviation of symptoms like inflammation, disrupted skin barrier redness, pain, swelling, itching, and lesions, compared to no treatment. In some embodiments, the administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating inflammation of the skin and / or skin fibrosis.

[0007] In a specific embodiment, the anti-TLIA antibody is modified in the Fc region to have an extended half-life compared to the unmodified form of the antibody. Exemplary modifications to increase antibody half-life include YTE and LS (as described in detail infra).

[0008] In some embodiments, the administration of an effective amount of the TL1A ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 inhibitor, such as an anti-TLl A antibody (e.g. an half-life extended anti-TLIA antibody), to the subject results in one or more of the following: changes in cytokine levels, particularly skin and serum or skin lesion cytokine levels, reduction of serum anti-collagen antibodies, modified histopathology’, e.g.. of skin lesion biopsy tissue, and / or altered RNA expression, e.g., in peripheral blood cells or skin lesions, compared to no treatment. The TL1 A inhibitor, such as an anti-TLIA antibody, may be at least as effective as TNF inhibitor for managing an inflammatory’ dermatologic disease. In another embodiment, the TL1A inhibitor, such as an anti-TLIA antibody, is more effective than a TNF inhibitor for managing an inflammatory’ dermatologic disease.

[0009] In a specific embodiment wherein the TL1A inhibitor is an anti-TLIA antibody, the anti-TLIA antibody binds TL1A with a dissociation constant (KD) less than about 0.5 nanomolar (nM), optionally less than about 0.4 nM, and optionally less than about 0.3 nM. In a specific embodiment, the anti-TLIA antibody binds TL1 A with a KD of 0.22 nM. In a specific embodiment the anti-TLIA antibody binds TL1A with a KD of 0.10 nM.

[0010] In some embodiments, the administration of an effective amount of the anti-TLIA antibody to the subject results in changes to the levels of serum or skin lesion cytokines, modified histopathology', and / or altered RNA expression in peripheral blood cells or skin lesions, compared to no treatment. In some embodiments, administration of an effective amount of the anti-TLIA antibody to the subject results in modulation of fibroblast or fibroblast-like cells. In some embodiments, administration of an effective amount of the anti-TLIA antibody to the subject results in a decrease of the level of cytokines, such as TNF, IL-I, IL-4, IL- 5, IL- 6, IL-13, IL-17, INFgamma. In some embodiments, administration of the anti-TLIA antibody to the subject results in a decrease of the level of TNF, IL-6, IL- 17 or combination thereof.

[0011] The administration of the anti-TLIA antibody to the subject may result in reduction of an immune system response, inflammation, skin fibrosis, disrupted skin barrier, redness, pain, swelling, itching, and lesions or combination thereof.

[0012] In some embodiments, the anti-TLIA antibody is a long acting anti-TLIA antibody. In methods of the disclosure, an anti-TLIA antibody can be modified to extend its half-life, to reduce Fc functionality, or to provide Fab or Fab’ fragments. In a specific embodiment, an anti-TLIA antibody Fc domain comprises amino acid modifications L234A / L235A (LALA) to reduce Fc functionality, and / or M252Y, S254T, and T256E (YTE) (according to EU numbering system) to increase half-life.ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0013] In some embodiments, the TL1A binding antibody comprises a heavy chain variable region (VH) comprising (i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 A. TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C. In some embodiments, the TL1A binding antibody comprises a light chain variable region (VL) comprising (i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C. In some embodiments, the TL1A binding antibody comprises a modified Fc domain that extends half-life of the TL1 A binding protein as compared to a TL1A binding protein that does not comprise the modified Fc domain.

[0014] In a specific embodiment, the anti-TLl A antibody binds an epitope that includes at least 5 amino acid residues selected from Lys243, Lys240, Thr239, Tyr238, Asp237, Val236, Leu235, Ser234, Ile233. Asp232, Metl58, Argl56. Trpll9, Hisll8, Lysl ll, PhellO, Hisl09, Glnl08, Thrl07, Prol06, Thrl05, Glnl04, Argl03, Vall02, and VallOl of a TL1A polypeptide comprising SEQ ID NO: 2493. In another specific embodiment, the anti-TLl A antibody binds an epitope that includes at least 5 amino acid residues selected from Vai 101, Vai 102. Arg 103, Gin 104, Thr 105, Pro 106, Thr 107. Gin 108, His 109, Phe 110, Lys 111, His 118. Trp 119. Glu 120, Glu 122, Leu 123, Gly 124, Lys 137. Arg 156. Gly 157, Met 158. Ser 234, Tyr 238, and Thr 239 of SEQ ID NO: 2493. In another specific embodiment, the anti-TLl A antibody binds an epitope that includes at least 5 amino acid residues selected from Vai 102, Arg 103, Gin 104, Thr 105, Thr 107, Gin 108, His 118, Trp 119, Glu 120, Glu 122, Leu ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 123, Gly 124, Lys 137, Arg 156, Gly 157, Met 158, Ser 234, Tyr 238, and Thr 239 of SEQ ID NO: 2493. In another specific embodiment, the anti-TLl A antibody binds an epitope that includes at least 5 amino acid residues selected from Lys240, Thr239, Tyr238, Asp237, Val236, Leu235, Ser234, Glnl04. and Argl03 of SEQ ID NO: 2493. In some embodiments, the TL1A binding antibody specifically binds to the TL1A polypeptide comprising SEQ ID NO: 2493 at one or more of amino acid residues Vai 102, Arg 103, Gin 104, Glu 120, Glu 122, Leu 123, and Arg 156.

[0015] In a specific embodiment, the anti-TLl A antibody binds an epitope that includes at least 5 amino acid residues selected from VallOl, Argl03, Glnl04, Thrl05, Thrl07, Hisll8, Glul20, Hisl21, Glul22, Leul23, Argl56, Metl58, Ser234, Tyr238, and Thr239 of aTLIA polypeptide comprising SEQ ID NO: 2493. In another specific embodiment, the anti-TLl A antibody binds an epitope that includes at least 5 amino acid residues selected from Argl03, Thrl05, Prol06. Thrl07, Glnl08. Hisl09, Argl56. Asp232, Ile233, Ser234. Leu235. Asp237, Tyr238, Thr239, Lys240, and Glu241 of a TL1 A polypeptide comprising SEQ ID NO: 2493.

[0016] Exemplar) anti-TLl A antibodies, CDRs, or both for use in the disclosure are described in PCT application No. PCT / US24 / 41774 entitled " TL1 A BINDING PROTEINS AND METHODS OF USE," filed on August 9, 2024, PCT application No PCT / US24 / 34949 entitled " TL1A ANTIBODY COMPOSITIONS AND METHODS OF USE" filed on June 21, 2024, which are incorporated by reference herein in their entireties.

[0017] In accordance with aspects of the disclosure, a TL1A inhibitor, such as an anti-TLIA antibody, can be used in methods of treating an inflammatory dermatologic disease comprising administering an effective amount of the TL1A inhibitor, such as an anti-TLIA antibody, to a subject in need of such treatment, e.g., diagnosed with an inflammatory dermatologic disease. In some embodiments, the method of the disclosure is as effective in treating an inflammatory dermatologic disease as administration of a TNF inhibitor. In some embodiments, the method of the disclosure the anti-TLIA antibody, particularly a half-life extended antibody, is more effective in treating an inflammatory dermatologic disease in a subject compared to TNF inhibitor treatment.

[0018] Inflammatory dermatologic diseases typically involve an overactive immune response, where the body’s defense system mistakenly targets healthy skin, leading to a variety of skin conditions, including disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, often the development of lesions, such as plaques, rashes, or blisters. Non-limiting examples of inflammatory dermatologic diseases that can be treated using the methods of the disclosure include, but are not limited to, eczema, psoriasis, psoriasis vulgaris, scleroderma,ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo and pemphigus. Inflammatory' dermatologic diseases can be associated with or caused by an autoimmune response.

[0019] Eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, and pemphigus are inflammatory conditions involving TL1A. In one embodiment, the TL1A inhibitor, such as an anti-TLIA antibody, is administered to the subject at the onset of the disease. In another embodiment, the TL1A inhibitor, such as an anti-TLIA antibody is administered to the subject in need thereof before the full symptoms of the disease appear. In another embodiment, the TL1A inhibitor, such as an anti-TLIA antibody is administered to the subject after the full symptoms of the disease appear. The TL1 A inhibitor, such as an anti-TLIA antibody, can be administered intravenously or subcutaneously.

[0020] In some embodiments, the anti-TLIA antibody is along acting anti-TLIA antibody. In methods of the disclosure, an anti-TLIA antibody can be modified to extend its half-life, to reduce Fc functionality', or to provide Fab or Fab’ fragments. In a specific embodiment, an anti-TLIA antibody Fc domain comprises amino acid modifications L234A / L235A (LALA) to reduce Fc functionality, and / or M252Y, S254T, and T256E (YTE) or M428L and N434S (LS) (according to EU numbering system) to increase half-life.

[0021] The subject receiving the treatment can be a primate. In some embodiments, the subj ect receiving the treatment is a human.

[0022] In some embodiments, as a result of the treatment, the subject achieves a clinical response and / or improvement in physical function. In some embodiments, the subject achieves slowing or reduction of lesion size, skin color normalization, and alleviation of symptoms like itching or pain. In some embodiments, laboratory tests may show lowered inflammatory' markers (e.g., C-reactive protein (CRP), or ery throcyte sedimentation rate (ESR)). In some embodiments, as a result of the treatment, patient-reported outcomes, including reduced symptoms of itching or discomfort, and visual improvement in skin appearance (e.g., less scaling in psoriasis) serve as indicators of disease improvement. In some embodiments, skin biopsies or imaging tests may7be used to monitor deeper or systemic effects, particularly in diseases like scleroderma. In a specific example of a rat model of rheumatic disease, where the rat is injected with collagen and adjuvant to induce the disease (collagen-induced arthritis or CIA model), administration of an anti-TLIA antibody resulted in improvement in symptoms. In some embodiments, the TL1A inhibitor reduces arthritis symptoms more effectively than a TNF inhibitor.

[0023] In another embodiment, a TL1 A inhibitor, such as an anti-TLIA antibody, may be ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 evaluated in the rat model using a collagen-induced arthritis (CIA) model. For example, the rat can be challenged with collagen and adjuvant on days 0 and 7, and the anti-TLIA antibody treatment may begin either before or after the second collagen administration. An immune response can be measured in the rat's joints, observable in the paws, and an arthritis score may be calculated as the sum of the scores for all four paws.

[0024] The anti-TLIA antibody may more effectively treat eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo or pemphigus in the subject compared to TNF inhibitor treatment.

[0025] A method for treating eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo or pemphigus in a subject may involve administering an effective amount of the anti-TLIA antibody, which can lead to improvements in slowing or reduction of lesion size, skin color normalization, and alleviation of symptoms like inflammation, disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, lesions, or a combination thereof, compared to no treatment. In some embodiments, administration of an effective amount of the anti-TLIA antibody to the subject results in modulation of fibroblast or fibroblast-like cells. The anti-TLIA antibody may effectively treat eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo or pemphigus as well as or beter than TNF inhibitor treatment. In some embodiments, the anti-TLIA antibody is a long- acting anti-TLIA antibody. In some embodiments, the anti-TLIA antibody is administered intravenously or subcutaneously.BRIEF DESCRIPTION OF THE DRAWINGS

[0026] FIG. 1 provides a schematic for the Collagen Induced Arthritis (CIA) model in rats used in Example 1.

[0027] FIG. 2 shows the binding activity of anti-TLIA antibody AbX to rat TL1A as determined with surface plasmon resonance (SPR). Surface plasmon resonance (SPR) sensorgram showing the binding of rat TL1 A to AbX. AbX was immobilized to the sensor chip, and recombinant rat TL1 A binding was measured at concentrations of 200 nM (purple), 100 nM (brown), 50 nM (pink), 25 (green) or 12.5 nM (orange) nM. The binding affinity of AbX to rat TL1 A was quantified based on a global curve fiting analysis.

[0028] FIG. 3 shows arthritis scores in the semi-established CIA model.

[0029] FIG. 4 shows arthritis scores in the therapeutic CIA model.ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0030] FIG. 5 shows effect of treatment on foot volume increase in the semi-established CIA model.

[0031] FIG. 6 shows effect of treatment on foot volume increase in the therapeutic CIA model.

[0032] FIG. 7 shows effect of treatment on hind paw x-ray score in the semi-established CIA model.

[0033] FIG. 8 shows effect of treatment on hind paw x-ray score in the therapeutic CIA model.

[0034] FIGS.9A-9D show Histopathology scores (Infiltration of cells FIG. 9A, Pannus severity grade FIG. 9B, Cartilage lesion severity grade FIG. 9C, Bone resorption severity grade FIG. 9D) in the semi-established CIA model.

[0035] FIG. 10A and FIG. 10B show PASI scores of sham (healthy) control mice, vehicle control mice and mice treated with anti-TLIA antibody or anti-IL-23 antibody at 25 mg / kg or 5 mg / kg, respectively.

[0036] FIGS. 11A and FIG. 11B show PASI scores of sham (healthy) control mice, vehicle control mice and mice treated with pairwise combinations of anti-TLIA antibody with anti-IL-23 antibody at 25 mg / kg or 5 mg / kg, respectively.

[0037] FIG. 12A shows histopathology score for sham (healthy) control mice, vehicle control mice and mice treated with anti-TLIA antibody or anti-IL-23 antibody at 25 mg / kg or 5 mg / kg (* P < 0.05 vs. vehicle (1-way ANOVA)). FIG. 12B and FIG. 12C show histopathology7scores of sham (healthy) control mice, vehicle control mice and mice treated with pairwise combinations of anti-TLIA antibody with anti-IL-23 antibody at 25 mg / kg or 5 mg / kg, respectively (* P < 0.05 vs. combination (t-test) for pairwise comparisons).

[0038] FIGS. 13A-13B show simulated PK in Serum and Tissue for Regimen 1 and Regimen 2. Regimen 1 includes administration of Antibody 63 at Weeks 0, 4 and 8, and extension Weeks 12, 24 and 36. Regimen 2 includes administration of Antibody 63 at Weeks 0, and extension Weeks 12 and 36. FIG. 13A is a graph showing serum PK concentration (pg / mL) for Regimen 1 and Regimen 2. FIG. 13B is a graph showing tissue PK concentration (pg / mL) for Regimen 1 and Regimen 2. PK concentration data shows median (solid line) and 2.5 to 97.5 percentiles (shaded area). Tissue to serum partitioning coefficient is assumed to be 0.35.

[0039] FIGS. 14A-14B show simulated Free sTLIA in Serum and tissue for Regimen 1 and Regimen 2. Regimen 1 includes administration of Antibody 63 at Weeks 0, 4 and 8, and extension Weeks 12, 24 and 36. Regimen 2 includes administration of Antibody 63 at Weeks 0, and extension Weeks 12 and 36. FIG. 14A is a graph showing serum sTLIA concentration (% ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 baseline) for Regimen 1 and Regimen 2. FIG. 14B is a graph showing tissue sTLl A concentration (% baseline) for Regimen 1 and Regimen 2. Baseline sTLl A assumed to be 500 pg / mL up to Week 12 and 100 pg / mL in extension in both serum and tissue. Tissue to serum partitioning coefficient is assumed to be 0.35. PD data shows median (solid line) and 5 to 95 percentiles (shaded area).DETAILED DESCRIPTION

[0040] It is to be understood that both the foregoing general description and the following detailed description are exemplary, and explanatory' only, and are not restrictive of the disclosure.

[0041] The section headings used herein are for organizational purposes only and are not to be construed as limiting the subject mater described.

[0042] All documents, or portions of documents, cited in this application, including, but not limited to, patents, patent applications, articles, books, and treatises, are hereby expressly incorporated by reference in their entirety7for any purpose.

[0043] Tumor Necrosis Factor-like protein 1A (TL1A) is a pro-inflammatory cytokine that plays a key role in regulating immune responses, particularly in the context of autoimmune and inflammatory diseases. It is primarily produced by immune cells such as dendritic cells, T cells, and macrophages, and it exerts its effects by interacting with its receptor Death Receptor 3 (DR3), which is found on various immune cells. By binding to DR3, TL1A may enhance the activation of T cells, leading to the release of inflammatory cytokines like IL-17, IL-4, IL-13, and IL-5. Various fibroblast cell types are also activated by TL1A. In this context, intervention by way of inhibiting the TL1 A pathway, particularly with novel anti-TLl A antibodies disclosed here, whether used alone or in combination with other interventions, represents a promising avenue for developing new treatments that offer improved outcomes for patients suffering from these debilitating conditions.Definitions

[0044] Unless otherwise indicated, all technical terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this disclosure belongs. Unless otherwise indicated or obvious from context, the following terms have the following meanings:

[0045] As used herein, unless otherwise indicated, the term “antibody” is understood to mean an intact antibody' (e.g., an intact monoclonal antibody), or a fragment thereof, such as a Fc fragment of an antibody (e.g., an Fc fragment of a monoclonal antibody), or an antigen- ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 binding fragment of an antibody (e.g., an antigen-binding fragment of a monoclonal antibody), including an intact antibody, antigen-binding fragment, or Fc fragment that has been modified, engineered, or chemically conjugated. In general, antibodies are multimeric proteins that contain four polypeptide chains. Two of the polypeptide chains are called immunoglobulin heavy chains (H chains), and two of the polypeptide chains are called immunoglobulin light chains (L chains). The immunoglobulin heavy and light chains are connected by an interchain disulfide bond. The immunoglobulin heavy chains are connected by interchain disulfide bonds. A light chain consists of one variable region (VL) and one constant region (CL). The heavy chain consists of one variable region (VH) and at least three constant regions (CHI, CH2 and CH3). The variable regions determine the binding specificity of the antibody. Each variable region contains three hypervariable regions known as complementarity determining regions (CDRs) flanked by four relatively conserved regions known as framework regions (FRs). The extent of the FRs and CDRs has been defined (Kabat 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 Chothia, C. et al. (1987) J. Mol. Biol. 196:901-917). The three CDRs, referred to as CDR1, CDR2, and CDR3, contribute to the antibody binding specificity. Naturally occurring antibodies have been used as starting material for engineered antibodies, such as chimeric antibodies and humanized antibodies. Examples of antibody -based antigen-binding fragments include Fab, Fab’, (Fab’)2, Fv, single chain antibodies (e.g., scFv), minibodies, and diabodies. Examples of antibodies that have been modified or engineered include chimeric antibodies, humanized antibodies, and multispecific antibodies (e.g.. bispecific antibodies). An example of a chemically conjugated antibody is an antibody conjugated to a toxin moiety.

[0046] The terms '‘variable domain” and '‘variable region” are used interchangeably and refer to the portions of the antibody or immunoglobulin domains that exhibit variability' in their sequence and that are involved in determining the specificity and binding affinity of a particular antibody. Variability is not evenly distributed throughout the variable domains of antibodies; it is concentrated in sub-domains of each of the heavy and light chain variable regions. These sub- domains are called “hypervariable regions” or “complementarity determining regions” (CDRs). The more conserved (i.e., non-hypervariable) portions of the variable domains are called the “framework” regions (FRM or FR) and provide a scaffold for the six CDRs in three-dimensional space to form an antigen-binding surface.

[0047] An “Fc polypeptide” of a dimeric Fc as used herein refers to one of the two polypeptides forming the dimeric Fc domain, i.e. a polypeptide comprising C-terminal constant regions of an immunoglobulin heavy chain, capable of stable self-association. For ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 example, an Fc polypeptide of a dimeric IgG Fc comprises an IgG CH2 and an IgG CH3 constant domain sequence. An Fc can be of the class IgA, IgD, IgE, IgG, and IgM. These classes are also designated a, 5, 8, y, and p, respectively. Several of these may be further divided into subclasses (isotypes), e.g., IgGl. IgG2, IgG3, IgG4. IgAl, and IgA2.

[0048] The terms “Fc receptor” and “FcR” are used to describe a receptor that binds to the Fc region of an antibody. For example, an FcR can be a native sequence human FcR. Generally, an FcR is one which binds an IgG antibody (a gamma receptor) and includes receptors of the FcyRI, FcyRII, and FcyRIII subclasses, including allelic variants and alternatively spliced forms of these receptors. FcyRII receptors include FcyRIIA (an “activating receptor”) and FcyRIIB (an “inhibiting receptor”), which have similar amino acid sequences that differ primarily in the cytoplasmic domains thereof. Immunoglobulins of other isotypes can also be bound by certain FcRs (see, e.g., Janeway et al., Immuno Biology: the immune system in health and disease, (Elsevier Science Ltd., NY) (4th ed., 1999)). Activating receptor FcyRIIA contains an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain. Inhibiting receptor FcyRIIB contains an immunoreceptor tyrosine-based inhibition motif (ITIM) in its cytoplasmic domain (reviewed in Daeron, Annu. Rev. Immunol. 15:203-234 (1997)). FcRs are reviewed in Ravetch and Kinet, Annu. Rev. Immunol 9:457-92 (1991); Capel et al., Immunomethods 4:25-34 (1994); and de Haas et al.. J. Lab. Clin. Med. 126:330-41 (1995). Other FcRs, including those to be identified in the future, are encompassed by the term “FcR” herein. The term also includes the neonatal receptor, FcRn, which is responsible for the transfer of maternal IgGs to the fetus (Guyer et al., J. Immunol. 117:587 (1976); and Kim et al., J. Immunol. 24:249 (1994)).

[0049] The terms “recipient”, “individual”, “subject”, “host”, and “patient”, are used interchangeably herein and in some embodiments, refer to any mammalian subject for whom diagnosis, treatment, or therapy is desired, particularly humans. “Mammal” for purposes of treatment refers to any animal classified as a mammal, including humans, domestic and farm animals, and laboratory, zoo, sports, or pet animals, such as dogs, horses, cats, cows, sheep, goats, pigs, mice, rats, rabbits, guinea pigs, monkeys etc. In some embodiments, the mammal is human. None of these terms require the supervision of medical personnel.

[0050] As used herein, the term “effective amount” refers to the amount of a compound (e.g., a compound of the present disclosure) sufficient to effect beneficial or desired results. An effective amount can be administered in one or more administrations, applications or dosages and is not intended to be limited to a particular formulation or administration route. As used herein, the term “treating” includes any effect, e.g.. lessening, reducing, modulating, ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 ameliorating or eliminating, that results in the improvement of the condition, disease, disorder, and the like, or ameliorating a symptom thereof.

[0051] As used herein, the term “pharmaceutical composition” refers to the combination of an active agent with a carrier, inert or active, making the composition especially suitable for diagnostic or therapeutic use in vivo or ex vivo.

[0052] As used herein, the term “pharmaceutically acceptable carrier” refers to any of the standard pharmaceutical carriers, such as a phosphate buffered saline solution, water, emulsions (e.g., such as an oil / water or water / oil emulsions), and various types of weting agents. The compositions also can include stabilizers and preservatives. For examples of carriers, stabilizers and adjuvants, see e.g., Martin, Remington's Pharmaceutical Sciences, 15th Ed., Mack Publ. Co.. Easton, PA (1975).

[0053] The terms “a” and “an” as used herein mean “one or more” and include the plural unless the context is inappropriate.

[0054] As used herein, all numerical values or numerical ranges include whole integers within or encompassing such ranges and fractions of the values or the integers within or encompassing ranges unless the context clearly indicates otherwise. Thus, for example, reference to a range of 90-100%, includes 91%, 92%, 93%, 94%, 95%, 95%, 96%, 97%, etc., as well as 91.1%, 91.2%, 91.3%, 91.4%, 91.5%, etc.. 92.1%. 92.2%. 92.3%. 92.4%. 92.5%. etc., and so forth. In another example, reference to a range of 1-5,000-fold includes 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, fold, etc., as well as 1.1, 1.2, 1.3, 1.4, 1.5, fold, etc., 2.1, 2.2, 2.3, 2.4, 2.5, fold, etc., and so forth.

[0055] “About” a number, as used herein, refers to range including the number and ranging from 10% below that number to 10% above that number. “About” a range refers to 10% below the lower limit of the range, spanning to 10% above the upper limit of the range.

[0056] “Percent (%) identity” refers to the extent to which two sequences (nucleotide or amino acid) have the same residue at the same positions in an alignment. For example, “an amino acid sequence is X% identical to SEQ ID NO: Y” refers to % identity of the amino acid sequence to SEQ ID NO: Y and is elaborated as X% of residues in the amino acid sequence are identical to the residues of sequence disclosed in SEQ ID NO: Y. Generally, computer programs are employed for such calculations. Exemplary programs that compare and align pairs of sequences include ALIGN (Myers and Miller, 1988), FASTA (Pearson and Lipman, 1988; Pearson, 1990) and gapped BLAST (Altschul et al., 1997), BLASTP, BLASTN, or GCG (Devereux et al., 1984).ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0057] As used herein, the term “total TL1 A” refers to both monomeric and trimeric TL1A including soluble form thereof.

[0058] An improvement in disease or an alleviation of clinical symptoms can be characterized as a complete alleviation of one or more symptoms, where the subject has or displays no clinical symptoms of the disease, or a partial alleviation of symptoms, where the subject displays at least a 20% improvement in one or more of clinical symptoms of the disease.

[0059] Throughout the description, where compositions are described as having, including, or comprising specific components, or where processes and methods are described as having, including, or comprising specific steps, it is contemplated that, additionally, there are compositions of the present disclosure that consist essentially of, or consist of. the recited components, and that there are processes and methods according to the present disclosure that consist essentially of, or consist of, the recited processing steps.

[0060] As a general mater, compositions specifying a percentage are by weight unless otherwise specified. Further, if a variable is not accompanied by a definition, then the previous definition of the variable controls.Tumor necrosis factor (TNF)-like cytokine 1 A (TL1 A) is part of the TNF superfamily and is a transmembrane protein expressed by myeloid mononuclear cells and endothelial cells, as well as T cells and B cells. It is a pro-inflammatory cytokine that plays a key role in regulating immune responses, particularly in the context of autoimmune and inflammatory diseases. It is primarily produced by immune cells such as dendritic cells, T cells, and macrophages, and it exerts its effects by interacting with its receptor Death Receptor 3 (DR3), which is found on various immune cells. In addition to immune cells, fibroblasts or fibroblast-like cells respond to TL1A by secreting additional inflammatory cytokines, including IL-6, IL-5, and IL-13. TL1A can be found as a soluble molecule in the airways. TL1A interacts with its receptors, membrane-bound death receptor 3 (DR3) and soluble decoy receptor 3 (DcR3), or TL1 A / tumor necrosis factor receptor 2. to trigger signaling. TL1A is elevated in individuals with inflammatory diseases, for example inflammatory dermatologic diseases (e.g. for example eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, and pemphigus, inflammatory bowel disease, systemic lupus erythematosus and ankylosing spondylitis), and DR3 expression is upregulated in inflamed tissue. By binding to DR3, TL1A may enhance the activation of T cells, leading to the release of inflammatory cytokines like IL-16. IL-17, IL-4, IL-13, and IL-5. Soluble TL1A exists in both monomeric and trimeric form in vivo and in vitro. Trimers dissociate naturally into monomers. TL1A is active as a homotrimer. Trimeric TL1A induces trimerization of DR3 receptors on the cell surface that is necessary for downstream signaling. In contrast, while the ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 monomeric TL1 A can bind DR3 receptors on T cells, it cannot induce trimerization of the DR3 receptors, and is, therefore, biologically inactive. Typical serum levels of soluble TL1A are about 100 pg / mL or below in humans. In contrast, patients with autoimmune diseases often exhibit elevated levels.

[0061] Current biologies targeting TNF are associated with serious side effects and infection, require frequent drug administration and are ineffective in a subset of patients highlighting the need for improved therapies targeting TL1 A with favorable safety and dosing profiles to improve patient care.

[0062] Aspects of the disclosure provide a method for treating inflammatory dermatologic diseases, including, but not limited to, eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hi dradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo and pemphigus, by administering a TL1 A inhibitor, e.g., an anti-TLl A antibody. In some embodiments, the TL1A inhibitor is an anti-TLIA antibody. In an embodiment, an anti-TLl A antibody is a fully human antibody, a humanized antibody, or a chimeric antibody. In an embodiment, the antibody is a fully human antibody. The anti-TLIA antibody may be modified to extend its half-life. The anti-TLIA antibody may also be modified to reduce Fc functional activity. Administration of the TL1A inhibitor, such as an anti-TLIA antibody, can result in improvement of one or more of inflammation, disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, or skin lesions. The treatment may be as effective as or even more effective than treatment with a TNF inhibitor. Treatment with the TL1A inhibitor, such as an anti-TLIA antibody, can begin prior to full symptom development, or after full symptom development. Treatment with the TL1A inhibitor, such as an anti-TLIA antibody, can begin at disease onset, or after disease onset. Treatment with the TL1A inhibitor, such as an anti-TLIA antibody, can begin at disease onset or prior to full symptom development, or after disease onset and full symptom development.

[0063] In some embodiments, an anti-TLIA antibody, as described herein, can preferentially bind to soluble human TL1A (sTLl A) relative to any TLlA-related TNFSF members. In some embodiments, an anti-TLIA antibody, as described herein, can have higher binding affinity for soluble human TL1 A relative to any TL1 A-related TNFSF members. In some embodiments, an anti-TLIA antibody, as described herein, may not bind to any TL1 A-related TNFSF members.

[0064] In some embodiments, an anti-TLIA antibody, as described herein, can have a concentration-dependent inhibitory effect on apoptosis induced by the combination of cycloheximide and TL1A in TF-1 cells, a human erythroleukemia cell line that expresses high levels of endogenous DR3. In some embodiments, an anti-TLIA antibody, as described herein, ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 can have a concentration-dependent inhibitory effect on binding of TL1A to DcR3 receptors, DR3 receptors, or combinations thereof. In some embodiments, an anti-TLIA antibody, as described herein, can inhibit human TLlA's ability to induce apoptosis and elicit IFNgamma secretion. In some embodiments, an anti-TLIA antibody, as described herein, shows enhanced binding (i.e., lower KD) to human FcRn at pH 5.8 compared to a control antibody lacking a YTE modification. In some embodiments, an anti-TLIA antibody, as described herein, does not bind to human FcRn at pH 7.2. In some embodiments, an anti-TLIA antibody, as described herein, does not bind to activating Fc receptors CD16a. CD16b, CD32a, CD32b or CD64 or to complement component Clq.

[0065] In some embodiments, the TL1A inhibitor, such as an anti-TLIA antibody, is administered in an effective amount to the subject at the onset of the disease. In other embodiments, the TL1 A inhibitor, such as an anti-TLIA antibody is administered in an effective amount to the subject in need thereof before the full symptoms of the inflammatory dermatologic diseases appear. In other embodiments, the TL1A inhibitor, such as an anti-TLIA antibody is administered in an effective amount to the subject after the full symptoms of the inflammatory dermatologic diseases appear. The TL1 A inhibitor, such as an anti-TLIA antibody, can be administered intravenously or subcutaneously.

[0066] In some embodiments, the inflammatory dermatologic diseases are characterized by¬ causing an immune system response, inflammation, disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, often the development of lesions such as plaques, rashes, or blisters. A disrupted skin barrier impairs the skin’s natural protective function, which can lead to moisture loss and vulnerability to infections and irritants. These diseases may also lead to inflammation of joint, the kidneys, or the cardiovascular system.

[0067] The TL1A inhibitor, such as an anti-TLIA antibody, may be administered to the subject, which may include primates such as humans and non-human primates, or a rat model, to treat inflammatory dermatologic diseases such as eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo and pemphigus.

[0068] In some embodiments, administration of an effective amount of the TL1A inhibitor, such as an anti-TLIA antibody, results in improvement of inflammation, disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, or lesions compared to no treatment. In some embodiments, administration of an effective amount of the TL1A inhibitor, such as an anti-TLIA antibody, results in reduction of the rate of progression of the disease. In an embodiment, the treatment the TL1A inhibitor, such as an anti-TLIA antibody, is as effective ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 as TNF inhibitor treatment for treating the inflammatory dermatologic disease. In an embodiment, the treatment the TL1 A inhibitor, such as an anti-TLl A antibody, is more effective than TNF inhibitor treatment for treating the inflammatory dermatologic disease.

[0069] In some embodiments, administration of an effective amount of the TL1A inhibitor, such as an anti-TLl A antibody, results in one or more of reducing inflammation, disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, or lesions. In some embodiments, the inflammation, disrupted skin barrier, skin fibrosis, redness, pain, swelling, itching, or lesions are reduced by at least about 10%, by at least about 20%, by at least about 30%, by at least about 40%, by at least about 50%, by at least about 60%, by at least about 70%, or by at least about 80%. In some embodiments, administration of an effective amount of the TL1A inhibitor, such as an anti-TLl A antibody, results in improvement of the disease treated as measured by ery throcyte sedimentation rate (ESR), levels of C -reactive protein, or combination thereof. In some embodiments, administration of an effective amount of the TL1 A inhibitor, such as an anti-TLIA antibody, results in improvement of the disease treated as measured by erythrocyte sedimentation rate (ESR), levels of C-reactive protein, or combination thereof by at least about 10%, by at least about 20%, by at least about 30%, by at least about 40%, by at least about 50%, by at least about 60%, by at least about 70%, or by at least about 80%.

[0070] In some embodiments, administration of an effective amount of the TL1A inhibitor, such as an anti-TLIA antibody, results in improvement of the disease treated as measured by disease activity score.

[0071] In some embodiments, administration of an effective amount of the TL1 A inhibitor, such as an anti-TLIA antibody, results in in one or more of the following: changes in cytokine levels, particularly serum cytokine levels, modified histopathology, e.g., of skin lesion biopsy tissue, modulation of fibroblast or fibroblast-like cells and altered RNA expression, e.g., in peripheral blood cells and / or skin cells compared to no treatment.

[0072] In some embodiments, administration of an effective amount of the TL1A inhibitor, such as an anti-TLIA antibody, results in reduction of the levels of serum cytokines, reduction of serum anti-collagen antibodies, modified histopathology, modulation of fibroblast or fibroblast-like cells and altered RNA expression in peripheral blood cells compared to no treatment. In some embodiments, administration of an effective amount of the anti-TLIA antibody to the subject results in a decrease of the level of cytokines, such as, TNF, TL1 A, IL-I, IL-4, IL-5, IL-6, IL-13, IL-17, and / or INFgamma. In some embodiments, administration of an effective amount of the anti-TLIA antibody to the subject results in a decrease of the level ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 of TNF, IL-6, IL- 17 or combination thereof.

[0073] In some embodiments, the TL1 A inhibitor, such as an anti-TLl A antibody, may be at least as effective as TNF inhibitor for managing a inflammatory dermatologic disease. In another embodiment, the TL1A inhibitor, such as an anti-TLIA antibody, is more effective than a TNF inhibitor for managing an inflammatory dermatologic disease.

[0074] Described herein, in certain embodiments, are methods of treating a inflammatory dermatologic diseases in a patient in need thereof, the method comprising subcutaneously or intravenously administering to the patient an effective amount of an anti-TLIA antibody disclosed herein. In some embodiments, the method comprises administering one or more effective amounts of the anti-TLIA antibody subcutaneously or intravenously. In some embodiments, the anti-TLIA antibody is a long acting (i.e. half-life extended) anti-TLIA antibody. In some embodiments, the long acting anti-TLl A antibody is administered subcutaneously or intravenously.

[0075] In some embodiments, methods of treatment described herein comprise administering an effective amount of a TL1A inhibitor (e.g, an anti-TLIA antibody), to a subject (e.g., a human) in need of treatment. In some embodiments, the effective amount of the anti-TLIA antibody is at least 200 mg, at least 300 mg, at least 400 mg, at least 500 mg, at least 600 mg, at least 700 mg, at least 800 mg, at least 900 mg, at least 1000 mg, at least 1100 mg, at least 1200 mg, at least 1300 mg, at least 1400 mg, or at least 1500 mg. In some embodiments, the effective amount of the anti-TLIA antibody is in a range of from about 200 mg to about 2000 mg, from about 300 mg to about 2000 mg, from about 400 mg to about 2000 mg, from about 500 mg to about 2000 mg, from about 800 mg to about 2000 mg, from about 1000 mg to about 2000 mg, from about 1200 mg to about 2000 mg, from about 1500 mg to about 2000 mg, from about 1800 mg to about 2000 mg. from about 200 mg to about 1800 mg. from about 300 mg to about 1800 mg, from about 400 mg to about 1800 mg, from about 500 mg to about 1800 mg, from about 800 mg to about 1800 mg, from about 1000 mg to about 1800 mg, from about 1200 mg to about 1800 mg, from about 1500 mg to about 1800 mg, from about 200 mg to about 1500 mg, from about 300 mg to about 1500 mg, from about 400 mg to about 1500 mg, from about 500 mg to about 1500 mg, from about 800 mg to about 1500 mg, from about 1000 mg to about 1500 mg, from about 1200 mg to about 1500 mg, from about 200 mg to about 1200 mg, from about 300 mg to about 1200 mg, from about 400 mg to about 1200 mg, from about 500 mg to about 1200 mg, from about 800 mg to about 1200 mg, from about 1000 mg to about 1200 mg, from about 200 mg to about 1000 mg, from about 300 mg to about 1000 mg, from about 400 mg to about 1000 mg, from about 500 mg to about 1000 mg, from about 800 mg to about 1000 mg, from about 200 mg to about 800 mg, from about 300 mg to about 800 mg, from about 400 mg to ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 about 800 mg, from about 500 mg to about 800 mg, from about 200 mg to about 500 mg, from about 300 mg to about 500 mg, from about 400 mg to about 500 mg, from about 200 mg to about 400 mg, from about 300 mg to about 400 mg, or from about 200 mg to about 300 mg. In some embodiments, the effective amount of the anti-TLIA antibody is about 200 mg, about 300 mg, about 400 mg, about 500 mg, about 600 mg, about 700 mg, about 800 mg, about 900 mg, about 1000 mg, about 1100 mg, about 1200 mg, about 1300 mg, about 1400 mg, about 1500 mg, about 1600 mg, about 1700 mg, about 1800 mg, about 1900 mg or about 2000 mg. In some embodiments, the administering of the effective dose of the anti-TLIA antibody in the subject reduces soluble TL1A levels from baseline (e.g, about 90% suppression of free serum sTLAl). Alternatively, the administering of the effective dose of the anti-TLIA antibody in the subject reduces soluble TL1A levels from about 500 pg / mL in serum (baseline) to about 100 pg / mL in serum. In some embodiments, the anti-TLIA antibody is administered subcutaneously or intravenously in an induction phase, and subcutaneously in a maintenance phase. In a specific embodiment, the anti-TLIA antibody is an extended half-life anti-TLIA antibody. In some embodiments, methods of treatment described herein comprise administering of the extended half-life anti-TLIA antibody. In some embodiments, the extended half-life anti-TLIA antibody is administered Q24W or Q6M. In specific embodiments, a maintenance dose of the extended half-life anti-TLIA antibody is administered Q12W / Q3M or Q24W / Q6M subcutaneously. In another embodiment, a maintenance dose of the extended half-life anti-TLIA antibody is administered Q52W subcutaneously. In another embodiment, a maintenance dose of the extended half-life anti-TLIA antibody is administered Q104W subcutaneously. In some embodiments, the maintenance dose of the extended half-life anti-TLIA antibody described herein is administered subcutaneously from Q12W to Q104W. In each of the foregoing therapeutic regimen, subcutaneous administration can be by autoinjector.

[0076] In some embodiments, the inflammatory dermatologic disease is eczema, a chronic inflammatory skin disease. Key pathophysiological features include immune dysregulation, and defective skin barrier function, leading to increased transepidermal water loss and enhanced permeability to irritants and allergens and exacerbates dryness and inflammation. This triggers a Th2-dominant immune response, with elevated levels of IL-4, IL-13, and IL-5, promoting IgE production and eosinophil recruitment. Over time, a shift toward Thl and Th 17 responses can occur, contributing to a mixed inflammatory response. Atopic dermatitis (AD) is the most common type of eczema out of seven different types (i.e., atopic dermatitis, contact dermatitis, neurodermatitis, dyshidrotic eczema, nummular dermatitis, seborrheic dermatitis, and stasis dermatitis). The main difference between the different types of eczema is the location where skin irritation manifests and the trigger or source of the reaction. Diagnosis ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 is primarily clinical, supported by serum IgE levels and skin prick or patch testing for allergen sensitivities. Current treatment focuses on topical corticosteroids, calcineurin inhibitors, emollients for barrier repair, and biologies targeting IL-4 or IL- 13. Eczema occurs in approximately 10% of the population in the United States.

[0077] In other embodiments, the inflammatory dermatologic disease is dermatomyositis (DM), which is an autoimmune disease characterized by chronic inflammation of skeletal muscles and skin. It primarily affects proximal muscles (e.g., shoulders, hips) and leads to muscle weakness. The skin findings in DM are distinctive and include the heliotrope rash (a purple, swollen rash around the eyelids), Gottron’s papules (raised, erythematous lesions over the knuckles, elbows, and knees), and shawl sign (a rash on the upper back and shoulders). The disease is associated with T cell-mediated immune responses, where CD4+ T cells atack muscle fibers, leading to muscle fiber necrosis and inflammation. Microvascular damage in both skin and muscle is a hallmark of DM, causing endothelial cell injury and vascular leakage. In adult cases, DM is frequently associated with malignancies, particularly in older patients, a phenomenon known as paraneoplastic dermatomyositis, with cancers like ovarian, lung, breast, and gastrointestinal malignancies being the most common. The pathogenesis of DM also involves type I interferons and the activation of the complement system. Serological testing often reveals elevated muscle enzymes, such as creatine kinase (CK) and aldolase, and autoantibodies, including anti-Mi-2 and anti-Jo-1. Diagnosis is further supported by muscle biopsy, which typically shows perifascicular atrophy, inflammatory infiltrates, and vascular damage. Immunosuppressive therapies, including corticosteroids, methotrexate, or azathioprine, are typical treatment methods to control inflammation, prevent muscle damage, and improve symptoms. Early diagnosis and management are crucial, as untreated DM can lead to irreversible muscle damage and disability.

[0078] In other embodiments, the inflammatory dermatologic disease is pemphigus, which is an autoimmune blistering disorder characterized by the formation of blisters and erosions on the skin and mucous membranes due to the disruption of cell-cell adhesion in the epidermis. This is caused by the production of autoantibodies against desmogleins, which are cadherin-like glycoproteins that mediate cell adhesion. The most common forms are pemphigus vulgaris (PV), which affects deeper layers of the skin and mucosal surfaces, and pemphigus foliaceus (PF), which primarily cause superficial skin blisters. The disease is typically mediated by IgG antibodies, leading to acantholysis (loss of intercellular connections) and Nikolsky's sign (skin detachment upon gentle pressure). Diagnosis is confirmed through skin lesion biopsy, revealing acantholysis and direct immunofluorescence, which shows the presence of IgG autoantibodies binding to epidermal cells. Current treatment involves ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 immunosuppressive therapies, such as corticosteroids and azathioprine, with biologies targeting CD20+ B cells (e.g., rituximab). Early diagnosis and management are essential to prevent severe complications and improve long-term outcomes.

[0079] In other embodiments, the inflammatory' dermatologic disease is psoriasis, which is a chronic, immune-mediated skin disorder characterized by accelerated keratinocyte proliferation and altered differentiation, leading to the formation of thick, scaly plaques on the skin. It is primarily driven by an overactive immune response, involving T cells, particularly CD4+ Thl7 cells, which release proinfl ammatory cytokines such as IL-17 and IL-22. These cytokines promote the activation of keratinocytes and the formation of psoriatic plaques, while also contributing to inflammation and the recruitment of other immune cells like neutrophils and dendritic cells. Psoriasis can be triggered by various factors, including genetic predisposition, environmental factors (e.g., infections, trauma, stress, and medications), and dysregulated skin barrier function. The most common type is psoriasis vulgaris, which presents as raised, erythematous plaques covered with silver-white scales. Other forms include gutate, inverse, pustular, and erythrodermic psoriasis. The condition can also be associated with systemic comorbidities, including psoriatic arthritis, cardiovascular disease, and metabolic syndrome. Diagnosis is clinical, based on characteristic skin lesions, and sometimes confirmed with skin lesion biopsy. Treatment options include topical therapies (e.g.. corticosteroids, vitamin D analogs), phototherapy (e.g.. narrowband UVB (NB-UVB)), and systemic treatments such as biologies targeting immune pathways (e.g, IL-17, IL-23, and TNF inhibitors) and oral immunosuppressants (e.g., methotrexate, cyclosporine, acitretin, sulfasalazine, and my cophenolate mofetil). Psoriasis occurs in 2 to 3% of people in the United States.

[0080] In other embodiments, the inflammatory dermatologic disease is scleroderma (also known as systemic sclerosis), a chronic autoimmune disease characterized by excessive collagen deposition leading to skin thickening and fibrosis of internal organs. It involves immune dysregulation, with autoantibodies targeting desmogleins and other self-antigens, leading to vascular injury and fibrosis. There are two major subtypes: limited cutaneous systemic sclerosis, which primarily affects the skin of the fingers, face, and forearms and may lead to pulmonary hypertension and gastrointestinal issues, and diffuse cutaneous systemic sclerosis, which affects more extensive areas of the skin and causes severe organ involvement such as interstitial lung disease (ILD), renal crisis, and cardiac complications. Pulmonary complications, particularly pulmonary hypertension and ILD, are the leading causes of death in people with scleroderma. Scleroderma can cause pulmonary sclerosis (also called pulmonary' fibrosis) as a result of excessive buildup of collagen in the lungs, leading to ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 scarring and thickening of lung tissue, which may result in impairment of lung function and can lead to respiratory problems. Through the overall disease process, pulmonary sclerosis can indirectly lead to skin changes, limited blood flow (Raynaud’s phenomenon), inflammation, and scarring. Diagnosis is based on clinical features, supported by serological testing for autoantibodies (e.g., anticentromere and anti-Scl-70) and imaging studies like HRCT for lung involvement. Treatment includes immunosuppressive agents (e.g., methotrexate, cyclophosphamide), antifibrotic medications (e.g., pirfenidone), and vasodilators (e.g., sildenafil) to manage symptoms and prevent complications, although there is no cure. The prognosis varies, with limited scleroderma having a more favorable outlook, while diffuse scleroderma can be more aggressive, especially with early organ involvement.

[0081] In other embodiments, the inflammatory dermatologic disease is hidradenitis suppurativa (HS). Hidradenitis suppurativa is also called acne inversa or Vemeuil’s disease. HS is a chronic, immune-mediated inflammatory dermatologic disease. It is a skin disorder of the apocrine glands and hair follicles. It affects approximately 1% of the general population in the West, with women being affected more commonly than men. Characteristic lesions such as inflammatory nodules, abscesses, and sinus tracts develop in the axillae, inguinal, and gluteal areas, typically during or after puberty. Factors that contribute to the disease include genetic and epigenetic changes, and hormonal, mechanical, microbial and lifestyle factors such as obesity and smoking. Immunological abnormalities of the hair follicle can play a role in the etiology of the disease. HS is characterized by recurrent inflamed nodules, abscesses, and fistulas, and it occurs when apocrine gland outlets become blocked by perspiration or are unable to drain normally, causing cyst formation and rupture induce acute inflammation, characterized by a mixed immune infiltrate of neutrophils, macrophages, dendritic cells, and T and B cells and increased expression of proinfl ammatory cytokines such as IL-1 [3, IL- 17, and TNF-a. Swollen, painful, chronically inflamed lesions or lumps develop in the groin and sometimes under the arms and under the breasts. Treatment includes long-term antibiotic therapy, immunosuppressive agents (e.g., methotrexate, cyclophosphamide), retinoids, tumor necrosis factor-a (TNF-a) inhibitors to manage symptoms. To date, there are no approved therapies for this disease in the US.

[0082] In other embodiments, the inflammatory dermatologic disease is Cutaneous Lupus Erythematosus (CLE). CLE is a diverse group of autoimmune connectivetissue disorders localized to the skin that can be associated with systemic lupus erythematosus (SLE) to varying degrees. CLE is classified as acute CLE (ACLE), subacute CLE (SCLE), and chronic CLE (CCLE). The disease is characterized by atypical histological patern consisting of colloid bodies and an anti-epidermal cytotoxic lymphocytic infiltrate in the ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 dermoepidermal junction which is driven by IFN-regulated proinfl ammatory cytokines. CLE is often associated with systemic lupus erythematosus (SLE). CLE is more common than SLE in men and older adults. ACLE is frequently associated with active SLE. The risk of progression to SLE is highest among patients with SCLE. The factors that contribute to pathogenesis in CLE include genetic predisposition, environmental stressors such as ultraviolet (UV) radiation and smoking, and drivers of chronic activation of the immune system, such as upregulation of type I Interferon (IFN) signaling. Treatment of CLE includes avoidance of triggering factors and use of topical corticosteroids, topical calcineurin inhibitors, hydroxychloroquine, immunosuppressive agents, such as methotrexate, and immunotherapy (e.g. Anifrolumab, a monoclonal antibody targeting IFNAR, Belimumab, a B-lymphocyte stimulator (BLyS) inhibitor, Litifihmab, an anti-BDCA2 antibody).

[0083] In other embodiments, the inflammatory dermatologic disease is alopecia areata.Alopecia areata is a chronic, immune-mediated autoimmune disorder that affects hair follicles, nails, and, occasionally, the retinal pigment epithelium. Inflammatory cells target the hair follicle matrix epithelium undergoing early cortical differentiation or anagen hair follicles, prematurely pushing them into the catagen or telogen phase. The condition leads to hair loss without permanent damage to the follicles. The risk of developing alopecia areata in the general population is estimated at 2%. The condition occurs more often among Asian. Black, and Hispanic patients, with a mean age of about 35 years. Triggers include emotional or physical stress, vaccinations, viral infections, and medications. Treatment includes corticosteroids, immunotherapy, Janus kinase (JAK) inhibitors, and topical solutions.

[0084] In other embodiments, the inflammatory dermatologic disease is vitiligo. Vitiligo is a pigmentary' skin disorder that results from the loss of melanocytes from the epidermis and clinically manifests as well-demarcated white macules on the body. In vitiligo, there is a total loss of functioning melanocytes in association with the complete loss of epidermal pigmentation. Vitiligo is associated with multiple autoimmune diseases. While it can appear at any age, it peaks at 20-30 years and affects 0.1 to 2% of people. Treatment includes topical medications (corticosteroids, calcineurin inhibitors, and vitamin D analogs) and systemic medications (Afamelanotide and JAK inhibitor therapy), phototherapy, laser therapy, and surgical therapy medications.

[0085] In some embodiments, a method of treating psoriasis in a subject (e., adult patients) in need thereof comprises administering an effective amount of an extended half-life of an anti-TL1A antibody, as described herein, subcutaneously or intravenously in an induction phase, and subcutaneously in a maintenance phase. In some embodiments, the subject is advanced therapy naive or experienced. The PASI (Psoriasis Area and Severity' Index) is a physician-assessed tool ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 to measure the extent and severity of skin involvement in psoriasis and is used to evaluate response to treatment. A PASI score can range from 0 to 72, wherein higher scores indicate a more severe disease. In some embodiments, the administering of the effective amount of an extended half-life of the anti-TLl A antibody result is a PASI75 or a PASI90, i.e. a 75% or a 90% reduction of the PASI score from baseline (e.g. before treatment), which are indicative of disease improvement.TL1A inhibitors

[0086] Death-domain receptor 3 (DR3) is a tumor necrosis factor receptor family member expressed specifically on T cells, natural killer (NK) cells, natural killer T (NKT), some dendritic cell types, and some fibroblast cell types. The ligand for DR3 is TL1 A, a TNF family member protein reported to be expressed by myeloid mononuclear cells, endothelial cells, and B and T cells, and endothelial cells.

[0087] The interaction between DR3 and TLIA can be blocked using inhibitors that directly interfere with the interaction between DR3 and TLIA, for example, by an inhibitor that binds to DR3 at its binding site for TLIA or an inhibitor that binds to TLIA at its binding site for DR3.

[0088] The interaction between DR3 and TLIA can be blocked by administration of an anti-TL1A antibody. In some embodiments, administration of the anti-TLIA antibody reduces an amount of free soluble TLIA (sTLl A) in the subject compared to no treatment. In one embodiment, such an antibody has the heavy and light chain sequences, or the heavy chain variable region and light chain variable region sequences, or the heavy chain CDR sequences as set out in PCT application No. PCT / US24 / 41774 entitled " TLIA BINDING PROTEINS AND METHODS OF USE." or PCT application No PCT / US24 / 34949 entitled " TLIA ANTIBODY COMPOSITIONS AND METHODS OF USE", as set forth above, which are incorporated by reference in their entireties.

[0089] The method comprises treating inflammatory dermatologic disease in a subject in need thereof by administering an inhibitor of TLIA binding to TLIA receptor, hereinafter a ‘“TLIA inhibitor.”

[0090] Provided herein are compositions, systems, and methods comprising a TLIA inhibitor. In some embodiments, the TLIA inhibitor is a small molecule TLIA inhibitor. In some embodiments, the TLIA inhibitor is a TLIA small molecule allosteric inhibitor. In some embodiments, the TLIA inhibitor is a TLIA binding protein. In some embodiments, the TLIA inhibitor is an anti-TLIA antibody or binding fragment thereof. In some embodiments, the compositions are injectable liquid compositions. In some embodiments, the compositions are injectable liquid composition for intravenous administration. In some embodiments, the ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 compositions are injectable liquid composition for subcutaneous administration.

[0091] The TL1A binding proteins described herein can bind to TL1A monomers and / or TL1A trimers. In some embodiments, the TL1 A binding protein is an anti-TLl A antibody having picomolar potency against TL1A monomers, TL1A trimers, or both. In some embodiments, the anti-TLIA antibody, as described herein, binds to monomeric TL1A, trimeric TL1A. or monomeric and trimeric TL1A. In some embodiments, the anti-TLIA antibody binds to monomeric TL1 A. In some embodiments, the anti-TLIA antibody binds to monomeric TL1 A and trimeric TL1 A. In some embodiments, the anti-TLIA antibody neutralizes the monomeric TL1A, trimeric TL1A, or both monomeric and trimeric TL1 A. In some embodiments, the anti-TLIA antibody neutralizes the monomeric TL1A, trimeric TL1A, or both monomeric and trimeric TL1A by from about 50% to about 99% or more (e.g. 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, or 99% of the monomeric TL1A, trimeric TL1 A, or both monomeric and trimeric TL1A. For example, the anti-TLIA antibody can neutralize both the monomeric and trimeric TL1A. In some embodiments, the anti-TLIA antibody blocks binding of TL1A to DR3 receptors, DcR3 receptors or DR3 receptors and DcR3 receptors. In some embodiments, the anti-TLIA antibody reduces TL1A concentration in a diseased tissue.

[0092] In some embodiments, the anti-TLIA antibody, as described herein, binds to TL1A trimer (homotrimers) only. In some embodiments, binding to the TL1A trimer stabilizes the timer. In some embodiments, binding of the antibody to the TL1 A trimer makes the TL1 A trimer inactive, whether or not it stabilizes the trimer configuration. In some embodiments such a trimer-binding antibody does not bind to the TL1 A monomer. In some embodiments, such a trimer-binding antibody can bind to more than one trimer. In some embodiments, each trimer-binding antibody can bind up to two TL1 A trimers. In some embodiments, each TL1 A trimer can bind up to three trimer-binding antibodies. In some embodiments, an effective amount of a trimer-binding antibody is administered in a subject in need thereof for treating inflammatory conditions (e.g., psoriasis). In some embodiments, clearance of trimer-binding antibodies may involve unbound trimer-binding antibodies and antibody-TLl A complexes, wherein the antibody -TL1A complexes can comprise one or more TL1A trimers bound to one or more antibodies. In some embodiments, an antibody-TLIA complex formed by anti-TLIA antibody and TL1 A trimer at a ratio of 3: 1 exhibits faster clearance relative to an antibody-TLIA complex that comprises less than 3: 1 ratio of the anti-TLIA antibody and TL1 A trimer. For example, in some embodiments, a TL1 A trimer bound to three antibodies exhibit faster clearance relative to a TL1A trimer bound to less than three antibodies (e.g., two or one). In some embodiments, treatment with the trimer-binding antibody does not affect the rate of ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 synthesis of TL1 A monomer. In some embodiments, treatment with the trimer-binding antibody does not affect the rate of saturation / equilibration of PD. Non-limiting exemplary trimer-binding anti-TLIA antibodies include Antibody 10, Antibody 47, Antibody 49, Antibody 69, Antibody 71 and Antibody 92.

[0093] In other embodiments, the anti-TLIA antibody, as described herein, is a disruptor that binds monomer and trimer. In some embodiments, the disruptor promotes dissociation of homotrimers into TL1 A monomers. In some embodiments, the disruptor can bind to more than one TL1 A monomer. For example, in some embodiments, each disruptor can bind up to two TL1A monomers. In some embodiments, an effective amount of a disruptor is administered in a subject in need thereof for treating inflammatory conditions (e.g, psoriasis). In some embodiments, clearance of disruptors may contain unbound disruptors and antibody -TL1A complex complexes, wherein the antibody-TLIA complex complexes can comprise disruptors bound to TL1 A trimers and / or TL1 A monomer(s). In some embodiments, treatment with the disruptors does not affect the rate of synthesis of TL1 A monomers. In some embodiments, treatment with the disruptors does not affect the rate of saturation / equilibration of PD. Nonlimiting exemplar^' disruptors include Antibody 19, Antibody 63, Antibody 86 and Antibody 98.

[0094] In some embodiments, an antibody-TLIA complex of an anti-TLIA antibody and a TL1A trimer, when comprises 3:1 ratio of the anti-TLIA antibody to the TL1A trimer, exhibits at least 10%, at least 20%, at least 30%, at least 50%, at least 80%, at least 100% or more faster rate of clearance relative to an antibody-TLIA complex comprising less than 3: 1 ratio of the anti-TLIA antibody to the TL1A trimer. In some embodiments, the trimer-binding anti-TLIA antibody (stabilizer), upon selectively binding to a TL1 A trimer, decreases rate of dissociation of the TL1A trimer into TL1A monomer by at least 10%, at least 20%, at least 50%, at least 80%, at least 100%, or more compared to no treatment. In some embodiments, the anti-TLIA antibody (disruptor), upon binding to TL1 A trimer. increases rate of dissociation of the TL1 A trimer into TL1A monomer by at least 10%, at least 20%, at least 50%, or more, compared to no treatment.

[0095] In some embodiments, the anti-TLIA antibody, as described herein, binds monomer and trimer. wherein the anti-TLIA antibody does not promote dissociation of homotrimers into TL1 A monomer(s). In some embodiments, the anti-TLIA antibody, upon contacting a TL1A trimer, modifies a rate of dissociation of the TL1 A trimer into TL1 A monomer less than 5%, less than 3%, less than 2%, less than 1%, or lesser compared to the rate of dissociation of the TL1A trimer prior to the contacting. In some embodiments, the anti-TLIA antibody, as described herein, selectively binds monomer(s) and does not bind trimers.ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0096] Disclosed herein are anti-TLIA antibodies, excluding RVT-3101, MK-7240 and / or TEV -48574, that (1) bind TL1 A trimer and optionally stabilize TL1 A trimer and do not bind TL1 A monomer; (2) bind TL1 A trimer and TL1 A monomer, and on binding TL1A trimer disrupts TL1 A trimer into TL1A monomer(s); (3) bind TL1A trimer and TL1 A monomer: or (4) selectively bind TL1 A monomer, wherein the anti-TLIA antibodies do not bind TL1 A trimer and do not disrupt TL1 A trimer into TL1 A monomer(s).

[0097] In some embodiments, an antibody-TLIA complex of an anti-TLIA antibody and a TL1A trimer, when comprising a 3: 1 ratio of the anti-TLIA antibody to the TL1A trimer, exhibits at least 10%, at least 20%, at least 30%, at least 50%, at least 80%, at least 100% or more faster rate of clearance relative to an antibody-TLIA complex comprising less than 3:1 ratio of the anti-TLIA antibody to the TL1A trimer. In some embodiments, the trimer-binding anti-TLIA antibody (stabilizer), upon selectively binding to a TL1 A trimer, decreases rate of dissociation of the TL1 A trimer into TL1 A monomer by at least 10%, at least 20%, at least 50%, at least 80%, at least 100%, or more compared to no treatment. In some embodiments, the anti-TLIA antibody (stabilizer), upon contacting a TL1 A trimer, decreases a rate of dissociation of the TL1A trimer into TL1A monomer by at least 10%, at least 20%, at least 50%, at least 80%, at least 100%, or more compared to the rate of dissociation of the TL1A trimer prior to the contacting. In some embodiments, the anti-TLIA antibody (disruptor), upon binding to TL1 A trimer, increases rate of dissociation of the TL1 A trimer into TL1A monomer by at least 10%, at least 20%, at least 50%, or more, compared to no treatment. In some embodiments, the anti-TLIA antibody (disruptor), upon contacting a TL1 A trimer, increases a rate of dissociation of the TL1 A trimer into TL1 A monomer by at least 10%, at least 20%, at least 50%, or more, compared to the rate of dissociation of the TL1 A trimer prior to the contacting.

[0098] In some embodiments, the anti-TLIA antibody is a fully human IgGl monoclonal anti-TLIA antibody or IgGl -humanized monoclonal antibody (e.g. RVT-3101, MK-7240, TEV-48574).

[0099] In some embodiments, the anti-TLIA antibody has an extended half-life (e.g., as compared to known TL1A directed antibodies). In some embodiments, the anti-TLIA antibodies described herein allow for less frequent dosing than known TL1 A-directed antibodies, e.g., every 8 weeks or every 12-13 weeks (or 3 months), or every 24-26 weeks (or 6 months), or every 52 weeks (or 12 months or ayear), or every 104 weeks (24 months or 2 years), etc. Anti-TLIA antibodies described herein may also have improved specificity. Anti-TLIA antibodies described herein may have specificity for monomeric and trimeric TL1A and not to related TNF super family proteins TNF, FasL, TRAIL, or LIGHT.ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0100] Binding kinetics of an antibody can be determined by SPR on a BIAcore instrument. In some embodiments, an anti-TLIA antibody has ka(M⁻¹s⁻¹) of 2.0xl06. In some embodiments, an anti-TLIA antibody has kd (s⁻¹) of 5.5×10⁻³. In some embodiments, an anti-TLIA antibody binds TL1A with a dissociation constant (KD) less than about 0.5 nanomolar (nM), optionally less than about 0.4 nM, and optionally less than about 0.3 nM. In a specific embodiment, the anti-TLIA antibody binds TL1 A with a KD of 0.22 nM. In a specific embodiment the anti-TLIA antibody binds TL1 A with a KD of 0.10 nM. In some embodiments, an anti-TLIA antibody binds TL1A with a KD(M) of 3.1×10⁻¹¹. In some embodiments, an anti-TLIA antibody binds TL1A with a KD of about 0.24 nM. In some embodiments, an anti-TLIA antibody, as described herein, does not bind to related TNFSF members TNFa, FasL, TRAIL, or LIGHT.

[0101] In some embodiments, the TL1A binding antibody comprises a heavy chain variable region (VH) comprising (i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 A, TABLE 1.1 B, and TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C. In some embodiments, the TL1 A binding antibody comprises a light chain variable region (VL) comprising (i) aCDRl comprising any one of CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C. In some embodiments, the TL1A binding antibody comprises a modified Fc that extends half-life of the TL1 A binding protein as compared to a TL1A binding protein that does not comprise the ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 modified Fc domain. In some embodiments, the TL1A binding antibody comprises: a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; b) a light chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL 1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE 1.1 B, and TABLE 1.1 C.

[0102] In some embodiments, the TL1A binding antibody comprises: a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; b) a light chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; and c) a modified Fc domain that extends half-life of the TL1A binding protein as compared to a TL1A binding protein that does not comprise the modified Fc domain.

[0103] In some embodiments, the TL1A binding antibody comprises a heavy chain variable region (VH) comprising (i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, or a ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C. In some embodiments, the TL1A binding antibody comprises a light chain variable region (VL) comprising (i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C. In some embodiments, the TL1 A binding antibody comprises a modified Fc domain that extends half-life of the TL1 A binding protein as compared to a TL1A binding protein that does not comprise the modified Fc domain.

[0104] In some embodiments, the TL1A binding antibody comprises: a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C; and b) a light chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C.

[0105] In some embodiments, the TL1A binding antibody comprises: a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C; b) a light chain variable region (VL) comprising (i) a CDR1 having an ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.2 A, TABLE 1.2 B, and TABLE 1.2 C: and c) a modified Fc domain that extends half-life of the TL1 A binding protein as compared to a TL1 A binding protein that does not comprise the modified Fc domain. In some embodiments, the TL1 A binding antibody comprises a heavy chain variable region (VH) comprising (i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C. In some embodiments, the TL1A binding antibody comprises a light chain variable region (VL) comprising (i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C. (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C. In some embodiments, the TL1A binding antibody comprises a modified Fc domain that extends halflife of the TL1 A binding protein as compared to a TL1 A binding protein that does not comprise the modified Fc domain.

[0106] In some embodiments, the TL1A binding antibody comprises: a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C; and b) alight chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C.

[0107] In some embodiments, the TL1A binding antibody compnses: a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C; b) a light chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.3 A, TABLE 1.3 B, and TABLE 1.3 C; and c) a modified Fc domain that extends half-life of the TL1A binding protein as compared to a TL1A binding protein that does not comprise the modified Fc domain.

[0108] In some embodiments, the TL1A binding antibodies comprise a VH comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or 100% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding antibodies comprises a VL comprising a sequence having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, or 100% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2.

[0109] In some embodiments, the TL1A binding antibodies comprise a VH comprising a sequence having at least 80% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2, and a VL comprising a sequence having at least 80% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a VH comprising a sequence having at least 85% sequence identity to the amino acid sequence ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2, and a VL comprising a sequence having at least 85% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a VH comprising a sequence having at least 90% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2, and a VL comprising a sequence having at least 90% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1 A binding protein comprises a VH comprising a sequence having at least 95% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2, and a VL comprising a sequence having at least 95% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a VH comprising a sequence having at least 96% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2, and a VL comprising a sequence having at least 96% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a VH comprising a sequence having at least 97% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2, and a VL comprising a sequence having at least 97% sequence identity to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a VH comprising a sequence having at least 98% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. and a VL comprising a sequence having at least 98% sequence identity’ to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a VH comprising a sequence having at least 99% sequence identity to the amino acid sequence of any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. and a VL comprising a sequence having at least 99% sequence identity’ to the amino acid sequence of any one of VL sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 80% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 85% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2 (SEQ ID NOs: 181-190 and 2275- 2383). In some embodiments, the TL1A binding protein comprises a heavy chain ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 variable region (VH) comprising an amino acid sequence having at least 90% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 95% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 96% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 97% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 98% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence having at least 99% sequence identity with an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2. In some embodiments, the TL1A binding protein comprises a heavy chain variable region (VH) comprising an amino acid sequence according to any one of VH sequences listed in TABLE 2.1 and TABLE 2.2.ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0110] TABLE 1. TL1A SEQUENCESName SEQ ID NO. SequenceHuman TL1A 2493 MAEDLGLSFGETASVEMLPEHGSCRPKARSSSARWALTCCLVLLPFLAGLTTYLLV (TNF15)-1 SQLRAQGEACVQFQALKGQEFAPSHQQVYAPLRADGDKPRAHLTVVRQTPTQHFK NQFPALHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQA GRPNKPDSITVVITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGD KLMVNVSDISLVDYTKEDKTFFGAFLLHuman TL1A 2494 MQLTKGRLHFSHPLSHTKHISPFVTDAPLRADGDKPRAHLTVVRQTPTQHFKNQFPA (TNF15)-2 LHWEHELGLAFTKNRMNYTNKFLLIPESGDYFIYSQVTFRGMTSECSEIRQAGRPNKP DSITWITKVTDSYPEPTQLLMGTKSVCEVGSNWFQPIYLGAMFSLQEGDKLMVNVS DISLVDYTKEDKTFFGAFLL

[0111] TABLE 1.1 A. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 1-4Kabat Numbering (EU index)Name CDRH1 CDRH1 CDRH2 CDRH2 CDRH3 CDRH3 CDRL1 CDRL1 CDRL2 CDRL2 CDRL3 CDRL3 SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID NO NO NO NO NO NOAntibody 1 SYAMH 11 VVSYE 21 LESAY 31 RSSQSL 41 LGSNR 51 MQALQ 1 GSQNY YFDY LYS AS TPYT YADSV NGYNS KG LDAntibody 2 SYYWS 12 LIYYSG 22 ADVVT 32 RASQTI 42 AASSL 52 QQSYS 2 STNYN 1DY SSYF QS TACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 PSLKS N PITAntibody 3 TYNMN 13 SIHSSS 23 DRAMV 33 RASQSI 43 AASSLQ 53 QQSYST 3 NYLYY DFDY STYL S PLT ADSVK N GAntibody 4 SNSAT 14 RTYYRS 24 EAVGPT 34 RASQSF 44 AASSLQ 54 QQSYFT 4 WN KWY KDFDY SSY S PRT NDYAV LNSVKS

[0112] TABLE 1.2 A. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 1-4Chothia NumberingName CDRH CDRH1 CDRH CDRH2 CDRH CDRH3 CDRL CDRL1 CDRL2 CDRL2 CDRL3 CDRL31 SEQ2SEQ 3SEQ 1 SEQ SEQID SEQIDID NO ID NO ID NO ID NO NO NOAntibody SQSLLY61 GFTFSS 71 SYEGSQ 81 ESAYYF 91SNG LGS 111 ALQTPY 1 DYNSAntibody62 GGSISS 72 YYSGS 82 DVVTID 92 SQTISS AAS 112 SYSTPI 2 Y YAntibody63 GFTFST 73 HSSSNY 83 RAMVD 93 SQSIST AAS 113 SYSTPL 3 Y FD YAntibody64 GDSVSS 74 YYRSK 84 AVGPT 94 SQSFSS AAS 114 SYFTPR 4NSA WY KDFDACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0113] TABLE 1.3 A. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 1-4IMGT NumberingCDRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3 Name SEQ ID CDRH1 SEQ ID CDRH2 SEQ ID CDRH3 SEQ ID CDRL1 SEQ ID CDRL2 SEQ ID CDRL3NO NO NO NO NO NO ANLES QSLLYAntibody GFTFSS VSYEG MQALQ 121 131 141 AYYFD 151 SNGYN LGS 1711 YA SQN TPYT Y SAntibody GGSISS IYYSGS ARADV QQSYS 122 132 142 152 QTISSY AAS 1722 YY T VTIDY TPIT ATDRAAntibody GFTFST IHSSSN QQSYS 123 133 143 MVDFD 153 QSISTY AAS 1733 YN YL TPLT Y AREAVAntibody GDSVS TYYRS QQSYF 124 134 144 GPTKD 154 QSFSSY AAS 1744 SNSAT KWYN TPRTFDY

[0114] TABLE 1.1 B. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 5-10Kabat Numbering (EU index)CDRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3 Name SEQ ID CDRH1 SEQ ID CDRH2 SEQ ID CDRH3 SEQ ID CDRL1 SEQ ID CDRL2 SEQ ID CDRL3NO NO NO NO NO NO LIKSKT RASQIFAntibody NVWM DAGTT DRGW GASSR QQYGN 5 15 25 35 SSSYL 45 555 N DYAAP GENY AT SPYT V VKG RIKSKI RASQSAntibody NVWM DAGTT DRGW GASSR QQYGG 6 16 26 36 VSSSY 46 566 N DYVAP GENY AT SPYT LV VKG RIKSKI RASQSIAntibody NAWM DAGTT DLGW GASSR HQYGS 7 17 27 37 SRSYL 47 577 S DYAAP GENY AT SPYTVVKGACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 RIKSKI RASQRAntibody NAWM DAGTT DLGW GASSR QQYGS 8 18 28 38 VSSSY 48 588 S DYAAP GENY AT SPYT LV VKG RIKSKI RASQRAntibody NAWM DAGTT DLGW GASSR QQYGS 9 19 29 39 VSSSY 49 599 T DYAAP GENY AT SPYT LV VKG RIKSKI RASQRAntibody NAWM DAGTT DLGW GASSR QQYGS 10 20 30 40 VSSSY 50 6010 T DYAAP GENY AT SPYTLVVKG

[0115] TABLE 1.2 B. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 5-10Chot lia NumberingCDRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3 Name SEQ ID CDRH1 SEQ ID CDRH2 SEQ ID CDRH3 SEQ ID CDRL1 SEQ ID CDRL2 SEQ ID CDRL3NO NO NO NO NO NOAntibody GFTFS KSKTD RGWGE SQIFSS YGNSP 65 75 85 95 GAS 1155 NV AGT N SYAntibody GFIFSN KSKID RGWGE SQSVSS YGGSP 66 76 86 96 GAS 1166 V AGT N SYAntibody GFTFS KSKID LGWGE SQSISR YGSSP 67 77 87 97 GAS 1177 NA AGT N SYAntibody GFTFS KSKID LGWGE SQRVS YGSSP 68 78 88 98 GAS 1188 NA AGT N SSYAntibody GFTFS KSKID LGWGE SQRVS YGSSP 69 79 89 99 GAS 1199 NA AGT N SSYAntibody GFTFS KSKID LGWGE SQRVS YGSSP 70 80 90 100 GAS 12010 NA AGT N SSY

[0116] TABLE 1.3 B. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 5-10IMGT NumberingCDRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3 Name CDRH1 CDRH2 CDRH3 CDRL1 CDRL2 CDRL3SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ IDACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 NO NO NO NO NO NO TTDRGAntibody GFTFS IKSKTD QIFSSS QQYGN 125 135 145 WGEN 155 GAS 1755 NVW AGTT SPYT Y ITDRGAntibody GFIFSN IKSKID QSVSSS QQYGG 126 136 146 WGEN 156 GAS 1766 VW AGTT SPYT Y TTDLGAntibody GFTFS IKSKID QSISRS HQYGS 127 137 147 WGEN 157 GAS 1777 NAW AGTT SPYT Y TTDLGAntibody GFTFS IKSKID QRVSS QQYGS 128 138 148 WGEN 158 GAS 1788 NAW AGTT SY SPYT Y TTDLGAntibody GFTFS IKSKID QRVSS QQYGS 129 139 149 WGEN 159 GAS 1799 NAW AGTT SY SPYT Y TTDLGAntibody GFTFS IKSKID QRVSS QQYGS 130 140 150 WGEN 160 GAS 18010 NAW AGTT SY SPYTY

[0117] TABLE 1.1 C. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 11-119Kabat Numbering (EU index)Name CDRH1 CDRH1 CDRH2 CDRH2 CDRH3 CDRH3 CDRL1 CDRL1 CDRL2 CDRL2 CDRL3 CDRL3SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID NO NO NO NO NO NOAntibody 313 GYYM 422 WINPK 531 GGSFD 640 RASQSI 749 GASSL 858 QQGFS 11 H SGGTIY AFDI SRYLY QS APLT AQKFQ GAntibody 314 GYYWS 423 EITHSG 532 GQVGT 641 RASQSI 750 AASSL 859 QQSYR 12 ITNYNP TDYYY RRYLN QS TIT SLES FYMDVAntibody 315 GYYM 424 WINPN 533 GGSFD 642 RASQSI 751 GAS SV 860 QQGD13 H SGGTN AFDI SRYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQNF QGAntibody 316 GYYM 425 WINPK 534 GGSFD 643 RASQSI 752 GAS SV 861 QQGD 14 H SGGTN AFDI SRYLN QS SSPFT YAQNF QGAntibody 317 GYYM 426 WINPN 535 GGSFD 644 RASQSI 753 GASSL 862 QQGH 15 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 318 AYYM 427 WINPN 536 GGSFD 645 RASQSI 754 GAS SV 863 QQGD 16 H SGGTN AFDI SRYLN QS SSPFT YAQSF QGAntibody 319 AYYM 428 WINPK 537 GGSFD 646 RASQSI 755 GAS SV 864 QQGD 17 H SGGTN AFDI SRYLN QS SSPFT YAQSF QGAntibody 320 AYYM 429 WINPN 538 GGSYD 647 RASQSI 756 GASRL 865 QQGH 18 H SGGTN AFDI SSYLN QS STPFT YAQQF QGAntibody 321 AYYM 430 WINPK 539 GGSYD 648 RASQSI 757 GASRL 866 QQGH 19 H SGGTN AFDI SSYLN QS STPFT YAQQF QGAntibody 322 AYYIH 431 WINPN 540 GGSFD 649 RASQSI 758 GASSL 867 QQGD 20 SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 323 AYYIH 432 WINPK 541 GGSFD 650 RASQSI 759 GASSL 868 QQGD 21 SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 324 GYYLH 433 WINPN 542 GGSYD 651 RASQSI 760 GASRL 869 QQGD22 SGGTN AFDI SSYLN QS STPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 FAQKF QGAntibody 325 GYYLH 434 WINPK 543 GGSYD 652 RASQSI 761 GASRL 870 QQGD 23 SGGTN AFDI SSYLN QS STPFT FAQKF QGAntibody 326 GYYM 435 WINPN 544 GGSYD 653 RASQSI 762 GASRL 871 QQGD 24 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 327 GYYM 436 WINPK 545 GGSYD 654 RASQSI 763 GASRL 872 QQGD 25 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 328 GYYLH 437 WINPN 546 GGSFD 655 RASQSI 764 GASRL 873 QQGD 26 SGGTN AFDI SSYLN QS SSPFT YAQRF QGAntibody 329 GYYLH 438 WINPK 547 GGSFD 656 RASQSI 765 GASRL 874 QQGD 27 SGGTN AFDI SSYLN QS SSPFT YAQRF QGAntibody 330 GYYM 439 WINPK 548 GGSFD 657 RASQSI 766 GASSL 875 QQGH 28 H SGGTIY AFDI SSYLN QS STPFT AQKFQ GAntibody 331 GYYM 440 WINPK 549 GGSFD 658 RASQSI 767 GASSL 876 QQGD 29 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 332 GYYM 441 WINPK 550 GGSYD 659 RASQSI 768 GASSL 877 QQGH 30 H SGGTS AFDI SSYLN QS STPFT YAQKF QGAntibody 333 GYYM 442 WINPK 551 GGSYD 660 RASQSI 769 GASRL 878 QQGY31 H SGGTN AFDI SSYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 334 AYYIH 443 WINPN 552 GGSFD 661 QASQD 770 GASSL 879 QQGD 32 SGGTN AFDI ISNYLN QS STPFT YAQNF QGAntibody 335 AYYIH 444 WINPK 553 GGSFD 662 QASQD 771 GASSL 880 QQGD 33 SGGTN AFDI ISNYLN QS STPFT YAQNF QGAntibody 336 GYYM 445 WINPK 554 GGSFD 663 RASQG 772 GASSL 881 QQGFS 34 H SGGTN AFDI ISRYLH QS TPFT YAQNF QGAntibody 337 GYYM 446 WINPN 555 GGSYD 664 RASQSI 773 GASRL 882 QQGSS 35 H SGGTN AFDI SSYLN QS PPFT YAQKF QGAntibody 338 GYYM 447 WINPK 556 GGSYD 665 RASQSI 774 GASRL 883 QQGSS 36 H SGGTN AFDI SSYLN QS PPFT YAQKF QGAntibody 339 AYYM 448 WINPN 557 GGSYD 666 RASQSI 775 GASRL 884 QQGY 37 H SGGTK AFDI SSYLN QS SSPFT YAQKF QGAntibody 340 AYYM 449 WINPK 558 GGSYD 667 RASQSI 776 GASRL 885 QQGY 38 H SGGTK AFDI SSYLN QS SSPFT YAQKF QGAntibody 341 AYYLH 450 WINPN 559 GGSFD 668 RASQSI 777 GAS SV 886 QQGD 39 SGGTN AFDI SRYLN QS SSPFT YAQKF QGAntibody 342 AYYLH 451 WINPK 560 GGSFD 669 RASQSI 778 GAS SV 887 QQGD40 SGGTN AFDI SRYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 343 GYFIH 452 WINPK 561 GGSYD 670 RASQSI 779 GASRL 888 QQGH 41 SGGTN AFDI SSYLN QS STPFT YAQKF QDAntibody 344 AYYM 453 WINPN 562 GGSYD 671 RASQSI 780 GASRL 889 QQGD 42 H SGGTK AFDI SSYLN QS STPFT YAQKF QGAntibody 345 AYYM 454 WINPK 563 GGSYD 672 RASQSI 781 GASRL 890 QQGD 43 H SGGTK AFDI SSYLN QS STPFT YAQKF QGAntibody 346 AYYIH 455 WINPN 564 GGSFD 673 RASQSI 782 GASRL 891 QQGY 44 SGGTS AFDI SSYLN QS SSPFT SAQKF QGAntibody 347 AYYIH 456 WINPK 565 GGSFD 674 RASQSI 783 GASRL 892 QQGY 45 SGGTS AFDI SSYLN QS SSPFT SAQKF QGAntibody 348 AYYIH 457 WVNPN 566 GGSFD 675 RASQSI 784 GASSL 893 QQGH 46 SGGTN AFDI SSYLN QS STPFT YAQSF QGAntibody 349 AYYIH 458 WVNPK 567 GGSFD 676 RASQSI 785 GASSL 894 QQGH 47 SGGTN AFDI SSYLN QS STPFT YAQSF QGAntibody 350 AYYM 459 WINPN 568 GGSFD 677 RASQSI 786 GASSL 895 QQGD 48 H SGGTK AFDI SSYLN QS STPFT YAQKF QGAntibody 351 AYYM 460 WINPK 569 GGSFD 678 RASQSI 787 GASSL 896 QQGD49 H SGGTK AFDI SSYLN QS STPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 352 GYYIH 461 WINPK 570 GGSYD 679 RASQSI 788 GASSL 897 QQGD 50 SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 353 GYYM 462 WINPN 571 GGSYD 680 RASQSI 789 GASSL 898 QQGD 51 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 354 GYYM 463 WINPK 572 GGSYD 681 RASQSI 790 GASSL 899 QQGD 52 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 355 GYYM 464 WIHPN 573 GGSYD 682 RASQSI 791 GASRL 900 QQGY 53 H SGGTN AFDI SSYLN QS SSPFT SAQKF QGAntibody 356 GYYM 465 WIHPK 574 GGSYD 683 RASQSI 792 GASRL 901 QQGY 54 H SGGTN AFDI SSYLN QS SSPFT TAQKF QGAntibody 357 GYFIH 466 WINPK 575 GGSFD 684 RASQSI 793 GAS SV 902 QQGD 55 SGGTN AFDI SRYLN QS SSPFT YAQKF QGAntibody 358 GYYM 467 WINPN 576 GGSFD 685 RASQSI 794 GASRL 903 QQGY 56 H SGGTN AFDI SSYLN QS SSPFT YAQKF QGAntibody 359 GYYM 468 WINPK 577 GGSFD 686 RASQSI 795 GASRL 904 QQGY 57 H SGGTN AFDI SSYLN QS SSPFT YAQKF QGAntibody 360 GYYM 469 WINPN 578 GGSFD 687 RASQSI 796 GTSRL 905 QQGY58 H SGGPN AFDI SNYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QDAntibody 361 GYYM 470 WINPK 579 GGSFD 688 RASQSI 797 GTSRL 906 QQGY 59 H SGGPN AFDI SNYLN QS SSPFT YAQKF QDAntibody 362 GYFMH 471 WINPN 580 GGSFD 689 RASQSI 798 GASRL 907 QQGY 60 SGGTN AFDI SSYLN QS SSPFT YAQRF QGAntibody 363 GYFMH 472 WINPK 581 GGSFD 690 RASQSI 799 GASRL 908 QQGY 61 SGGTN AFDI SSYLN QS SSPFT YAQRF QGAntibody 364 GYYM 473 WINPN 582 GGSFD 691 RASQSI 800 GASRL 909 QQGD 62 H SGGTN AFDV SSYLN QS NTPFT YAQKF QGAntibody 365 GYYM 474 WINPK 583 GGSFD 692 RASQSI 801 GASRL 910 QQGD 63 H SGGTN AFDV SSYLN QS NTPFT YAQKF QGAntibody 366 GYYM 475 WINPN 584 GGSFD 693 RASQSI 802 GASRL 911 QQGH 64 Q SGGTIY AFDI SSYLN QS STPFT AQKFQ GAntibody 367 GYYM 476 WINPK 585 GGSFD 694 RASQSI 803 GASRL 912 QQGH 65 Q SGGTIY AFDI SSYLN QS STPFT AQKFQ GAntibody 368 GYYLH 477 WIKPN 586 GGSYD 695 RASQSI 804 GASRL 913 QQGY 66 SGGTN AFDI SSYLN QS SSPFT YAQKF QGAntibody 369 GYYLH 478 WIKPK 587 GGSYD 696 RASQSI 805 GASRL 914 QQGY67 SGGTN AFDI SSYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 370 AYYM 479 WVNPN 588 GGSFD 697 RASQSI 806 GASSL 915 QQGH 68 H SGGTN AFDI SSYLN QS STPFT YAQNF QGAntibody 371 AYYM 480 WVNPK 589 GGSFD 698 RASQSI 807 GASSL 916 QQGH 69 H SGGTN AFDI SSYLN QS STPFT YAQNF QGAntibody 372 GYYM 481 WINPN 590 GGSFD 699 RASQTI 808 GASSL 917 QQGD 70 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 373 GYYM 482 WINPK 591 GGSFD 700 RASQTI 809 GASSL 918 QQGD 71 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 374 GYYM 483 WINPN 592 GGSFD 701 RASQSI 810 GASSL 919 QQGH 72 H SGGTN AFDI SKYLI QS STPFT YAQRF QGAntibody 375 GYYM 484 WINPK 593 GGSFD 702 RASQSI 811 GASSL 920 QQGH 73 H SGGTN AFDI SKYLI QS STPFT YAQRF QGAntibody 376 GYYM 485 WIKPN 594 GGSYD 703 RASQSI 812 GASRL 921 QQGD 74 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 377 GYYM 486 WIKPK 595 GGSYD 704 RASQSI 813 GASRL 922 QQGD 75 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 378 GYYIH 487 WINPN 596 GGSFD 705 RASQSI 814 GASRL 923 QQGY76 SGGTN AFDI SSYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 379 GYYIH 488 WINPK 597 GGSFD 706 RASQSI 815 GASRL 924 QQGY 77 SGGTN AFDI SSYLN QS SSPFT YAQKF QGAntibody 380 AYYM 489 WINPN 598 GGSYD 707 RASLSI 816 GASSL 925 QQGH 78 H SGGTK AFDI SSYLN QS STPFT YAQKF QGAntibody 381 AYYM 490 WINPK 599 GGSYD 708 RASLSI 817 GASSL 926 QQGH 79 H SGGTK AFDI SSYLN QS STPFT YAQKF QGAntibody 382 GYYM 491 WINPN 600 GGSFD 709 RASQSI 818 GASSL 927 QQGD 80 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 383 GYYM 492 WINPN 601 GGSYD 710 RSSQSI 819 GASSL 928 QQGD 81 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 384 GYYM 493 WINPK 602 GGSYD 711 RSSQSI 820 GASSL 929 QQGD 82 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 385 GYYM 494 WINPN 603 GGSFD 712 RASRSI 821 GASRL 930 QQGY 83 H SGATN AFDI SSYLN QT SSPFT FAQKF QGAntibody 386 GYYM 495 WINPK 604 GGSFD 713 RASRSI 822 GASRL 931 QQGY 84 H SGATN AFDI SSYLN QT SSPFT FAQKF QGAntibody 387 AYYLH 496 WINPN 605 GGSYD 714 RASQSI 823 GASSL 932 QQGY85 SGGTN AFDI NSYLN QS STPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QDAntibody 388 AYYLH 497 WINPK 606 GGSYD 715 RASQSI 824 GASSL 933 QQGY 86 SGGTN AFDI QSYLN QS STPFT YAQKF QDAntibody 389 AYYM 498 WINPN 607 GGSYD 716 RASQSI 825 GASRL 934 QQGD 87 H SGGTK AFDI SSYLN QS NTPFT YAQKF QGAntibody 390 AYYM 499 WINPK 608 GGSYD 717 RASQSI 826 GASRL 935 QQGD 88 H SGGTK AFDI SSYLN QS NTPFT YAQKF QGAntibody 391 GYYM 500 WINPK 609 GGSYD 718 RASQSI 827 GASSL 936 QQGY 89 H SGGTN AFDI NSYLY QS STPFT YAQKF QGAntibody 392 GYYM 501 WINPK 610 GGSYD 719 RASQSI 828 GASSL 937 QQGY 90 H SGGTN AFDI QSYLY QS STPFT YAQKF QGAntibody 393 AYYLH 502 WINPN 611 GGSFD 720 RASQSI 829 GASSL 938 QQGD 91 SGGTS AFDI SSYLN QS STPFT SAQKF QGAntibody 394 AYYLH 503 WINPK 612 GGSFD 721 RASQSI 830 GASSL 939 QQGD 92 SGGTS AFDI SSYLN QS STPFT SAQKF QGAntibody 395 GYYM 504 WINPN 613 GGSFD 722 RASLSI 831 GASSL 940 QQGH 93 H SGGTH AFDI SSYLN QS STPFT YAQKF QGAntibody 396 GYYM 505 WINPK 614 GGSFD 723 RASLSI 832 GASSL 941 QQGH94 H SGGTH AFDI SSYLN QS STPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 397 GYYIH 506 WINPN 615 GGSFD 724 RASQSI 833 GASRL 942 QQGY 95 SGGTN AFDI SSYLN QS SSPFT YAQRF QGAntibody 398 GYYM 507 WINPK 616 GGSFD 725 RASQTI 834 GASSL 943 QQSYS 96 H SGGTIY AFDI SRYLN QS TPFT AQKFQ GAntibody 399 AYYIH 508 WINPN 617 GGSYD 726 RASQTI 835 GASSL 944 QQGY 97 SGGTN AFDI SRYLN QS STPFT YAQKF QGAntibody 400 GYFMH 509 WINPK 618 GGSFD 727 RASQSI 836 GASRL 945 QQGD 98 SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 401 GYYM 510 WINPN 619 GGSFD 728 RASQSI 837 GASRL 946 QQGY 99 H SGGTK AFDI SSYLN QS SSPFT YAQKF QGAntibody 402 GYYM 511 WINPN 620 GGSFD 729 RASQSI 838 GAS SV 947 QQGD 100 H SGGTN AFDI SRYLN QS SSPFT YAQKF QGAntibody 403 GYYM 512 WINPN 621 GGSYD 730 RASQSI 839 GASSL 948 QQGY 101 H SGGTN AFDI SRYLN QS STLFT YAQKF QGAntibody 404 GYYM 513 WINPN 622 GGSFD 731 RASQSI 840 GASRL 949 QQGY 102 H SGGTK AFDI SSYLN QS SSPFT YSQKF QGAntibody 405 GYYM 514 WINPN 623 GGSYD 732 RASQSI 841 GASRL 950 QQGY103 H SGGTN AFDI SSYLN QS SNPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 406 AYYM 515 WINPN 624 GGSID 733 RASQSI 842 GASRL 951 QQGFS 104 H SGGTN AFDI SSYLN QS TPFT YAQKF QGAntibody 407 AYYIH 516 WINPN 625 GGSYD 734 RASQSI 843 GASRL 952 QQGY 105 SGGTN AFDI SSYLN QS SSPFT YAQKF QDAntibody 408 GYYIH 517 WINPN 626 GGSFD 735 RASQSI 844 GASRL 953 QQGY 106 SGGTK AFDI SRYLN QS SSPFT YAQKF HGAntibody 409 GYYM 518 WINPN 627 GGSFD 736 RASQSI 845 GASSL 954 QQGD 107 H SGGTN AFDV SSYLN QS STPFT YAQKF QGAntibody 410 GYYM 519 WINPN 628 GGSFD 737 RASQSI 846 GASRL 955 QQGD 108 H SGGTN AFDI SSFLN QS STPFT YAQKF QGAntibody 411 AYYIH 520 WINPN 629 GGSFD 738 RASQSI 847 GASSL 956 QQGH 109 SGGTN AFDI SSYLN QS STPFT YAQRF QGAntibody 412 GYYM 521 WINPK 630 GGSFD 739 RASQSI 848 GASSL 957 QQGH 110 H SGGTN AFDI SSYLN QS STPFT YAQKF QGAntibody 413 AYYIH 522 WINPN 631 GGSFD 740 RASQSI 849 GASRL 958 QQGH 111 SGGTS AFDI SSYLN QS STPIT SAQKF QGAntibody 414 GYYM 523 WINPN 632 GGSYD 741 RASQSI 850 GASRL 959 QQGY112 H SGGTN AFDI SSYLN QS SSPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YAQKF QGAntibody 415 GYYM 524 WINPN 633 GGSYD 742 RASQSI 851 AASSL 960 QQGY 113 H SGGTK AFDI SRYLY QS DTPFT YAQKF QGAntibody 416 GYYM 525 WINPK 634 GGSFD 743 QASQD 852 AASSL 961 QQGD 114 H SGGTN AFDI ISNYLN QT STPFT YAQKF QGAntibody 417 RYGM 526 WINTN 635 DNWN 744 RASQS 853 GAS SR 962 QQYG 115 N TGNPT YVSDY VSDSY AT TSPIT YAQDF LA TGAntibody 418 GYYM 527 WINPK 636 GGSFD 745 RASQSI 854 GASSL 963 QQAK 116 H SGGTIY AFDI SSYLN QS SFPLT AQKFQ GAntibody 419 VYYM 528 WINPN 637 GGSFD 746 RASQSI 855 GASRL 964 QQGY 117 H SGGTN AFDI SSYLN QS SSPFT YAQKF QGAntibody 420 RYGM 529 WINTN 638 DNWN 747 KSSQS 856 KISNRF 965 MQVT 118 N TGNPT YDFDY LVHSD S QFPIT YAQGF GNTYL TG SAntibody 421 TYGMN 530 WINTN 639 DNWN 748 RSSQSL 857 KISNRF 966 MQAT 119 TGNPT YDLDY VHSDG S QFPIT YAQGF NTYLSTG

[0118] TABLE 1.2 C. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 11-119Chot lia NumberingName CDRH1 CDRH1 CDRH2 CDRH2 CDRH3 CDRH3 CDRL1 CDRL1 CDRL2 CDRL2 CDRL3 CDRL3SEQ ID SEQ ID SEQ ID SEQ ID SEQ ID SEQ IDNO NO NO NO NO NOACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 967 GYTFT 1076 NPKSG 1185 GSFDA 1294 SQSISR GAS 1512 GFSAP 11 GY G FD L Antibody 968 GGSFS 1077 THSGI 1186 QVGTT 1295 SQSIRR AAS 1513 SYRTI 12 GY DYYYF YYMDAntibody 969 GYTFT 1078 NPNSG 1187 GSFDA 1296 SQSISR GAS 1514 GDSSPF 13 GY G FDAntibody 970 GYTFT 1079 NPKSG 1188 GSFDA 1297 SQSISR GAS 1515 GDSSPF 14 GY G FD YAntibody 971 GYTFT 1080 NPNSG 1189 GSFDA 1298 SQSISS GAS 1516 GHSTP 15 GY G FD F Antibody 972 GYTFT 1081 NPNSG 1190 GSFDA 1299 SQSISR GAS 1517 GDSSPF 16 AY G FDAntibody 973 GYTFT 1082 NPKSG 1191 GSFDA 1300 SQSISR GAS 1518 GDSSPF 17 AY G FD YAntibody 974 GYTFT 1083 NPNSG 1192 GSYDA 1301 SQSISS GAS 1519 GHSTP 18 AY G FD F Antibody 975 GYTFT 1084 NPKSG 1193 GSYDA 1302 SQSISS GAS 1520 GHSTP 19 AY G FD F Antibody 976 GYTFT 1085 NPNSG 1194 GSFDA 1303 SQSISS GAS 1521 GDSTP 20 AY G FD F Antibody 977 GYTFT 1086 NPKSG 1195 GSFDA 1304 SQSISS GAS 1522 GDSTP 21 AY G FD Y F Antibody 978 GYTFT 1087 NPNSG 1196 GSYDA 1305 SQSISS GAS 1523 GDSTP 22 GY G FD F Antibody 979 GYTFT 1088 NPKSG 1197 GSYDA 1306 SQSISS GAS 1524 GDSTP 23 GY G FD F Antibody 980 GYTFT 1089 NPNSG 1198 GSYDA 1307 SQSISS GAS 1525 GDSTP 24 GY G FD F Antibody 981 GYTFT 1090 NPKSG 1199 GSYDA 1308 SQSISS GAS 1526 GDSTP 25 GY G FD F Antibody 982 GYTFT 1091 NPNSG 1200 GSFDA 1309 SQSISS GAS 1527 GDSSPF 26 GY G FD YAntibody 983 GYTFT 1092 NPKSG 1201 GSFDA 1310 SQSISS GAS 1528 GDSSPF27 GY G FDACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 984 GYTFT 1093 NPKSG 1202 GSFDA 1311 SQSISS GAS 1529 GHSTP 28 GY G FD F Antibody 985 GYTFT 1094 NPKSG 1203 GSFDA 1312 SQSISS GAS 1530 GDSTP 29 GY G FD Y F Antibody 986 GYTFT 1095 NPKSG 1204 GSYDA 1313 SQSISS GAS 1531 GHSTP 30 GY G FD F Antibody 987 GYTFT 1096 NPKSG 1205 GSYDA 1314 SQSISS GAS 1532 GYSSPF 31 GY G FD YAntibody 988 GYTFT 1097 NPNSG 1206 GSFDA 1315 SQDISN GAS 1533 GDSTP 32 AY G FD Y F Antibody 989 GYTFT 1098 NPKSG 1207 GSFDA 1316 SQDISN GAS 1534 GDSTP 33 AY G FD F Antibody 990 GYTFT 1099 NPKSG 1208 GSFDA 1317 SQGISR GAS 1535 GFSTPF 34 GY G FDAntibody 991 GYTFT 1100 NPNSG 1209 GSYDA 1318 SQSISS GAS 1536 GSSPPF 35 GY G FDAntibody 992 GYTFT 1101 NPKSG 1210 GSYDA 1319 SQSISS GAS 1537 GSSPPF 36 GY G FD YAntibody 993 GYTFT 1102 NPNSG 1211 GSYDA 1320 SQSISS GAS 1538 GYSSPF 37 AY G FDAntibody 994 GYTFT 1103 NPKSG 1212 GSYDA 1321 SQSISS GAS 1539 GYSSPF 38 AY G FDAntibody 995 GYTFT 1104 NPNSG 1213 GSFDA 1322 SQSISR GAS 1540 GDSSPF 39 AY G FDAntibody 996 GYTFT 1105 NPKSG 1214 GSFDA 1323 SQSISR GAS 1541 GDSSPF 40 AY G FDAntibody 997 GYTFT 1106 NPKSG 1215 GSYDA 1324 SQSISS GAS 1542 GHSTP 41 GY G FD Y F Antibody 998 GYTFT 1107 NPNSG 1216 GSYDA 1325 SQSISS GAS 1543 GDSTP 42 AY G FD F Antibody 999 GYTFT 1108 NPKSG 1217 GSYDA 1326 SQSISS GAS 1544 GDSTP 43 AY G FD Y F Antibody 1000 GYTFT 1109 NPNSG 1218 GSFDA 1327 SQSISS GAS 1545 GYSSPF 44 AY G FDAntibody 1001 GYTFT 1110 NPKSG 1219 GSFDA 1328 SQSISS GAS 1546 GYSSPF ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 45 AY G FD YAntibody 1002 GYTFT 1111 NPNSG 1220 GSFDA 1329 SQSISS GAS 1547 GHSTP 46 AY G FD F Antibody 1003 GYTFT 1112 NPKSG 1221 GSFDA 1330 SQSISS GAS 1548 GHSTP 47 AY G FD Y F Antibody 1004 GYTFT 1113 NPNSG 1222 GSFDA 1331 SQSISS GAS 1549 GDSTP 48 AY G FD F Antibody 1005 GYTFT 1114 NPKSG 1223 GSFDA 1332 SQSISS GAS 1550 GDSTP 49 AY G FD F Antibody 1006 GYTFT 1115 NPKSG 1224 GSYDA 1333 SQSISS GAS 1551 GDSTP 50 GY G FD F Antibody 1007 GYTFT 1116 NPNSG 1225 GSYDA 1334 SQSISS GAS 1552 GDSTP 51 GY G FD Y F Antibody 1008 GYTFT 1117 NPKSG 1226 GSYDA 1335 SQSISS GAS 1553 GDSTP 52 GY G FD F Antibody 1009 GYTFT 1118 HPNSG 1227 GSYDA 1336 SQSISS GAS 1554 GYSSPF 53 GY G FDAntibody 1010 GYTFT 1119 HPKSG 1228 GSYDA 1337 SQSISS GAS 1555 GYSSPF 54 GY G FDAntibody 1011 GYTFT 1120 NPKSG 1229 GSFDA 1338 SQSISR GAS 1556 GDSSPF 55 GY G FDAntibody 1012 GYTFT 1121 NPNSG 1230 GSFDA 1339 SQSISS GAS 1557 GYSSPF 56 GY G FD YAntibody 1013 GYTFT 1122 NPKSG 1231 GSFDA 1340 SQSISS GAS 1558 GYSSPF 57 GY G FDAntibody 1014 GYTFT 1123 NPNSG 1232 GSFDA 1341 SQSISN GTS 1559 GYSSPF 58 GY G FD YAntibody 1015 GYTFT 1124 NPKSG 1233 GSFDA 1342 SQSISN GTS 1560 GYSSPF 59 GY G FDAntibody 1016 GYTFT 1125 NPNSG 1234 GSFDA 1343 SQSISS GAS 1561 GYSSPF 60 GY G FDAntibody 1017 GYTFT 1126 NPKSG 1235 GSFDA 1344 SQSISS GAS 1562 GYSSPF 61 GY G FDAntibody 1018 GYTFT 1127 NPNSG 1236 GSFDA 1345 SQSISS GAS 1563 GDNTP62 GY G FD F ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 1019 GYTFT 1128 NPKSG 1237 GSFDA 1346 SQSISS GAS 1564 GDNTP 63 GY G FD F Antibody 1020 GYTFT 1129 NPNSG 1238 GSFDA 1347 SQSISS GAS 1565 GHSTP 64 GY G FD Y F Antibody 1021 GYTFT 1130 NPKSG 1239 GSFDA 1348 SQSISS GAS 1566 GHSTP 65 GY G FD F Antibody 1022 GYTFT 1131 KPNSG 1240 GSYDA 1349 SQSISS GAS 1567 GYSSPF 66 GY G FD YAntibody 1023 GYTFT 1132 KPKSG 1241 GSYDA 1350 SQSISS GAS 1568 GYSSPF 67 GY G FD YAntibody 1024 GYTFT 1133 NPNSG 1242 GSFDA 1351 SQSISS GAS 1569 GHSTP 68 AY G FD F Antibody 1025 GYTFT 1134 NPKSG 1243 GSFDA 1352 SQSISS GAS 1570 GHSTP 69 AY G FD F Antibody 1026 GYTFT 1135 NPNSG 1244 GSFDA 1353 SQTISS GAS 1571 GDSTP 70 GY G FD F Antibody 1027 GYTFT 1136 NPKSG 1245 GSFDA 1354 SQTISS GAS 1572 GDSTP 71 GY G FD Y F Antibody 1028 GYTFT 1137 NPNSG 1246 GSFDA 1355 SQSISK GAS 1573 GHSTP 72 GY G FD F Antibody 1029 GYTFT 1138 NPKSG 1247 GSFDA 1356 SQSISK GAS 1574 GHSTP 73 GY G FD F Antibody 1030 GYTFT 1139 KPNSG 1248 GSYDA 1357 SQSISS GAS 1575 GDSTP 74 GY G FD F Antibody 1031 GYTFT 1140 KPKSG 1249 GSYDA 1358 SQSISS GAS 1576 GDSTP 75 GY G FD F Antibody 1032 GYTFT 1141 NPNSG 1250 GSFDA 1359 SQSISS GAS 1577 GYSSPF 76 GY G FD YAntibody 1033 GYTFT 1142 NPKSG 1251 GSFDA 1360 SQSISS GAS 1578 GYSSPF 77 GY G FDAntibody 1034 GYTFT 1143 NPNSG 1252 GSYDA 1361 SLSISS GAS 1579 GHSTP 78 AY G FD Y F Antibody 1035 GYTFT 1144 NPKSG 1253 GSYDA 1362 SLSISS GAS 1580 GHSTP 79 AY G FD FAntibody 1036 GYTFT 1145 NPNSG 1254 GSFDA 1363 SQSISS GAS 1581 GDSTP ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 80 GY G FD Y F Antibody 1037 GYTFT 1146 NPNSG 1255 GSYDA 1364 SQSISS GAS 1582 GDSTP 81 GY G FD F Antibody 1038 GYTFT 1147 NPKSG 1256 GSYDA 1365 SQSISS GAS 1583 GDSTP 82 GY G FD Y F Antibody 1039 GYTFT 1148 NPNSG 1257 GSFDA 1366 SRSISS GAS 1584 GYSSPF 83 GY A FDAntibody 1040 GYTFT 1149 NPKSG 1258 GSFDA 1367 SRS1SS GAS 1585 GYSSPF 84 GY A FDAntibody 1041 GYTFT 1150 NPNSG 1259 GSYDA 1368 SQSINS GAS 1586 GYSTP 85 AY G FD F Antibody 1042 GYTFT 1151 NPKSG 1260 GSYDA 1369 SQSIQS GAS 1587 GYSTP 86 AY G FD Y F Antibody 1043 GYTFT 1152 NPNSG 1261 GSYDA 1370 SQSISS GAS 1588 GDNTP 87 AY G FD F Antibody 1044 GYTFT 1153 NPKSG 1262 GSYDA 1371 SQSISS GAS 1589 GDNTP 88 AY G FD F Antibody 1045 GYTFT 1154 NPKSG 1263 GSYDA 1372 SQSINS GAS 1590 GYSTP 89 GY G FD F Antibody 1046 GYTFT 1155 NPKSG 1264 GSYDA 1373 SQSIQS GAS 1591 GYSTP 90 GY G FD F Antibody 1047 GYTFT 1156 NPNSG 1265 GSFDA 1374 SQSISS GAS 1592 GDSTP 91 AY G FD Y F Antibody 1048 GYTFT 1157 NPKSG 1266 GSFDA 1375 SQSISS GAS 1593 GDSTP 92 AY G FD F Antibody 1049 GYTFT 1158 NPNSG 1267 GSFDA 1376 SLSISS GAS 1594 GHSTP 93 GY G FD Y F Antibody 1050 GYTFT 1159 NPKSG 1268 GSFDA 1377 SLSISS GAS 1595 GHSTP 94 GY G FD F Antibody 1051 GYTFT 1160 NPNSG 1269 GSFDA 1378 SQSISS GAS 1596 GYSSPF 95 GY G FDAntibody 1052 GYTFT 1161 NPKSG 1270 GSFDA 1379 SQTISR GAS 1597 SYSTPF 96 GY G FDAntibody 1053 GYTFT 1162 NPNSG 1271 GSYDA 1380 SQTISR GAS 1598 GYSTP97 AY G FD F ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 1054 GYTFT 1163 NPKSG 1272 GSFDA 1381 SQSISS GAS 1599 GDSTP 98 GY G FD F Antibody 1055 GYTFT 1164 NPNSG 1273 GSFDA 1382 SQSISS GAS 1600 GYSSPF 99 GY G FD YAntibody 1056 GYTFT 1165 NPNSG 1274 GSFDA 1383 SQSISR GAS 1601 GDSSPF 100 GY G FDAntibody 1057 GYTFT 1166 NPNSG 1275 GSYDA 1384 SQSISR GAS 1602 GYSTL 101 GY G FD Y F Antibody 1058 GYTFN 1167 NPNSG 1276 GSFDA 1385 SQSISS GAS 1603 GYSSPF 102 GY G FD YAntibody 1059 GYTFT 1168 NPNSG 1277 GSYDA 1386 SQSISS GAS 1604 GYSNP 103 GY G FD F Antibody 1060 GYTFT 1169 NPNSG 1278 GSIDAF 1387 SQSISS GAS 1605 GFSTPF 104 AY G DAntibody 1061 GYTFT 1170 NPNSG 1279 GSYDA 1388 SQSISS GAS 1606 GYSSPF 105 AY G FDAntibody 1062 GYTFT 1171 NPNSG 1280 GSFDA 1389 SQSISR GAS 1607 GYSSPF 106 GY G FD YAntibody 1063 GYTFT 1172 NPNSG 1281 GSFDA 1390 SQSISS GAS 1608 GDSTP 107 GY G FD F Antibody 1064 GYTFT 1173 NPNSG 1282 GSFDA 1391 SQSISS GAS 1609 GDSTP 108 GY G FD F F Antibody 1065 GYTFT 1174 NPNSG 1283 GSFDA 1392 SQSISS GAS 1610 GHSTP 109 AY G FD F Antibody 1066 GYTFT 1175 NPKSG 1284 GSFDA 1393 SQSISS GAS 1611 GHSTP 110 GY G FD F Antibody 1067 GYTFT 1176 NPNSG 1285 GSFDA 1394 SQSISS GAS 1612 GHSTPI 111 AY G FD YAntibody 1068 GYTFT 1177 NPNSG 1286 GSYDA 1395 SQSISS GAS 1613 GYSSPF 112 GY G FDAntibody 1069 GYTFT 1178 NPNSG 1287 GSYDA 1396 SQSISR AAS 1614 GYDTP 113 GY G FD Y F Antibody 1070 GYTFT 1179 NPKSG 1288 GSFDA 1397 SQDISN AAS 1615 GDSTP 114 GY G FD FAntibody 1071 GYTFT 1180 NTNTG 1289 NWNY 1398 SQSVS GAS 1616 YGTSPI ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 115 RY N VSD DSYAntibody 1072 GYTFT 1181 NPKSG 1290 GSFDA 1399 SQSISS GAS 1617 AKSFP 116 GY G FD L Antibody 1073 GYTFT 1182 NPNSG 1291 GSFDA 1400 SQSISS GAS 1618 GYSSPF 117 VY G FD YAntibody 1074 GYTFT 1183 NTNTG 1292 NWNY 1401 SQSLV KIS 1619 VTQFPI 118 RY N DFD HSDGNTYAntibody 1075 GYTFT 1184 NTNTG 1293 NWNY 1402 SQSLV KIS 1620 ATQFPI 119 TY N DLD HSDGNTY

[0119] TABLE 1.3 C. AMINO ACID SEQUENCES OF EXEMPLARY CDRS OF ANTIBODY 11-119IMGT NumberingName CDRH1 CDRH1 CDRH2 CDRH2 CDRH3 CDRH3 CDRL1 CDRL1 CDRL2 CDRL2 CDRL3 CDRL3SEQID SEQ ID SEQID SEQ ID SEQID SEQ ID NO NO NO NO NO NOAntibody 1621 GYTFT 1730 INPKSG 1839 ATGGS 1948 QSISRY GAS 2166 QQGFS 11 GYY GT FDAFDI APLT Antibody 1622 GGSFS 1731 ITHSGI 1840 ARGQV 1949 QSIRRY AAS 2167 QQSYR 12 GYY T GTTDY TIT YYFYM DVAntibody 1623 GYTFT 1732 INPNSG 1841 AVGGS 1950 QSISRY GAS 2168 QQGDS 13 GYY GT FDAFDI SPFT Antibody 1624 GYTFT 1733 INPKSG 1842 AVGGS 1951 QSISRY GAS 2169 QQGDS 14 GYY GT FDAFDI SPFT Antibody 1625 GYTFT 1734 INPNSG 1843 AVGGS 1952 QSISSY GAS 2170 QQGHS 15 GYY GT FDAFDI TPFT Antibody 1626 GYTFT 1735 INPNSG 1844 ATGGS 1953 QSISRY GAS 2171 QQGDS 16 AYY GT FDAFDI SPFT Antibody 1627 GYTFT 1736 INPKSG 1845 ATGGS 1954 QSISRY GAS 2172 QQGDS 17 AYY GT FDAFDI SPFT Antibody 1628 GYTFT 1737 INPNSG 1846 AVGGS 1955 QSISSY GAS 2173 QQGHS18 AYY GT YDAFD TPFT ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 IAntibody 1629 GYTFT 1738 INPKSG 1847 AVGGS 1956 QSISSY GAS 2174 QQGHS 19 AYY GT YDAFD TPFT IAntibody 1630 GYTFT 1739 INPNSG 1848 AVGGS 1957 QSISSY GAS 2175 QQGDS 20 AYY GT FDAFDI TPFT Antibody 1631 GYTFT 1740 INPKSG 1849 AVGGS 1958 QSISSY GAS 2176 QQGDS 21 AYY GT FDAFDI TPFT Antibody 1632 GYTFT 1741 INPNSG 1850 AVGGS 1959 QSISSY GAS 2177 QQGDS 22 GYY GT YDAFD TPFT IAntibody 1633 GYTFT 1742 INPKSG 1851 AVGGS 1960 QSISSY GAS 2178 QQGDS 23 GYY GT YDAFD TPFT IAntibody 1634 GYTFT 1743 INPNSG 1852 AVGGS 1961 QSISSY GAS 2179 QQGDS 24 GYY GT YDAFD TPFT IAntibody 1635 GYTFT 1744 INPKSG 1853 AVGGS 1962 QSISSY GAS 2180 QQGDS 25 GYY GT YDAFD TPFT IAntibody 1636 GYTFT 1745 INPNSG 1854 ATGGS 1963 QSISSY GAS 2181 QQGDS 26 GYY GT FDAFDI SPFT Antibody 1637 GYTFT 1746 INPKSG 1855 ATGGS 1964 QSISSY GAS 2182 QQGDS 27 GYY GT FDAFDI SPFT Antibody 1638 GYTFT 1747 INPKSG 1856 ATGGS 1965 QSISSY GAS 2183 QQGHS 28 GYY GT FDAFDI TPFT Antibody 1639 GYTFT 1748 INPKSG 1857 ATGGS 1966 QSISSY GAS 2184 QQGDS 29 GYY GT FDAFDI TPFT Antibody 1640 GYTFT 1749 INPKSG 1858 AVGGS 1967 QSISSY GAS 2185 QQGHS 30 GYY GT YDAFD TPFT IAntibody 1641 GYTFT 1750 INPKSG 1859 AVGGS 1968 QSISSY GAS 2186 QQGYS 31 GYY GT YDAFD SPFTIAntibody 1642 GYTFT 1751 INPNSG 1860 AVGGS 1969 QDISN GAS 2187 QQGDS ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 32 AYY GT FDAFDI Y TPFT Antibody 1643 GYTFT 1752 INPKSG 1861 AVGGS 1970 QDISN GAS 2188 QQGDS 33 AYY GT FDAFDI TPFT Antibody 1644 GYTFT 1753 INPKSG 1862 ATGGS 1971 QGISR GAS 2189 QQGFS 34 GYY GT FDAFDI Y TPFT Antibody 1645 GYTFT 1754 INPNSG 1863 AVGGS 1972 QSISSY GAS 2190 QQGSS 35 GYY GT YDAFD PPFT IAntibody 1646 GYTFT 1755 INPKSG 1864 AVGGS 1973 QSISSY GAS 2191 QQGSS 36 GYY GT YDAFD PPFT IAntibody 1647 GYTFT 1756 INPNSG 1865 AVGGS 1974 QSISSY GAS 2192 QQGYS 37 AYY GT YDAFD SPFT IAntibody 1648 GYTFT 1757 INPKSG 1866 AVGGS 1975 QSISSY GAS 2193 QQGYS 38 AYY GT YDAFD SPFT IAntibody 1649 GYTFT 1758 INPNSG 1867 ASGGS 1976 QSISRY GAS 2194 QQGDS 39 AYY GT FDAFDI SPFT Antibody 1650 GYTFT 1759 INPKSG 1868 ASGGS 1977 QSISRY GAS 2195 QQGDS 40 AYY GT FDAFDI SPFT Antibody 1651 GYTFT 1760 INPKSG 1869 AVGGS 1978 QSISSY GAS 2196 QQGHS 41 GYF GT YDAFD TPFT IAntibody 1652 GYTFT 1761 INPNSG 1870 AVGGS 1979 QSISSY GAS 2197 QQGDS 42 AYY GT YDAFD TPFT IAntibody 1653 GYTFT 1762 INPKSG 1871 AVGGS 1980 QSISSY GAS 2198 QQGDS 43 AYY GT YDAFD TPFT IAntibody 1654 GYTFT 1763 INPNSG 1872 AVGGS 1981 QSISSY GAS 2199 QQGYS 44 AYY GT FDAFDI SPFT Antibody 1655 GYTFT 1764 INPKSG 1873 AVGGS 1982 QSISSY GAS 2200 QQGYS 45 AYY GT FDAFDI SPFTAntibody 1656 GYTFT 1765 VNPNS 1874 AVGGS 1983 QSISSY GAS 2201 QQGHS ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 46 AYY GGT FDAFDI TPFT Antibody 1657 GYTFT 1766 VNPKS 1875 AVGGS 1984 QSISSY GAS 2202 QQGHS 47 AYY GGT FDAFDI TPFT Antibody 1658 GYTFT 1767 INPNSG 1876 ATGGS 1985 QSISSY GAS 2203 QQGDS 48 AYY GT FDAFDI TPFT Antibody 1659 GYTFT 1768 INPKSG 1877 ATGGS 1986 QSISSY GAS 2204 QQGDS 49 AYY GT FDAFDI TPFT Antibody 1660 GYTFT 1769 INPKSG 1878 AVGGS 1987 QSISSY GAS 2205 QQGDS 50 GYY GT YDAFD TPFT IAntibody 1661 GYTFT 1770 INPNSG 1879 AVGGS 1988 QSISSY GAS 2206 QQGDS 51 GYY GT YDAFD TPFT IAntibody 1662 GYTFT 1771 INPKSG 1880 AVGGS 1989 QSISSY GAS 2207 QQGDS 52 GYY GT YDAFD TPFT IAntibody 1663 GYTFT 1772 IHPNSG 1881 AVGGS 1990 QSISSY GAS 2208 QQGYS 53 GYY GT YDAFD SPFT IAntibody 1664 GYTFT 1773 IHPKSG 1882 AVGGS 1991 QSISSY GAS 2209 QQGYS 54 GYY GT YDAFD SPFT IAntibody 1665 GYTFT 1774 INPKSG 1883 ASGGS 1992 QSISRY GAS 2210 QQGDS 55 GYF GT FDAFDI SPFT Antibody 1666 GYTFT 1775 INPNSG 1884 ATGGS 1993 QSISSY GAS 2211 QQGYS 56 GYY GT FDAFDI SPFT Antibody 1667 GYTFT 1776 INPKSG 1885 ATGGS 1994 QSISSY GAS 2212 QQGYS 57 GYY GT FDAFDI SPFT Antibody 1668 GYTFT 1777 INPNSG 1886 ATGGS 1995 QSISNY GTS 2213 QQGYS 58 GYY GP FDAFDI SPFT Antibody 1669 GYTFT 1778 INPKSG 1887 ATGGS 1996 QSISNY GTS 2214 QQGYS 59 GYY GP FDAFDI SPFT Antibody 1670 GYTFT 1779 INPNSG 1888 ATGGS 1997 QSISSY GAS 2215 QQGYS 60 GYF GT FDAFDI SPFTAntibody 1671 GYTFT 1780 INPKSG 1889 ATGGS 1998 QSISSY GAS 2216 QQGYS ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 61 GYF GT FDAFDI SPFT Antibody 1672 GYTFT 1781 INPNSG 1890 ATGGS 1999 QSISSY GAS 2217 QQGDN 62 GYY GT FDAFD TPFT VAntibody 1673 GYTFT 1782 INPKSG 1891 ATGGS 2000 QSISSY GAS 2218 QQGDN 63 GYY GT FDAFD TPFT VAntibody 1674 GYTFT 1783 INPNSG 1892 ATGGS 2001 QSISSY GAS 2219 QQGHS 64 GYY GT FDAFDI TPFT Antibody 1675 GYTFT 1784 INPKSG 1893 ATGGS 2002 QSISSY GAS 2220 QQGHS 65 GYY GT FDAFDI TPFT Antibody 1676 GYTFT 1785 IKPNSG 1894 AVGGS 2003 QSISSY GAS 2221 QQGYS 66 GYY GT YDAFD SPFT IAntibody 1677 GYTFT 1786 IKPKSG 1895 AVGGS 2004 QSISSY GAS 2222 QQGYS 67 GYY GT YDAFD SPFT IAntibody 1678 GYTFT 1787 VNPNS 1896 AVGGS 2005 QSISSY GAS 2223 QQGHS 68 AYY GGT FDAFDI TPFT Antibody 1679 GYTFT 1788 VNPKS 1897 AVGGS 2006 QSISSY GAS 2224 QQGHS 69 AYY GGT FDAFDI TPFT Antibody 1680 GYTFT 1789 INPNSG 1898 ATGGS 2007 QTISSY GAS 2225 QQGDS 70 GYY GT FDAFDI TPFT Antibody 1681 GYTFT 1790 INPKSG 1899 ATGGS 2008 QTISSY GAS 2226 QQGDS 71 GYY GT FDAFDI TPFT Antibody 1682 GYTFT 1791 INPNSG 1900 ATGGS 2009 QSISKY GAS 2227 QQGHS 72 GYY GT FDAFDI TPFT Antibody 1683 GYTFT 1792 INPKSG 1901 ATGGS 2010 QSISKY GAS 2228 QQGHS 73 GYY GT FDAFDI TPFT Antibody 1684 GYTFT 1793 IKPNSG 1902 AVGGS 2011 QSISSY GAS 2229 QQGDS 74 GYY GT YDAFD TPFT IAntibody 1685 GYTFT 1794 IKPKSG 1903 AVGGS 2012 QSISSY GAS 2230 QQGDS 75 GYY GT YDAFD TPFTIACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 1686 GYTFT 1795 INPNSG 1904 ATGGS 2013 QSISSY GAS 2231 QQGYS 76 GYY GT FDAFDI SPFT Antibody 1687 GYTFT 1796 INPKSG 1905 ATGGS 2014 QSISSY GAS 2232 QQGYS 77 GYY GT FDAFDI SPFT Antibody 1688 GYTFT 1797 INPNSG 1906 AVGGS 2015 LSISSY GAS 2233 QQGHS 78 AYY GT YDAFD TPFT IAntibody 1689 GYTFT 1798 INPKSG 1907 AVGGS 2016 LSISSY GAS 2234 QQGHS 79 AYY GT YDAFD TPFT IAntibody 1690 GYTFT 1799 INPNSG 1908 ATGGS 2017 QSISSY GAS 2235 QQGDS 80 GYY GT FDAFDI TPFT Antibody 1691 GYTFT 1800 INPNSG 1909 AVGGS 2018 QSISSY GAS 2236 QQGDS 81 GYY GT YDAFD TPFT IAntibody 1692 GYTFT 1801 INPKSG 1910 AVGGS 2019 QSISSY GAS 2237 QQGDS 82 GYY GT YDAFD TPFT IAntibody 1693 GYTFT 1802 INPNSG 1911 ATGGS 2020 RSIS SY GAS 2238 QQGYS 83 GYY AT FDAFDI SPFT Antibody 1694 GYTFT 1803 INPKSG 1912 ATGGS 2021 RSISSY GAS 2239 QQGYS 84 GYY AT FDAFDI SPFT Antibody 1695 GYTFT 1804 INPNSG 1913 AVGGS 2022 QSINSY GAS 2240 QQGYS 85 AYY GT YDAFD TPFT IAntibody 1696 GYTFT 1805 INPKSG 1914 AVGGS 2023 QSIQSY GAS 2241 QQGYS 86 AYY GT YDAFD TPFT IAntibody 1697 GYTFT 1806 INPNSG 1915 AVGGS 2024 QSISSY GAS 2242 QQGDN 87 AYY GT YDAFD TPFT IAntibody 1698 GYTFT 1807 INPKSG 1916 AVGGS 2025 QSISSY GAS 2243 QQGDN 88 AYY GT YDAFD TPFTIAntibody 1699 GYTFT 1808 INPKSG 1917 ATGGS 2026 QSINSY GAS 2244 QQGYS ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 89 GYY GT YDAFD TPFT IAntibody 1700 GYTFT 1809 INPKSG 1918 ATGGS 2027 QSIQSY GAS 2245 QQGYS 90 GYY GT YDAFD TPFT IAntibody 1701 GYTFT 1810 INPNSG 1919 AVGGS 2028 QSISSY GAS 2246 QQGDS 91 AYY GT FDAFDI TPFT Antibody 1702 GYTFT 1811 INPKSG 1920 AVGGS 2029 QSISSY GAS 2247 QQGDS 92 AYY GT FDAFDI TPFT Antibody 1703 GYTFT 1812 INPNSG 1921 AVGGS 2030 LSISSY GAS 2248 QQGHS 93 GYY GT FDAFDI TPFT Antibody 1704 GYTFT 1813 INPKSG 1922 AVGGS 2031 LSISSY GAS 2249 QQGHS 94 GYY GT FDAFDI TPFT Antibody 1705 GYTFT 1814 INPNSG 1923 ATGGS 2032 QSISSY GAS 2250 QQGYS 95 GYY GT FDAFDI SPFT Antibody 1706 GYTFT 1815 INPKSG 1924 ATGGS 2033 QTISRY GAS 2251 QQSYS 96 GYY GT FDAFDI TPFT Antibody 1707 GYTFT 1816 INPNSG 1925 AVGGS 2034 QTISRY GAS 2252 QQGYS 97 AYY GT YDAFD TPFT IAntibody 1708 GYTFT 1817 INPKSG 1926 ASGGS 2035 QSISSY GAS 2253 QQGDS 98 GYF GT FDAFDI TPFT Antibody 1709 GYTFT 1818 INPNSG 1927 ATGGS 2036 QSISSY GAS 2254 QQGYS 99 GYY GT FDAFDI SPFT Antibody 1710 GYTFT 1819 INPNSG 1928 ASGGS 2037 QSISRY GAS 2255 QQGDS 100 GYY GT FDAFDI SPFT Antibody 1711 GYTFT 1820 INPNSG 1929 AVGGS 2038 QSISRY GAS 2256 QQGYS 101 GYY GT YDAFD TLFT IAntibody 1712 GYTFN 1821 INPNSG 1930 ATGGS 2039 QSISSY GAS 2257 QQGYS 102 GYY GT FDAFDI SPFT Antibody 1713 GYTFT 1822 INPNSG 1931 AVGGS 2040 QSISSY GAS 2258 QQGYS 103 GYY GT YDAFD NPFTIAntibody 1714 GYTFT 1823 INPNSG 1932 ASGGSI 2041 QSISSY GAS 2259 QQGFS ACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 104 AYY GT DAFDI TPFT Antibody 1715 GYTFT 1824 INPNSG 1933 AVGGS 2042 QSISSY GAS 2260 QQGYS 105 AYY GT YDAFD SPFT IAntibody 1716 GYTFT 1825 INPNSG 1934 AVGGS 2043 QSISRY GAS 2261 QQGYS 106 GYY GT FDAFDI SPFT Antibody 1717 GYTFT 1826 INPNSG 1935 VTGGS 2044 QSISSY GAS 2262 QQGDS 107 GYY GT FDAFD TPFT VAntibody 1718 GYTFT 1827 INPNSG 1936 TSGGS 2045 QSISSF GAS 2263 QQGDS 108 GYY GT FDAFDI TPFT Antibody 1719 GYTFT 1828 INPNSG 1937 ATGGS 2046 QSISSY GAS 2264 QQGHS 109 AYY GT FDAFDI TPFT Antibody 1720 GYTFT 1829 INPKSG 1938 ASGGS 2047 QSISSY GAS 2265 QQGHS 110 GYY GT FDAFDI TPFT Antibody 1721 GYTFT 1830 INPNSG 1939 AVGGS 2048 QSISSY GAS 2266 QQGHS 111 AYY GT FDAFDI TPIT Antibody 1722 GYTFT 1831 INPNSG 1940 ATGGS 2049 QSISSY GAS 2267 QQGYS 112 GYY GT YDAFD SPFT IAntibody 1723 GYTFT 1832 INPNSG 1941 ATGGS 2050 QSISRY AAS 2268 QQGYD 113 GYY GT YDAFD TPFT IAntibody 1724 GYTFT 1833 INPKSG 1942 ATGGS 2051 QDISN AAS 2269 QQGDS 114 GYY GT FDAFDI Y TPFT Antibody 1725 GYTFT 1834 INTNT 1943 ARDN 2052 QSVSD GAS 2270 QQYGT 115 RYG GNP WNYVS SY SPIT DYAntibody 1726 GYTFT 1835 INPKSG 1944 ATGGS 2053 QSISSY GAS 2271 QQAKS 116 GYY GT FDAFDI FPLT Antibody 1727 GYTFT 1836 INPNSG 1945 ASGGS 2054 QSISSY GAS 2272 QQGYS 117 VYY GT FDAFDI SPFT Antibody 1728 GYTFT 1837 INTNT 1946 ARDN 2055 QSLVH K1S 2273 MQVTQ 118 RYG GNP WNYDF SDGNT FPITDY YACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 1729 GYTFT 1838 INTNT 1947 ARDN 2056 QSLVH KIS 2274 MQATQ 119 TYG GNP WNYD SDGNT FPITLDYACTIVE 717944506v1Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0120] TABLE 2.1. SEQUENCES OF HEAVY CHAIN VARIABLE REGIONS (VH) AND LIGHT CHAIN VARIABLE REGIONS (VL) OF TL1A BINDING PROTEINS (ANTIBODY 5-10) Name SEQ VH SEQ VLID NO ID NOAntibody 185 EVQLVESGGGLVKPG 195 ENVLTQSPGTLSLSPGERATLS 5 GSLRLSCAAFGFTFSN CRASQIFSSSYLVWYQKKPGQ VWMNWVRQAPGKGL APRLLIYGASSRATGIPDRFSG EWVGLIKSKTDAGTTD SGSGTDFTLTISRLEPEDFAVY YAAPVKGRFTISRDDS YCQQYGNSPYTFGQGTKLEIK KNMLYLQMNSLKTED TAVYYCTTDRGWGEN YWGQGTLVTVSSAntibody 186 EVQLVESGGGLVKPG 196 EIVLTQSPGTLSLSPGERATLS 6 GSLRLSCAASGFIFSNV CRASQSVSSSYLVWYQQKPG WMNWVRQAPGKGLE QAPRLLIYGASSRATGIPDRFS WVGRIKSKIDAGTTDY GSGSGTDFTFTISRLEPEDFAV VAPVKGRFTISRDDSK YYCQQYGGSPYTFGQGTKLEI NTLSLQMNSLKTEDTA K VYYCITDRGWGENYW GQGTLVTVSSAntibody 187 EVQLVESGGGLVKPG 197 EIVLTQSPGTLSLSPGERATLS 7 GSLRLSCAASGFTFSN CRASQSISRSYLVWYEQKPGQ AWMSWVRQAPGKGL APRLLIYGASSRATGIPDRFSG EWVGRIKSKIDAGTTD SGSGTDFTLTISRLEPEDFAVY YAAPVKGRFTISRDDS YCHQYGSSPYTFGQGTKLEIK RNTLYLQMNSLRTEDT ADYYCTTDLGWGENY WGQGTLVTVSSAntibody 188 EVQLVESGGGLVKPG 198 ENVLTQSPGTLSLSPGERATLS 8 GSLRLSCAASGFTFSN CRASQRVSSSYLVWYQQKPG AWMSWVRQAPGKGL QAPRLLIYGASSRATGIPDRFS EWVGRIKSKIDAGTTD GSGSGTDFTLTISRLEPEDFAV YAAPVKGRFTISRDDS YYCQQYGSSPYTFGQGTKLES KNTLYLQMNSLKTED K TAVYYCTTDLGWGEN YWGQGTLVTVSSAntibody 189 EVQLVESGGGLVKPG 199 ENVLTQSPGTLSLSPGERATLS 9 GSLRLSCAASGFTFSN CRASQRVSSSYLVWYQQKPG AWMTWVRQAPGKGL QAPRLLIYGASSRATGIPDRFS EWVGRIKSKIDAGTTD GSGSGTDFTLTISRLEPEDFAV YAAPVKGRFTISRYDS YYCQQYGSSPYTFGQGTKLEI KNTLYLQMNSLKTED K TAVYYCTTDLGWGEN YWGQGTLVTVSSAntibodv 190 EVQLVESGGGLVKPG 200 ENVLTQSPGTLSLSPGERATLS 10 GSLRLSCAASGFTFSN CRASQRVSSSYLVWYQQKPG AWMTWVRQAPGKGL QAPRLLIYGASSRATGIPDRFS EWVGRIKSKIDAGTTD GSGSGTDFTLTISRLEPEDFAV YAAPVKGRFTISRDDS YYCQQYGSSPYTFGQGTKLEIKNTLYLQMNSLKTED KACTIVE 717944506v1 66Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 TAVYYCTTDLGWGEN YWGQGTLVTVSS

[0121] TABLE 2.2. SEQUENCES OF HEAVY CHAIN VARIABLE REGIONS (VH) AND LIGHT CHAIN VARIABLE REGIONS (VL) OF TL1A BINDING PROTEINS (ANTIBODY 1-4, 11-119)Name SEQ VH SEQ VLID NO ID NOAntibody 181 QVKLVESGGGVVQPG 191 DIVMTQSPLSLPVTPGEPASISC 1 RSLRLSCAASGFTFSSY RSSQSLLYSNGYNSLDWYLQK AMHWVRQAPGKGLE TGQSPQLLIYLGSNRASGVPD WVAVVSYEGSQNYYA RFSGSGSGTDFTLKISRVEAED DSVKGRFTISRDNSKN VGVYYCMQALQTPYTFGQGT TLYLQMNSLRAEDTA KLEIK VYYCANLESAYYFDY WGQGTLVTVSSAntibody 182 QVQLQESGPGLVKPSE 192 DIQMTQSPSSLSASVGDRVTIT 2 TLSLTCTVSGGSISSYY CRASQTIS SYFNWYQQKAGEA WSWIRQPPGKGLEWIG PKLLIYAASSLQSGVPSRFSGS LIYYSGSTNYNPSLKSR GSGTDFTLTISSLQPEDFATYY VTISVDTSKNQFSLKLS CQQSYSTPITFGQGTRLEIK SVTAADTAVYYCARA DVVTIDYWGQGTLVT VSSAntibody 183 EVQLVESGGGLVKPG 193 DIQMTQSPSSLSASVGDRVTIT 3 GSLRLSCAASGFTFST CRASQSISTYLNWYQQKPGKA YNMNWVRQAPGKGL PKLLIYAASSLQSGVPSRFSGS EWISSIHSSSNYLYYAD GSGTDFTLTISSLQPEDFAAYY SVKGRFTISRDNAKNS CQQSYSTPLTFGGGTRVEIK LYLQMNSLRAEDTAV YYCATDRAMVDFDY WGQGTLVTVSSAntibody 184 QVQLQQSGPGLVKPSQ 194 DIQMTQSPSSLSASVGDRVTIT 4 TLSLTCAISGDSVSSNS CRASQSFSSYLNWYQQTPGKA ATWNWIRQSPSRGLE PKLLIYAASSLQSGVPSRFSGS WLGRTYYRSKWYND GSGTYFTLTISSLQPEDLATYY YAVSVKSRLTINPDTS CQQSYFTPRTFGQGTKVEIK KNQFSLQLNSVTPEDT AVYYCAREAVGPTKD FDYWGQGTLVPVSSAntibody 2275 EVQLVQSGAEVKKPG 2384 DIQMTQSPSSLSASVGDRVTIT 11 ASVKVSCKASGYTFTG CRASQSISRYLYWYQQKPGKA YYMHWVRQAPGQGL PKLLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTIY GSGTDFTLTVSSMQPEDFATY AQKFQGRVTMTRDTSI YCQQGFSAPLTFGGGTKVDIK STAYMELSRLRSDDTAVYSCATGGSFDAFDIWACTIVE 717944506v1 67Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 GQGTMVTVSSAntibody 2276 QVQLQQWGAGLLKPS 2385 DIQMTQSPSSLSASVGDRVTIT 12 ETLSLTCAVYGGSFSG CRASQSIRRYLNWYQQKPGK YYWSWIRQPPGKGLE APKLLIYAASSLQSGVPSRFSG WIGEITHSGITNYNPSL SGSGTDFTLTISSLQPEDFASYF ESRVTMSVDTSKNQFS CQQSYRTITFGQGTKLEIK LKLS S VTAADTAVYY CARGQVGTTDYYYFY MDVWGKGTLVTVSSAntibody 2277 QVQLVQSGAEVKKPG 2386 DIQLTQSPSSLSASVGDRVTIT 13 ASVKVSCKASGYTFTG CRASQSISRYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSVQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLAISSLQPEDFATYY AQNFQGRVTMTRDTSI CQQGDSSPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2278 QVQLVQSGAEVKKPG 2387 DIQLTQSPSSLSASVGDRVTIT 14 ASVKVSCKASGYTFTG CRASQSISRYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSVQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLAISSLQPEDFATYY AQNFQGRVTMTRDTSI CQQGDSSPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2279 QVQLVQSGPEVEKPG 2388 DIVMTQSPSSLSASVGDRVTIT 15 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWMRQAPGQGL PKFLIYGASSLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKVEIK STAYMDLSGLRSDDT AVYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2280 QVQLVQSGAEVKKPG 2389 DIVMTQSPSSLSASVGDRVTIT 16 ASVKVSCKASGYTFTA CRASQSISRYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSVQSGVPSRFSGS EWIGWINPNSGGTNYA GSGTDFTLAISSLQPEDFATYY QSFQGRVTMTRDTSIT CQQGDSSPFTFGPGTKVEIK TAYMDLSRLRSDDTAI YYCATGGSFDAFDIW GQGTMVTVSSAntibodv 2281 QVQLVQSGAEVKKPG 2390 DIVMTQSPSSLSASVGDRVTIT 17 ASVKVSCKASGYTFTA CRASQSISRYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSVQSGVPSRFSGS EWIGWINPKSGGTNYA GSGTDFTLAISSLQPEDFATYY QSFQGRVTMTRDTSIT CQQGDSSPFTFGPGTKVEIK TAYMDLSRLRSDDTAI YYCATGGSFDAFDIWGQGTMVTVSSACTIVE 717944506v1 68Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 2282 QVQLVQSGAEVKEPG 2391 DIQMTQSPSSLSASVGDRVTIT 18 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLSISSLQPEDFATYY AQQFQGRVTMTRDTSI CQQGHSTPFTFGPGTKLEIK STAYMELSRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2283 QVQLVQSGAEVKEPG 2392 DIQMTQSPSSLSASVGDRVTIT 19 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLSISSLQPEDFATYY AQQFQGRVTMTRDTSI CQQGHSTPFTFGPGTKLEIK STAYMELSRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2284 EVQLVQSGVEVKKPG 2393 DIQMTQSPSSLSASVGDRVTIT 20 ASVKVSCQASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKILIYGASSLQSGVPSRFSGSG WMGWINPNSGGTNYA SGTDFTLAISSLQPEDFATYYC QKFQGRVTMTRDSSIS QQGDSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSFDAFDIWGQGTMVTVSSAntibodv 2285 EVQLVQSGVEVKKPG 2394 DIQMTQSPSSLSASVGDRVTIT 21 ASVKVSCQASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKILIYGASSLQSGVPSRFSGSG WMGWINPKSGGTNYA SGTDFTLAISSLQPEDFATYYC QKFQGRVTMTRDSSIS QQGDSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2286 EVQLVQSGAEVKKPG 2395 DIQMTQSPSSLSASVGDRVTIT 22 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKV YYLHWVRQAPGQGLE PKILIYGASRLQSGVPSRFSGS WMGWINPNSGGTNFA GSGTDFTLAISSLQPEDFATYY QKFQGRVTMTRDTSIN CQQGDSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody- 2287 EVQLVQSGAEVKKPG 2396 DIQMTQSPSSLSASVGDRVTIT 23 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKV YYLHWVRQAPGQGLE PKILIYGASRLQSGVPSRFSGS WMGWINPKSGGTNFA GSGTDFTLAISSLQPEDFATYY QKFQGRVTMTRDTSIN CQQGDSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody- 2288 EVQLVQSGAEVKKPG 2397 DIVMTQSPSSLSASVGDRVTIT 24 ASVKVSCKASGYTFTG CRASQSISSYLNWYQEKPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGSACTIVE 717944506v1 69Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 EWMGWINPNSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDSTPFTFGPGTKVEIK STAYMELSGLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2289 EVQLVQSGAEVKKPG 2398 DIVMTQSPSSLSASVGDRVTIT 25 ASVKVSCKASGYTFTG CRASQSISSYLNWYQEKPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDSTPFTFGPGTKVEIK STAYMELSGLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2290 QVQLVQSGAEVKKPG 2399 DIQMTQSPSSLSASVGDRVTIT 26 ASVKFSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YYLHWVRQAPGQGLE PKILIYGASRLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLAISSLQPEDFATYY QRFQGRVTMTRDTSIN CQQGDSSPFTFGPGTKVEIK TAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2291 QVQLVQSGAEVKKPG 2400 DIQMTQSPSSLSASVGDRVTIT 27 ASVKFSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YYLHWVRQAPGQGLE PKILIYGASRLQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLAISSLQPEDFATYY QRFQGRVTMTRDTSIN CQQGDSSPFTFGPGTKVEIK TAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2292 EVQLVQSGAEVKKPG 2401 DIVLTQSPSSLSASVGDRVTIT 28 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTIY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYSCATGGSFDAFDIW GQGTMVTVSSAntibody 2293 EVQLVESGAEVKKPG 2402 DIQMTQSPSSLSASVGDRVTIT 29 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPKSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKLEIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2294 EVQLVQSGAEVKKPG 2403 DIQMTQSPSSLSASVGDRVTIT 30 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTSY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKLEIKSTAYMELSRLRSDDTAACTIVE 717944506v1 70Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2295 EVQLVESGAEVKKPG 2404 DIQMTQSPSSLSASVGDRVTIT 31 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2296 EVQLVQSGAEVRKPG 2405 DIQLTQSPSSLSASVGDRVTIT 32 ASVKVSCKASGYTFTA CQASQDISNYLNWYQQKPGK YYIHWVRQAPGQGLE APKILIYGASSLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLAISSLQPEDYATYY QNFQGRVTMTRDTSIS CQQGDSTPFTFGPGTKVEIK TAYMELSRLRPDDTA VYFCAVGGSFDAFDIW GQGTMVTVSSAntibody 2297 EVQLVQSGAEVRKPG 2406 DIQLTQSPSSLSASVGDRVTIT 33 ASVKVSCKASGYTFTA CQASQDISNYLNWYQQKPGK YYIHWVRQAPGQGLE APKILIYGASSLQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLAISSLQPEDYATYY QNFQGRVTMTRDTSIS CQQGDSTPFTFGPGTKVEIK TAYMELSRLRPDDTA VYFCAVGGSFDAFDIW GQGTMVTVSSAntibody 2298 QVQLVQSGAEVKRPG 2407 DIQMTQSPSSVSASVGDRVTIT 34 AAVKVSCKASGYTFT CRASQGISRYLHWYQQKPGK GYYMHWVRQAPGQG APNFLIYGASSLQSGVPSRFSG LEWMGWINPKSGGTN SGSGTDFTLTISSLQPEDFATY YAQNFQGRVTMTRDT YCQQGFSTPFTFGPGTKLEIK SISTAYMELSRLTSDDT AMYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2299 EVQLVQSGAEVKKPG 2408 DIQMTQSPSSLSASVGDRVTIT 35 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYH AQKFQGRVTMTRDTSI CQQGSSPPFTFGPGTKLEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibodv 2300 EVQLVQSGAEVKKPG 2409 DIQMTQSPSSLSASVGDRVTIT 36 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLTISSLQPEDFATYH AQKFQGRVTMTRDTSI CQQGSSPPFTFGPGTKLEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDIWGQGTMVTVSSACTIVE 717944506v1 71Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 2301 EVQLVQSGAEVKSPG 2410 DIVMTQSPSSLSASVGDRVTIT 37 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PNFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGYSSPFTFGPGTKVDIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2302 EVQLVQSGAEVKSPG 2411 DIVMTQSPSSLSASVGDRVTIT 38 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PNFLIYGASRLQSGVPSRFSGS EWMGWINPKSGGTKY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGYSSPFTFGPGTKVDIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2303 EVQLVQSGAEVKKPG 2412 DIQMTQSPSSLSASVGDRVTIT 39 ASVKVSCKASGYTFTA CRASQSISRYLNWYQQKPGKA YYLHWVRQAPGQGLE PKILIYGASSVQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLAISSLQPEDFATYY QKFQGRVTMTRDTSIS CQQGDSSPFTFGPGTKLEIK TAYMELSRLRSDDTA VYYCASGGSFDAFDIW GQGTMVTVSSAntibodv 2304 EVQLVQSGAEVKKPG 2413 DIQMTQSPSSLSASVGDRVTIT 40 ASVKVSCKASGYTFTA CRASQSISRYLNWYQQKPGKA YYLHWVRQAPGQGLE PKILIYGASSVQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLAISSLQPEDFATYY QKFQGRVTMTRDTSIS CQQGDSSPFTFGPGTKLEIK TAYMELSRLRSDDTA VYYCASGGSFDAFDIW GQGTMVTVSSAntibody 2305 QVQLVESGAEVKKPG 2414 DIVLTQSPSSLSASVGDRVTIT 41 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YFIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLTISSLQPEDFVTYY QKFQDRVTMTRDTSIS CQQGHSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody- 2306 QVQLVQSGAEVKSPG 2415 DIQMTQSPSSLSASVGDRVTIT 42 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGDSTPFTFGPGTKVEIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody- 2307 QVQLVQSGAEVKSPG 2416 DIQMTQSPSSLSASVGDRVTIT 43 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGSACTIVE 717944506v1 72Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 EWMGWINPKSGGTKY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGDSTPFTFGPGTKVEIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2308 QVQLVQSGAEVKKPG 2417 DIVMTQSPSSLSASVGDRVTIT 44 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPNSGGTSSA GSGTDFTLTISSLQPEDFATYS QKFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKVDIK TAYMDLSRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2309 QVQLVQSGAEVKKPG 2418 DIVMTQSPSSLSASVGDRVTIT 45 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPKSGGTSSA GSGTDFTLTISSLQPEDFATYS QKFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKVDIK TAYMDLSRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2310 EVQLVQSGAEVKKPG 2419 DIVMTQSPSSLSASVGDRVTIT 46 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASSLQSGVPSRFSGS WMGWVNPNSGGTNY GSGTDFTLTISSLQPEDFATYY AQSFQGRVTMTGDTSI CQQGHSTPFTFGPGTKVDIK TTAYMDLSELRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2311 EVQLVQSGAEVKKPG 2420 DIVMTQSPSSLSASVGDRVTIT 47 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASSLQSGVPSRFSGS WMGWVNPKSGGTNY GSGTDFTLTISSLQPEDFATYY AQSFQGRVTMTGDTSI CQQGHSTPFTFGPGTKVDIK TTAYMDLSELRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2312 QVQLVQSGAEVKSPG 2421 DIQMTQSPSSLSASVGDRVTIT 48 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPNSGGTKY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTVTRDTSI QQGDSTPFTFGPGTKVDIK STAYMELNRLTSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2313 QVQLVQSGAEVKSPG 2422 DIQMTQSPSSLSASVGDRVTIT 49 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPKSGGTKY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTVTRDTSI QQGDSTPFTFGPGTKVDIKSTAYMELNRLTSDDTAACTIVE 717944506v1 73Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2314 EVQLVQSGAEVKKPG 2423 DIVLTQSPSSLSASVGDRVTIT 50 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKILIYGASSLQSGVPSRFSGSG WMGWINPKSGGTNYA SGTDFTLAISSLQPEDFATYYC QKFQGRVTMTRDTSIS QQGDSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2315 EVQLVQSGAEVKKPG 2424 DIVLTQSPSSLSASVGDRVTIT 51 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPNSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2316 EVQLVQSGAEVKKPG 2425 DIVLTQSPSSLSASVGDRVTIT 52 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPKSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2317 QVQLVQSGAEVKKPG 2426 DIVMTQSPSSLSASEGDRVTIT 53 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWIHPNSGGTNS GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2318 QVQLVQSGAEVKKPG 2427 DIVMTQSPSSLSASEGDRVTIT 54 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWIHPKSGGTNT GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibodv 2319 QVQLVQSGAEVKKPG 2428 DIQMTQSPSSLSASVGDRVTIT 55 ASVKVSCKASGYTFTG CRASQSISRYLNWYQQKPGKA YF1HWVRQAPGQGLE PKILIYGASSVQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLAISSLQPEDFATYY QKFQGRVTMTRDTSIS CQQGDSSPFTFGPGTKVEIK TAYMELSRLS SDDTAV YYCASGGSFDAFDIWGQGTMVTVSSACTIVE 717944506v1 74Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 2320 QVQLVQAGAEVKKPG 2429 DIQMTQSPSSLSASVGDRVTIT 56 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2321 QVQLVQAGAEVKKPG 2430 DIQMTQSPSSLSASVGDRVTIT 57 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2322 EVQLVQSGAEVKNPG 2431 DIVMTQSPSSLSASVGDRVTIT 58 ASVKVSCKASGYTFTG CRASQSISNYLNWYQQKPGK YYMHWVRQAPGQGL APKFLIYGTSRLQSGVPSRFSG EWMGWINPNSGGPNY SGSGTDFTLTISSLQPEDFATY AQKFQDRVTMTRDTSI YCQQGYSSPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibodv 2323 EVQLVQSGAEVKNPG 2432 DIVMTQSPSSLSASVGDRVTIT 59 ASVKVSCKASGYTFTG CRASQSISNYLNWYQQKPGK YYMHWVRQAPGQGL APKFLIYGTSRLQSGVPSRFSG EWMGWINPKSGGPNY SGSGTDFTLTISSLQPEDFATY AQKFQDRVTMTRDTSI YCQQGYSSPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2324 EVQLVESGAEVKKPG 2433 DIVMTQSPSSLSASVGDRVTIT 60 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YFMHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLTISSLQPEDFATYY QRFQGRVTMTRDTSIN CQQGYSSPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2325 EVQLVESGAEVKKPG 2434 DIVMTQSPSSLSASVGDRVTIT 61 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YFMHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLTISSLQPEDFATYY QRFQGRVTMTRDTSIN CQQGYSSPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2326 EVQLVQSGAEVKKPG 2435 DIVMTQSPSSLSASVGDRVTIT 62 ASVNVSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGSACTIVE 717944506v1 75Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 EWMGWINPNSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDNTPFTFGPGTKLEIK STAYMELSRLISDDTA VYYCATGGSFDAFDV WGQGTMVTVSSAntibody 2327 EVQLVQSGAEVKKPG 2436 DIVMTQSPSSLSASVGDRVTIT 63 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDNTPFTFGPGTKLEIK STAYMELSRLISDDTA VYYCATGGSFDAFDV WGQGTMVTVSSAntibody 2328 QVQLVQSGAEVKKPG 2437 DIVLTQSPSSLSASVGDRVTIT 64 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMQWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTIY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYSCATGGSFDAFDIW GQGTMVTVSSAntibody 2329 QVQLVQSGAEVKKPG 2438 DIVLTQSPSSLSASVGDRVTIT 65 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMQWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPKSGGTIY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYSCATGGSFDAFDIW GQGTMVTVSSAntibody 2330 EVQLVESGAEVKNPG 2439 DIVMTQSPSSLSASVGDRVTIT 66 ASVKVSCKASGYTFTG CRASQS1SSYLNWYQQQPGKA YYLHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWIKPNSGGTNYA GSGTDFTLTINSLQPEDFATYF QKFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKVEIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2331 EVQLVESGAEVKNPG 2440 DIVMTQSPSSLSASVGDRVTIT 67 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQQPGKA YYLHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWIKPKSGGTNYA GSGTDFTLTINSLQPEDFATYF QKFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKVEIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2332 QVQLVQSGAEVKKPG 2441 DIVLTQSPASLSASVGDRVAIT 68 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASSLQSGVPSRFSGS EWMGWVNPNSGGTN GSGTDFTLTISSLQPEDFATYY YAQNFQGRVTMTGDT CQQGHSTPFTFGPGTKLEIKSITTAYMDLSGLRSDDACTIVE 717944506v1 76Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 TAVYYCAVGGSFDAF DIWGQGTMVTVSSAntibody 2333 QVQLVQSGAEVKKPG 2442 DIVLTQSPASLSASVGDRVAIT 69 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASSLQSGVPSRFSGS EWMGWVNPKSGGTN GSGTDFTLTISSLQPEDFATYY YAQNFQGRVTMTGDT CQQGHSTPFTFGPGTKLEIK SITTAYMDLSGLRSDD TAVYYCAVGGSFDAF DIWGQGTMVTVSSAntibody 2334 QVQLVQSGAEVKKPG 2443 DIVMTQSPSSLSASVGDRVTIT 70 ASVKVSCKASGYTFTG CRASQTISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPNSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVDIK STAYMELSRLISDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2335 QVQLVQSGAEVKKPG 2444 DIVMTQSPSSLSASVGDRVTIT 71 ASVKVSCKASGYTFTG CRASQTISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPKSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVDIK STAYMELSRLISDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2336 QVQLVQSGAEVKKPG 2445 DIVLTQSPSSLSASVGDRVTIT 72 ASMKVSCKASGYTFT CRASQSISKYLIWYQQKPGKA GYYMHWVRQAPGQG PNLLIYGASSLQSGVPSRFSGS LEWMGWINPNSGGTN GSGTDFTLTISSLQPEDFATYY YAQRFQGRVTMTRDT CQQGHSTPFTFGPGTKVDIK SVSTAYMDLSRLRSDD TAVYYCATGGSFDAF DIWGQGTMVTVSSAntibody 2337 QVQLVQSGAEVKKPG 2446 DIVLTQSPSSLSASVGDRVTIT 73 ASMKVSCKASGYTFT CRASQSISKYLIWYQQKPGKA GYYMHWVRQAPGQG PNLLIYGASSLQSGVPSRFSGS LEWMGWINPKSGGTN GSGTDFTLTISSLQPEDFATYY YAQRFQGRVTMTRDT CQQGHSTPFTFGPGTKVDIK SVSTAYMDLSRLRSDD TAVYYCATGGSFDAF DIWGQGTMVTVSSAntibodv 2338 EVQLVESGAEVKKPG 2447 DIQLTQSPSSLSASVGDRVTIT 74 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWIKPNSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDIWGQGTMVTVSSACTIVE 717944506v1 77Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 2339 EVQLVESGAEVKKPG 2448 DIQLTQSPSSLSASVGDRVTIT 75 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWIKPKSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2340 EVQLVESGAEVKKPG 2449 DIVMTQSPSSLSASVGDRVTIT 76 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLTISSLQPEDFATYY QKFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKVDIK TAYMDLSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2341 EVQLVESGAEVKKPG 2450 DIVMTQSPSSLSASVGDRVTIT 77 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPKSGGTNYA GSGTDFTLTISSLQPEDFATYY QKFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKVDIK TAYMDLSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibodv 2342 EVQLVQSGAEVKSPG 2451 DIVLTQSPSSLSASVGDRVTIT 78 ASVKVSCKASGYTFTA CRASLSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKLLIYGASSLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGHSTPFTFGPGTKLEIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2343 EVQLVQSGAEVKSPG 2452 DIVLTQSPSSLSASVGDRVTIT 79 ASVKVSCKASGYTFTA CRASLSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKLLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTKY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGHSTPFTFGPGTKLEIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2344 QVQLVQSGAEVKKPG 2453 DIQMTQSPSSLSASVGDRVTIT 80 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPNSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2345 EVQLVQSGAEVKKPG 2454 DIQMTQSPSSLSASVGDRVTIT 81 APVKVSCKASGYTFTG CRSSQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSGACTIVE 717944506v1 78Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 EWMGWINPNSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2346 EVQLVQSGAEVKKPG 2455 DIQMTQSPSSLSASVGDRVTIT 82 APVKVSCKASGYTFTG CRSSQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPKSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2347 EVQLVQSGAEVKKPG 2456 DIQMTQSPSSLSASVGDRVTIT 83 ASVKVSCKASGYTFTG CRASRSISSYLNWYQQRPGKA YYMHWVRQAPGQGL PKFLIYGASRLQTGVPSRFSGS EWMGWINPNSGATNF GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVDIK TTAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2348 EVQLVQSGAEVKKPG 2457 DIQMTQSPSSLSASVGDRVTIT 84 ASVKVSCKASGYTFTG CRASRSISSYLNWYQQRPGKA YYMHWVRQAPGQGL PKFLIYGASRLQTGVPSRFSGS EWMGWINPKSGATNF GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVDIK TTAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2349 QVQLVQSGAEVKRPG 2458 DIQMTQSPSSLSASVGDRVTIT 85 ASVKVSCKASGYTFTA CRASQS1NSYLNWYQQKPGK YYLHWVRQAPGQGLE APKFLIYGASSLQSGVPSRFSG WMGWINPNSGGTNYA SGSGTDFTLTI S SLQPEDF ATY QKFQDRVTMTGDTSIS YCQQGYSTPFTFGPGTKVEIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2350 QVQLVQSGAEVKRPG 2459 DIQMTQSPSSLSASVGDRVTIT 86 ASVKVSCKASGYTFTA CRASQSIQSYLNWYQQKPGK YYLHWVRQAPGQGLE APKFLIYGASSLQSGVPSRFSG WMGWINPKSGGTNYA SGSGTDFTLTISSLQPEDFATY QKFQDRVTMTGDTSIS YCQQGYSTPFTFGPGTKVEIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2351 QVQLVQSGAEVKSPG 2460 DIQMTQSPSTLSASVGDRVTIT 87 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGDNTPFTFGPGTKVDIKSTAYMELNRLTSDDTAACTIVE 717944506v1 79Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2352 QVQLVQSGAEVKSPG 2461 DIQMTQSPSTLSASVGDRVTIT 88 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWINPKSGGTKY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGDNTPFTFGPGTKVDIK STAYMELNRLTSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2353 QVQLVQSGAEVKKPG 2462 DIQMTQSPSSLSASVGDRVTIT 89 ASVKVSCKASGYTFTG CRASQSINSYLYWYQQKPGK YYMHWVRQAPGQGL APKLLIYGASSLQSGVPSRFSG EWMGWINPKSGGTNY SGSGTDFTLTISSLQPEDSATY AQKFQGRVTMTRDTSI YCQQGYSTPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCATGGSYDAFDI WGQGTMVTVSSAntibody 2354 QVQLVQSGAEVKKPG 2463 DIQMTQSPSSLSASVGDRVTIT 90 ASVKVSCKASGYTFTG CRASQSIQSYLYWYQQKPGK YYMHWVRQAPGQGL APKLLIYGASSLQSGVPSRFSG EWMGWINPKSGGTNY SGSGTDFTLTISSLQPEDSATY AQKFQGRVTMTRDTSI YCQQGYSTPFTFGPGTKVEIK STAYMELSRLRSDDTA VYYCATGGSYDAFDI WGQGTMVTVSSAntibody 2355 EVQLVQSGAEVKKPG 2464 DIQMTQSPSSLSASVGDRVTIT 91 ASVKVSCKTSGYTFTA CRASQSISSYLNWYQQKPGKA YYLHWVRQAPGQGLE PKILIYGASSLQSGVPSRFSGSG WMGWINPNSGGTSSA SGTDFTLAISSLQPEDFATYYC QKFQGRVTMTRDTSIS QQGDSTPFTFGPGTKVDIK TAYMDLTRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2356 EVQLVQSGAEVKKPG 2465 DIQMTQSPSSLSASVGDRVTIT 92 ASVKVSCKTSGYTFTA CRASQSISSYLNWYQQKPGKA YYLHWVRQAPGQGLE PKILIYGASSLQSGVPSRFSGSG WMGWINPKSGGTSSA SGTDFTLAISSLQPEDFATYYC QKFQGRVTMTRDTSIS QQGDSTPFTFGPGTKVDIK TAYMDLTRLRSDDTA VYYCAVGGSFDAFDI WGQGTMVTVSSAntibodv 2357 QVQLVQSGAEVKKPG 2466 DIVMTQSPSSLSASVGDRVTIT 93 ASVKVSCKASGYTFTG CRASLSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKLL1YGASSLQSGVPSRFSGS EWMGWINPNSGGTHY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKLEIK STAYMELSRLRSDDTA VYFCAVGGSFDAFDIWGQGTMVTVSSACTIVE 717944506v1 80Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 2358 QVQLVQSGAEVKKPG 2467 DIVMTQSPSSLSASVGDRVTIT 94 ASVKVSCKASGYTFTG CRASLSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKLLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTHY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKLEIK STAYMELSRLRSDDTA VYFCAVGGSFDAFDIW GQGTMVTVSSAntibody 2359 EVQLVQSGAEVKKPG 2468 DIVMTQSPSSLSASVGDRVTIT 95 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLTISSLQPEDFATYF QRFQGRVTMTRDTSIS CQQGYSSPFTFGPGTKLEIK TAYMDLSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2360 QVQLVQSGAEVKKPG 2469 EIVMTQSPASLSASVGDRVTIT 96 ASVKVSCKASGYTFTG CRASQTISRYLNWYQQKPGK YYMHWVRQAPGQGL APKFLIYGASSLQSGVPSRFSG EWMGWINPKSGGTIY SGSGTDFTLTISSLQPEDFATY AQKFQGRVTMTRDTSI YCQQSYSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYSCATGGSFDAFDIW GQGTMVTVSSAntibodv 2361 QVQLVQSGAEVKRPG 2470 EIVMTQSPASLSASVGDRVTIT 97 ASLTVSCKSSGYTFTA CRASQTISRYLNWYQQKPGK YYIHWVRQAPGQGLE APKFLIYGASSLQSGVPSRFSG WMGWINPNSGGTNYA SGSGTDFTLTISSLQPEDFATY QKFQGRVTMTRDTSIT YCQQGYSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2362 QVQLVQSGAEVKKPG 2471 DIQMTQSPSSLSASVGDRVTIT 98 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQSPGKA YFMHWVRQAPGQGLE PKILIYGASRLQSGVPSRFRGS WMGWINPKSGGTNYA GSGTDFTLAISSLQPEDFATYY QKFQGRVTMTRDTSIS CQQGDSTPFTFGPGTKVDIK TAYMELSRLRFDDTA VYYCASGGSFDAFDIW GQGTMVTVSSAntibody- 2363 EVQLVESGAEVKKPG 2472 DIVLTQSPSSLSASVGDRVTIT 99 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGRGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLTISSLQPEDFATYF AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKLEIK NTAYMELSRLRPDDT AVYYCATGGSFDAFDI WGQGTMVTVSSAntibody- 2364 EVQLVESGAEVKKPG 2473 DIQMTQSPSSLSASVGDRVTIT 100 ASVKVSCKASGYTFTG CRASQSISRYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSVQSGVPSRFSGSACTIVE 717944506v1 81Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 EWMGWINPNSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGDSSPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCASGGSFDAFDIW GQGTMVTVSSAntibody 2365 QVQLVQSGAEVKKPG 2474 DIQMTQSPSSLSASVGDRVTIT 101 ASVKVSCKASGYTFTG CRASQSISRYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPNSGGTNY SGTDFTLTISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGYSTLFTFGPGTKLEIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2366 EVQLVQSGAEVKKPG 2475 DIQMTQSPSSLSASVGDRVTIT 102 ASVKVSCKASGYTFN CRASQSISSYLNWYQQKPGKA GYYMHWIRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLTISSLQPEDFATYY SQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2367 EVQLVQSGAEVKKPG 2476 DIQMTQSPSSLSASVGDRVTIT 103 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSNPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2368 EVQLVESGAEVKKPG 2477 DIVMTQSPSSLSASVGDRVTIT 104 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKLLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGFSTPFTFGPGTKLEIK NTAYMELSRLRSDDT AVYYC AS GGSID AFDI WGQGTMVTVSSAntibody 2369 QVQLVQ SE AEVKKPG 2478 DIQMTQSPSSLSASVGDRVTIT 105 ASVKVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASRLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLTISSLQPEDFATYY QKFQDRVTMTGDTSIS CQQGYSSPFTFGPGTKVDIK TAYMELRRLRSDDTA VYYCAVGGSYDAFDI WGQGTMVTVSSAntibody 2370 EVQLVQSGAEVKKPG 2479 DIVMTQSPSSLSASVGDRVTIT 106 ASMKVSCKASGYTFT CRASQSISRYLNWYQQKPGKA GYYIHWVRQAPGQGL PNFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLTISSLQPEDFATYY AQKFHGRVTLTRDTSV CQQGYSSPFTFGPGTKVDIKNTAYMDLSGLRSDDTACTIVE 717944506v1 82Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 AVYYCAVGGSFDAFDI WGQGTMVTVSSAntibody 2371 EVQLVQSGAEVKKPG 2480 DIQMTQSPSSLSASVGDRVTIT 107 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKILIYGASSLQSGVPSRFSGSG EWMGWINPNSGGTNY SGTDFTLAISSLQPEDFATYYC AQKFQGRVTMTRDTSI QQGDSTPFTFGPGTKVDIK STAYMELSRLISDDTA VYYCVTGGSFDAFDV WGQGTMVTVSSAntibody 2372 QVQLVQSGAEVKKPG 2481 DIVMTQSPSSLSASVGDRVTIT 108 ASVRVSCKASGYTFTG CRASQSISSFLNWYQQSPGKA YYMHWVRQAPGQGL PKILIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLAISSLQPEDFATYY AQKFQGRVTVTRDTSI CQQGDSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCTSGGSFDAFDIW GQGTMVTVSSAntibody 2373 EVQLVQSGAEVKRPG 2482 DIQMTQSPSSLSASVGDRVTIT 109 ASLTVSCKSSGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKFLIYGASSLQSGVPSRFSGS WMGWINPNSGGTNYA GSGTDFTLTISSLQPEDFATYY QRFQGRVTMTRDTSIS CQQGHSTPFTFGPGTKVDIK TAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2374 EVQLVQSGAEVKKPG 2483 DIVMTQSPSSLSASVGDRVTIT 110 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTNY GSGTDFTLTISSLQPEDFAAYY AQKFQGRVTMTRDTSI CQQGHSTPFTFGPGTKVDIK STAYMELSRLRSDDTA VYYCASGGSFDAFDIW GQGTMVTVSSAntibody 2375 EVQLVESGAEVKKPG 2484 DIVMTQSPSSLSASVGDRVTIT 111 ASVRVSCKASGYTFTA CRASQSISSYLNWYQQKPGKA YYIHWVRQAPGQGLE PKLLIYGASRLQSGVPSRFSGS WMGWINPNSGGTSSA GSGTDFTLTISSLQPEDFASYF QKFQGRVTMTRDTSIS CQQGHSTPITFGQGTKLEIK TAYMDLNRLRSDDTA MYYCAVGGSFDAFDI WGQGTMVTVSSAntibodv 2376 EVQLVQSGAEVKRPG 2485 DIQLTQSPSSLSASVGDRVTIT 112 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYF AQKFQGRVTMTRDTSI CQQGYSSPFTFGPGTKVDIK STAYLELSRLRSDDTA VYYCATGGSYDAFDIWGQGTMVTVSSACTIVE 717944506v1 83Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Antibody 2377 QVQLVQSGAEVKKPG 2486 DIVLTQSPSSLSASVGDRVTIT 113 ASVKVSCKASGYTFTG CRASQSISRYLYWYQQNPGKA YYMHWVRQAPGQGL PKLLIYAASSLQSGVPSRFSGS EWMGWINPNSGGTKY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYDTPFTFGPGTKVDIK STAYMELSSLRSDDTA VYYCATGGSYDAFDI WGQGTMVTVSSAntibody 2378 EVQLVESGAEVKKPG 2487 DIQLTQSPSSLSASVGDRVTIT 114 ASVKVSCKASGYTFTG C Q AS QDI SNYLNWYQQKPGK YYMHWVRQAPGQGL APKLLIYAASSLQTGVPSRFSG EWMGWINPKSGGTNY SGSGTDFTLAISSLQPEDFATY AQKFQGRVTMTRDTSI YCQQGDSTPFTFGPGTKLEIK STAYMELSRLRSDDTA VYYCATGGSFDAFDI WGQGTMVTVSSAntibody 2379 QVQLVQSGSDLKKPG 2488 EIVLTQSPGTLSLSPGERATLS 115 ASVKVSCKASGYTFTR CRASQSVSDSYLAWYQQKPG YGMNWVRQAPGQGL QAPRLLIYGASSRATGIPDRFS EWMGWINTNTGNPTY GSGSGTDFTLTISRLEPEDFAV AQDFTGRFVFSLDTSV YYCQQYGTSPITFGQGTKLEIK STAYLQIS SLKAEDTA VYYCARDNWNYVSD YWGQGTLVTVSSAntibodv 2380 EVQLVQSGAEVKKPG 2489 DIQMTQSPSSLSASVGDRVIIT 116 ASVKVSCKASGYTFTG CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKLLIYGASSLQSGVPSRFSGS EWMGWINPKSGGTIY GAGTEFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQAKSFPLTFGGGTKVEIK STAYMELSRLRSDDTA VYSCATGGSFDAFDIW GQGTMVTVSSAntibody 2381 EVQLVESGAEVKKPG 2490 DIVMTQSPSSLSASVGDRVTIT 117 ASVKVSCKASGYTFTV CRASQSISSYLNWYQQKPGKA YYMHWVRQAPGQGL PKFLIYGASRLQSGVPSRFSGS EWMGWINPNSGGTNY GSGTDFTLTISSLQPEDFATYY AQKFQGRVTMTRDTSI CQQGYSSPFTFGGGTKVDIK STAYMELSRLRSDDTA VYYCASGGSFDAFDIW GQGTMVTVSSAntibody 2382 QVQLVQSGSELQKPG 2491 DIVMTQTPLSSPVPLGQPASIS 118 ASVKVSCKTSGYTFTR CKSSQSLVHSDGNTYLSWLQQ YGMNWVRQAPGQGL RPGQPPRLLIYKISNRFSGVPD EWMGWINTNTGNPTY RFSGSGAGTDFTLKISRVEAED AQGFTGRFVFSLDTSV VGVYYCMQVTQFPITLGQGT STAYLQIS SLKAEDTA KLEIK VYYCARDNWNYDFD YWGQGTTVTVSSAntibody 2383 QVQLVQSGSELKRPGA 2492 DIVMTQTPLSSPVTLGQPASIS 119 SVKVSCKASGYTFTTY CRSSQSLVHSDGNTYLSWLQQ GMNWVRQAPGQGLE RPGQPPRLLIYKISNRFSGVPDACTIVE 717944506v1 84Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 WMGWINTNTGNPTYA RFSGSGAGTDFTLKISRVEAED QGFTGRFVFSLDTSVS VGVYYCMQATQFPITLGQGT TAYLQISSLKAEDTAV KLEIK YYC ARDNWNYDLDYWGQGTLVTVSS

[0122] In some embodiments, the anti-TLl A antibody binds an epitope that includes at least 5 (e.g., 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25) amino acid residues selected from Lys243, Lys240, Thr239, Tyr238, Asp237, Val236, Leu235, Ser234, Ile233, Asp232, Metl58, Argl56, Trpll9, Hisll8, Lyslll, PhellO, Hisl09, Glnl08, Thrl07, Prol06, Thrl05, Glnl04, Argl03, Vall02, and VallOl of aTLIA polypeptide comprising SEQ ID NO: 2493. In another embodiment, the anti-TLIA antibody binds an epitope that includes at least 5 (e.g. 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, or 24) amino acid residues selected from Vai 101, Vai 102, Arg 103, Gin 104, Thr 105, Pro 106, Thr 107, Gin 108, His 109, Phe 110, Lys 111, His 118, Trp 119, Glu 120, Glu 122, Leu 123, Gly 124, Lys 137, Arg 156, Gly 157, Met 158, Ser 234, Tyr 238, and Thr 239 of SEQ ID NO: 2493. In another embodiment, the anti-TLIA antibody binds an epitope that includes at least 5 (e.g., 5, 6, 7, 8, 9,10, 11, 12, 13, 14, 15, 16, 17, 18, or 19) amino acid residues selected from Vai 102, Arg 103, Gin 104, Thr 105, Thr 107, Gin 108, His 118, Trp 119, Glu 120, Glu 122, Leu 123, Gly 124, Lys 137, Arg 156, Gly 157. Met 158. Ser 234, Tyr 238, and Thr 239 of SEQ ID NO: 2493. In another embodiment, the anti-TLIA antibody binds an epitope that includes at least 5 (e.g., 5, 6, 7, 8, or 9) amino acid residues selected from Lys240, Thr239, Tyr238, Asp237, Val236, Leu235, Ser234, Glnl04, and Argl03 of SEQ ID NO: 2493. In some embodiments, the TL1 A binding antibody specifically binds to the TL1A polypeptide comprising SEQ ID NO: 2493 at one or more of amino acid residues Vai 102, Arg 103. Gin 104. Glu 120, Glu 122, Leu 123, and Arg 156.

[0123] In some embodiments, the anti-TLIA antibody binds an epitope that includes at least 5 (e.g. 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, or 15) amino acid residues selected from Argl03, Thrl05, Prol06, Thrl07, Glnl08, Hisl09, Argl56, Asp232, Ile233, Ser234. Leu235. Asp237, Tyr238, Thr239, Lys240, and Glu241 of aTLIA polypeptide comprising SEQ ID NO: 2493. In some embodiments, the anti-TLIA antibody binds an epitope that includes at least 5 (e.g. 5, 6, 7, 8, 9, 10, 11, or 12) amino acid residues selected from Argl03, Thrl07, Glnl08, Hisl09, Argl56, Ser231, Ile233. Ser234, Asp237. Tyr238, Thr239, and Glu241 of a TL1 A polypeptide comprising SEQ ID NO: 2493. In some embodiments, the anti-TLIA antibody is aTLIA trimer disruptor. In some embodiments, the anti-TLl A antibody, upon binding to TL1 A trimer, increases rate of dissociation of the TL1A trimer into TL1A monomer by at least 10%, at least 20%, at least 50%, ACTIVE 717944506v1 85Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 or more, compared to no treatment. Non-limiting exemplary disruptors include Antibody 19, Antibody 63, Antibody 86 and Antibody 98.

[0124] In some embodiments, the anti-TLl A antibody binds an epitope that includes at least 5 (e.g. 5, 6. 7, 8, 9, 10, 11, 12, 13, 14, or 15) amino acid residues selected from VallOl, Argl03. Glnl04, Thrl05, Thrl07, Hisl 18, Glul20, Hisl21, Glul22, Leul23, Argl56, Metl58, Ser234, Tyr238, and Thr239 of aTLIA polypeptide comprising SEQ ID NO: 2493. In some embodiments, the anti-TLIA antibody binds an epitope that includes at least 5 (e.g. 5 or 6) amino acid residues selected from Argl03, Thrl07, Hisll8, Glul20. Argl56, and Tyr238 of a TL1A polypeptide comprising SEQ ID NO: 2493. In some embodiments, the anti-TLIA antibody is a TL1A trimer stabilizer. In some embodiments, the anti-TLIA antibody, upon selectively binding to a TL1A trimer, decreases rate of dissociation of the TL1A trimer into TL1A monomer by at least 10%, at least 20%, at least 50%, at least 80%, or more compared to no treatment. Nonlimiting exemplary trimer-binding anti-TLIA antibodies include Antibody 10, Antibody 47, Antibody 49, Antibody 69, Antibody 71 and Antibody 92.

[0125] In some embodiments, the TL1A binding antibody is a TL1 A binding antibody disclosed in PCT application No. PCT / US24 / 41774 entitled " TL1 A BINDING PROTEINS AND METHODS OF USE," filed on August 9, 2024, which is incorporated by reference herein in its entirety. In some embodiments, the TL1A binding antibody is a TL1 A binding antibody disclosed in PCT application No PCT / US24 / 34949 entitled " TL1A ANTIBODY COMPOSITIONS AND METHODS OF USE" filed on June 21, 2024, which is incorporated by reference herein in its entirety.Fc Modifications

[0126] The TL1A binding protein may comprise a modified Fc region. Unless otherwise specified herein, numbering of amino acid residues in the Fc region or constant region is according to the EU numbering system, also called the EU index, as described in Kabat et al, Sequences of Proteins of Immunological Interest, 5th Ed. Public Health Service, National Institutes of Health, Bethesda, MD, 1991.

[0127] In some embodiments, the TL1 A binding protein comprises a modified Fc domain comprising one or more modifications. In some embodiments, the one or more modifications are located in a Fc from IgGl (e.g., human IgGl (hlgGl)). In some embodiments, the one or more modifications are located in a Fc from IgG4 (e.g., human IgG4 (hIgG4)). In some embodiments, the one or more modifications are located in a Fc from IgG2. In some embodiments, the one or more modifications promote selective binding of Fc-gamma receptors. ACTIVE 717944506v1 86Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0128] In some embodiments, one or more modifications in the modified Fc is selected from the group consisting of: S298A, E333A, K334A, K326A, F243L, R292P, Y300L, V305I, P396L, F243L, R292P. Y300L, L235V, P396L, F243L, S239D. I332E, A330L, S267E, L328F, D265S, S239E. K326A, A327H, G237F. K326E, G236A, D270L. H268D, S324T, L234F, N325L, V266L, and S267D. In some embodiments, one or more modifications in the modified Fc is selected from the group consisting of S228P, M252Y, S254T, T256E, T256D, T250Q, H285D, T307A, T307Q, T307R, T307W, L309D, Q411H, Q311V, A378V, E380A, M428L, N434A, N434S. N297A, D265A, L234A, L235A, and N434W.

[0129] In some embodiments, the modified Fc comprises a specific combination of amino acid substitutions selected from the group consisting of: L234A / L235A; V234AG237A;L235AG237AE318A; S228P / L236E; H268Q / V309L / A330S / A331S;C220S / C226S / C229S / P238S; C226S / C229S / E3233P / L235V / L235A; L234F / L235E / P331S; C226S / P230S; L234A / G237A; L234A / L235A / G237A; Q311R / M428L; and L234A / L235A / P329G.

[0130] In some embodiments, the modified Fc comprises a specific combination of amino acid substitutions selected from the group consisting of M428L / N434S (LS); M252Y / S254T / T256E (YTE); T250Q / M428L; T307A / E380A / N434A; T256D / T307Q (DQ); T256D / T307W (DW); M252Y / T256D (YD); T307Q / Q311V / A378V (QVV); T256D / H285D / T307R / Q311V / A378V (DDRVV); L309D / Q311H / N434S (DHS); S228P / L235E (SPLE); L234A / L235A (LALA);M428L / N434A (LA); L234A / G237A (LAGA); L234A / L235A / G237A (LALAGA);L234AL235 P329G (LALAPG); N297AYTE; D265A / YTE; LALA / YTE; LAGAYTE;LALAGAYTE; LALAPG / YTE: N297A / LS; D265ALS; LALA / LS; LAGALS; LALAGALS; LALAPG / LS; N297A / DHS; D265A / DHS; LALA / DHS; LAGA / DHS; LALAGA / DHS;LALAPG / DHS; SP / YTE; SPLE / YTE; SP / LS; SPLE / LS; SP / DHS; SPLE / DHS; N297A / LA; D265A / LA; LALA / LA; LAGALA; LALAGA / LA; LALAPG / LA; N297A / N434A;D265A / N434A; LALA / N434A; LAGA / N434A; LALAGA / N434A; LALAPG / N434A;N297A / N434W; D265A / N434W; LALA / N434W; LAGA / N434W; LALAGA / N434W;LALAPG / N434W; N297A / DQ; D265A / DQ; LALA / DQ; LAGA / DQ; LALAGA / DQ;LALAPG / DQ; N297A / DW; D265A / DW; LALA / DW; LAGA / DW; LALAGA / DW;LALAPG / DW; N297A / YD; D265AYD; LALAYD; LAGA / YD; LALAGAYD;LALAPG / YD: N297AQVV; D265 QVV; LALAQVV; LAGAQVV, LALAGAQVV;LALAPG / QVV; N297ADDRVV; D265ADDRVV; LALADDRVV; LAGADDRVV;LALAGADDRVV; LALAPG / DDRVV; SP / Q311R / M428L; SPLE / Q311R / M428L;N297A / Q311R / M428L; D265A / Q311R / M428L; LALA / Q311R / M428L;ACTIVE 717944506v1 87Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 LAGA / Q311R / M428L; LALAGA / Q311R / M428L; and LALAPG / Q311R / M428L. In some embodiments, the modified Fc comprises a specific combination of amino acid substitutions selected from the group consisting of L234A / L235A and P329G (PG). In some embodiments, the modified Fc comprises L234A / L235A modifications. In some embodiments, the modified Fc comprises P329G (PG) modifications.

[0131] In certain embodiments, the Fc region comprises one or more amino acid substitutions, wherein the one or more substitutions result in an increase in antibody half-life, and / or in a reduction of Fc functionality' compared with the Fc without the one or more substitutions. In certain embodiments, the one or more amino acid substitutions results in increased antibody half- life at pH 6.0 compared to an antibody comprising a wild-type Fc region. In certain embodiments, the antibody has an increased half-life that is about 10,000-fold, 1,000-fold, 500-fold, 100-fold, 50-fold, 20-fold, 10-fold, 9-fold, 8-fold, 7-fold, 6-fold, 5-fold, 4.5-fold, 4-fold, 3.5-fold, 3-fold, 2.5-fold, 2-fold, 1.95-fold, 1.9-fold. 1.85-fold, 1.8-fold, 1.75-fold, 1.7-fold, 1.65-fold, 1.6-fold. 1.55-fold, 1.50-fold, 1.45-fold, 1.4-fold. 1.35-fold, 1.3-fold, 1.25-fold, 1.2-fold, 1.15-fold, 1.1 -fold, or 1.05-fold longer compared to an antibody comprising a wild-type Fc region.

[0132] In certain embodiments, the Fc region comprises one or more amino acid substitutions, wherein the one or more substitutions result in a decrease in one or more of ADCC activity, ADCP activity, or CDC activity compared with the Fc without the one or more substitutions.

[0133] In some embodiments, the binding proteins described herein include posltranslational modifications to improve its ability to mediate effector function. Such modifications are known in the art and include afucosylation, or engineering of the affinity of the Fc towards an activating receptor, mainly FCGRIIIa for antibody-dependent cellular cytotoxicity7(ADCC), and / or towards Clq for complement-dependent cytotoxicity (CDC).

[0134] In some embodiments, an antibody provided herein comprises a Fc domain (e.g., IgGl) with reduced fucose content at position Asn 297 (EU numbering) compared to a naturally occurring Fc domain. Such Fc domains are known to have increased ADCC. In some aspects, such antibodies do not comprise any' fucose at position Asn 297.

[0135] In some embodiments, the binding proteins described herein comprise an Fc region with one or more amino acid substitutions which increase ADCC, such as a substitution at one or more of positions 298, 333, and 334 of the Fc region. In some embodiments, an antibody provided herein comprises an Fc region with one or more amino acid substitutions at positions 239, 332, and 330.ACTIVE 717944506v1 88Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0136] In some embodiments, the binding proteins described herein comprise an Fc region with at least one galactose residue in the oligosaccharide attached to the Fc region. Such antibody variants may have improved CDC function.

[0137] In some embodiments, the binding proteins described herein comprise one or more alterations that improve or diminish Clq binding and / or CDC.

[0138] In certain embodiments, the Fc region binds an Fey Receptor selected from the group consisting of: FcyRI, FcyRIIa, FcyRIIb, FcyRIIc, FcyRIIIa, and FcyRIIIb. In certain embodiments, the Fc region binds an Fey Receptor with higher affinity at pH 6.0 compared to an antibody comprising a wild-type Fc region.

[0139] In some embodiments, the TL1A binding proteins described herein (e.g. anti-TLl A antibodies) comprise an extended half-life (i.e., serum half-life) and are also referred herein as long acting TL1A binding proteins. In some embodiments, the TL1A binding proteins described herein comprise a half-life of at least about 10, 12, 14, 16, 18, 20, 22, 24, 26, 28, 42, 56, 70, 84, 96, or more than 96 days. In some embodiments, the TL1A binding proteins described herein comprise a half-life in a range of about 10 to about 20 days, about 10 to about 30 days, about 18 days to about 30 days, about 14 days to about 96 days, about 14 days to about 84 days, about 14 days to about 70 days, about 14 days to about 56 days, about 14 days to about 42 days, about 14 days to about 28 days, of about 28 days to about 96 days, about 28 days to about 84 days, about 28 days to about 70 days, about 28 days to about 56 days, about 28 days to about 42 days, of about 42 days to about 96 days, about 42 days to about 84 days, about 42 days to about 70 days, or about 42 days to about 56 days. In some embodiments, the TL1A binding proteins described herein comprise a half-life in a range of about 42 days to about 56 days. In some embodiments, the TL1 A binding proteins described herein comprise a half-life in a range of about 42 days to about 60 days. In a specific embodiment, an anti-TLl A binding protein is an antibody with a popPK half-life of 75 days. In some embodiments, the TL1 A binding proteins described herein comprise a half-life of at least about 18 days. In some embodiments, the TL1A binding proteins described herein comprise a half-life of about 18 days. In some embodiments, the TL1A binding proteins described herein comprise a half-life of at least about 50 days. In some embodiments, the TL1A binding proteins described herein comprise a half-life of about 50 days. Methods of measuring half-life are known in the art. In some embodiments, the half-life is measured in a rodent model, such as Tg276 mice. In some embodiments, the half-life is measured in a nonhuman primate. In some embodiments, the half- life is measured in a human. In some embodiments, the half-life is measured following intravenous administration. In some ACTIVE 717944506v1 89Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 embodiments, the half-life is measured following subcutaneous administration.

[0140] In some embodiments, the TL1 A binding proteins described herein have a half-life that is at least 20% longer than a comparator antibody. In some embodiments, the comparator antibody comprises the same complementarity determining regions and variable regions but different Fc regions. In some embodiments, the half-life of the TL1 A binding proteins described herein is at least 30%, at least 40%, at least 50%, at least 60%, at least 70%, at least 80%, or at least 90% longer than the half-life of the comparator antibody. In some embodiments, the halflife of the TL1 A binding proteins described herein is longer than the half-life of the comparator antibody by at least 2 fold, at least 3 fold, at least 4 fold, at least 5 fold, at least 6 fold, at least 7 fold, at least 8 fold, at least 9 fold, or at least 10 fold.Combination Products and Methods

[0141] Aspects of the disclosure include combination products, compositions and methods of treatment with combinations of the TL1A inhibitors, e.g., anti-TLIA antibodies, with other immunomodulatory drugs. In a specific embodiment, treatment of an inflammatory dermatologic disease includes co-administration of a TL1 A inhibitor, such as an anti-TLIA antibody, and a corticosteroid, an immunosuppressive drug (e.g., methotrexate, azathioprine. my cophenolate mofetil, and cyclophosphamide), which aim to reduce inflammation and slow disease progression. Steroids are often indicated for the treatment of inflammatory conditions and may be used in combination with a TL1 A inhibitor, such as an anti-TLIA antibody, at least transiently.

[0142] In some embodiments, treatment of inflammatory dermatologic diseases includes coadministration of aTLIA inhibitor, such as an anti-TLIA antibody, and at least an IL-23 inhibitor, an IL- 17 inhibitor, an IL- 12 inhibitor, an IL-6 inhibitor, IL-1 inhibitor. In some embodiments, the IL-23 inhibitor is an anti-IL-23 antibody. In some embodiments, the anti-IL-23 antibody is guselkumab, risankizumab. tildrakizumabor mirikizumab, brazikumab or ustekinumab. In some embodiments, the anti-IL-23 antibody is modified to have an extended half-life, e.g., as described in PCT Publication W02024 / 263900. In some embodiments, the IL-17 inhibitor is an anti-IL-17 antibody. The anti-IL-17 antibody can bind IL-17A, IL-17F, or IL17A / F. In some embodiments, the anti-IL-17 antibody is secukinumab. ixekizumab, brodalumab or bimekizumab. In some embodiments, the anti-IL-17 antibody is modified to have an extended half-life as described in PCT Publication WO2024 / 263945. In some embodiments, the IL-12 inhibitor is an anti-IL-12 antibody. The anti-IL-12 antibody can bind IL-12 and / or IL-23. In some embodiments, the anti-IL-12 antibody is ustekinumab. In some ACTIVE 717944506v1 90Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 embodiments, the IL-6 inhibitor is an anti-IL-6 antibody. In some embodiments, the anti-IL-6 antibody is siltuximab, olokizumab, clazakizumab, sirukumab, or vobarilizumab. In some embodiments, the IL-1 inhibitor is an anti-IL-1 antibody. In some embodiments, the anti-IL-1 antibody is canakinumab.

[0143] In a specific embodiment, treatment of an inflammatory dermatologic disease includes co-administration of a TL1 A inhibitor, such as an anti-TLIA antibody, and another active, including but not limited to IL-4 and IL-13 inhibitors (e.g., dupilumab); a TNF inhibitor (e g., etanercept, adalimumab, and infliximab) which targets Tumor Necrosis Factor (TNF); IL- 17 inhibitors (e.g., secukinumab, ixekizumab, and brodalumab); a phosphodiesterase-4 inhibitor (e.g., apremilast), an anti-CD20 antibody (e.g., rituximab); IL-6 inhibitors (e.g., tocilizumab); and B cell Activating Factor (BAFF) inhibitor (e.g., belimumab).

[0144] In a specific embodiment, the anti-IL-23 antibody is an antibody as described in PCT International Application No. PCT / US25 / 14593 filed on February' 5, 2025 entitled “IL-23 BINDING PROTEIN COMPOSITIONS AND METHODS OF USE / ’

[0145] In some embodiments, the anti-IL-23 antibody comprises a heavy chain variable domain comprises complementarity determining regions CDR-H1, CDR-H2, and CDR-H3 with sequences as shown in a table selected from Table 3A. In some embodiments, anti-IL-23 antibody comprises further comprise a light chain variable domain comprising complementarity determining regions CDR-L1, CDR-L2, and CDR-L3 with sequences as shown in the same table of Table 3 A. In some embodiments, anti-IL-23 comprises a heavy chain as shown in Table 3.1 A and alight chain as shown in Table 3.1 A. In some embodiments, an IL-23 binding protein is means for binding IL-23 with a Fc portion modified to increase half-life in humans compared to that antibody without such modification, e.g., M252Y, S254T, and T256E (YTE) and / or M428L and N434S (LS), for example an increase by a factor of at least two, or at least three, or at least four. In some embodiments the half-life extension modification is the YTE modification. In some embodiments the half-life extension modification is the LS modification.

[0146] Table 3A. Exemplary heavy chain variable domain, light chain variable domain, and complementarity-determining region sequences of anti-IL-23 antibodyIL-23binding Heavy chain variable domain Light chain variable domainantibodyACTIVE 717944506v1 91Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Clone QVQLVQSGAEVKKPGSSVKVSCK DIQMTQSPSSLSASVGDRVTITCK MAbOOl ASGYTFTTQTLHWMRQAPGQGLE ASRDVAIAVAWYQQKPGKVPKLL WIGYIYPRDGSTKYNENFKGKVTI IYWASTRHTGVPSRFSGSGSRTDF TADKSTSTAYMELSSLRSEDTAVY TLTIS SLQPEDV ADYFCHQYS S YPF YCAIPDRSGYAWFQHWGQGTLVT TFGSGTKLEIKvss (SEQ ID NO: 2496)(SEQ ID NO: 2495)Kabat CDRsKabat CDRs CDR-L1: KASRDVAIAVACDR-H1: TQTLH (SEQ ID NO: 2500)(SEQ ID NO: 2497)CDR-L2: WASTRHTCDR-H2: YIYPRDGSTKYNENFKG (SEQ ID NO: 2501)(SEQ ID NO: 2498)CDR-L3: HQYSSYPFTCDR-H3: PDRSGYAWFQH (SEQ ID NO: 2502)(SEQ ID NO: 2499)IMGT CDRs IMGT CDRsCDR-H1: GYTFTTQT CDR-L1: RDVAIA(SEQ ID NO: 2503) (SEQ ID NO: 2506)CDR-H2: IYPRDGST CDR-L2: WAS(SEQ ID NO: 2504)CDR-L3: HQYSSYPFTCDR-H3: AIPDRSGYAWFQH (SEQ ID NO: 2502)(SEQ ID NO: 2505)Chothia CDRs Chothia CDRsCDR-H1: GYTFTTQ CDR-L1: SRDVAIA(SEQ ID NO: 2507) (SEQ ID NO: 2510)CDR-H2: YPRDGS CDR-L2: WAS(SEQ ID NO: 2508)CDR-H3: DRSGYAWFQ CDR-L3: YSSYPF(SEQ ID NO: 2509) (SEQ ID NO: 2511)

[0147] Table 3.1 A. Exemplary heavy and light chain amino acid sequences of anti-IL- 23 antibodyAnti-IL-23Heavy chain Light chainantibodyMAbOOl QVQLVQSGAEVKKPGSSVKVSCK DIQMTQSPSSLSASVGDRVTITCK ASGYTFTTQTLHWMRQAPGQGLE ASRDVAIAVAWYQQKPGKVPKLLWIGYIYPRDGSTKYNENFKGKVTI IYWASTRHTGVPSRFSGSGSRTDF ACTIVE 717944506v1 92Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 TADKSTSTAYMELSSLRSEDTAVY TLTIS SLQPEDV ADYFCHQYS S YPF YCAIPDRSGYAWFQHWGQGTLVT TFGSGTKLEIKRTVAAPSVFIFPPS VSSASTKGPSVFPLAPSSKSTSGGT DEQLKSGTASVVCLLNNFYPREA AALGCLVKDYFPEPVTVSWNSGA KVQWKVDNALQSGNSQESVTEQ LTSGVHTFPAVLQSSGLYSLSSVV DSKDSTYSLSSTLTLSKADYEKHK TVPSSSLGTQTYICNVNHKPSNTK VYACEVTHQGLSSPVTKSFNRGEC VDKKVEPKSCDKTHTCPPCPAPEA (SEQ ID NO: 2601) AGGPSVFLFPPKPKDTLYITREPEV TC V V VDV SHEDPEVKFNWYVDG VEVHNAKTKPREEQYNSTYRVVS VLTVLHQDWLNGKEYKCKV SNK ALPAPIEKTISKAKGQPREPQVYTL PPSRDELTKNQVSLTCLVKGFYPS DIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGN VFSCSVMHEALHNHYTQKSLSLSP GK(SEQ ID NO: 2600)

[0148] In some embodiments, anti-IL-23 antibody comprises a heavy chain variable domain comprises complementarity determining regions CDR-H1, CDR-H2, and CDR-H3 with sequences as shown in a table selected from Table 3B. In some embodiments, anti-IL-23 antibody comprises further comprise a light chain variable domain comprising complementarity determining regions CDR-L1, CDR-L2, and CDR-L3 with sequences as shown in the same table of Table 3B. In some embodiments, anti-IL-23 antibody comprises a heavy chain as shown in Table 3. IB and a light chain as shown in Table 3. IB. In some embodiments, an IL-23 binding protein is means for binding IL-23 with a Fc portion modified to increase half-life in humans compared to that antibody without such modification, e.g., M252Y, S254T, and T256E (YTE) and / or M428L and N434S (LS), for example an increase by a factor of at least two, or at least three, or at least four. In some embodiments the half-life extension modification is the YTE modification. In some embodiments the half-life extension modification is the LS modification.

[0149] Table 3B. Exemplary heavy chain variable domain, light chain variable domain, and complementarity-determining region sequences of anti-IL-23 antibodyAnti-IL-23Heavy chain variable domain Light chain variable domain antibodyClone QVQLVQSGAEVKKPGSSVKVSCK DIQMTQSPSSLSASVGDRVTITCK MAb003 ASGYTFTSQTMHWMRQAPGQGL ASRDVAIAVAWYQQKPGKVPKLL EWIGYIYPRDDYPKYNDNFKGKV IYWASTRHTGVPSRFSGSGSRTDFTITADKSTSTAYMELSSLRSEDTAACTIVE 717944506v1 93Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 VYYC AIPDRS GYAWFIHWGQGTL TLTIS SLQPEDV ADYFCHQYS S YPF VTVSS TFGSGTKLEIK(SEQ ID NO: 2512) (SEQ ID NO: 2496)Kabat CDRsCDR-H1: SQTMH Kabat CDRs(SEQ ID NO: 2513) CDR-L1: KASRDVAIAVA(SEQ ID NO: 2500)CDR-H2: YIYPRDDYPKYNDNFKG(SEQ ID NO: 2514) CDR-L2: WASTRHT(SEQ ID NO: 2501)CDR-H3: PDRSGYAWFIH(SEQ ID NO: 2515) CDR-L3: HQYSSYPFT(SEQ ID NO: 2502)IMGT CDRsCDR-H1: GYTFTSQT IMGT CDRs(SEQ ID NO: 2516) CDR-L1: RDVAIA(SEQ ID NO: 2506)CDR-H2: IYPRDDYP(SEQ ID NO: 2517) CDR-L2: WASCDR-H3: AIPDRS GY AWFIH(SEQ ID NO: 2518) CDR-L3: HQYSSYPFT(SEQ ID NO: 2502)Chothia CDRsCDR-H1: GYTFTSQ Chothia CDRs(SEQ ID NO: 2519) CDR-L1: SRDVAIA(SEQ ID NO: 2510)CDR-H2: YPRDDY(SEQ ID NO: 2520) CDR-L2: WASCDR-H3: DRSGYAWFI(SEQ ID NO: 2521) CDR-L3: YSSYPF(SEQ ID NO: 2511)

[0150] Table 3.1 B. Exemplary heavy and light chain amino acid sequences of anti-IL-23 antibody proteinsAnti-IL-23Heavy chain Light chainantibodyMAb003 QVQLVQSGAEVKKPGSSVKVSCK DIQMTQSPSSLSASVGDRVTITCKASGYTFTSQTMHWMRQAPGQGL ASRDVAIAVAWYQQKPGKVPKLL ACTIVE 717944506v1 94Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 EWIGYIYPRDDYPKYNDNFKGKV IYWASTRHTGVPSRFSGSGSRTDF TITADKSTSTAYMELSSLRSEDTA TLTIS SLQPEDV ADYFCHQYS S YPF VYYCAIPDRSGYAWFIHWGQGTL TFGSGTKLEIKRTVAAPSVFIFPPS VTVSSASTKGPSVFPLAPSSKSTSG DEQLKS GT AS V VCLLNNFYPREA GTAALGCLVKDYFPEPVTVSWNS KVQWKVDNALQSGNSQESVTEQ GALTSGVHTFPAVLQSSGLYSLSS DSKDSTYSLSSTLTLSKADYEKHK VVTVPSSSLGTQTYICNVNHKPSN VYACEVTHQGLSSPVTKSFNRGEC TKVDKKVEPKSCDKTHTCPPCPAP (SEQ ID NO: 2605)EAAGGP S VFLFPPKPKDTLYITREP EVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRV VSVLTVLHQDWLNGKEYKCKVS NKALPAPIEKTISKAKGQPREPQV YTLPPSRDELTKNQVSLTCLVKGF YPSDIAVEWESNGQPENNYKTTPP VLDSDGSFFLYSKLTVDKSRWQQ GNVFSCSVMHEALHNHYTQKSLS LSPGK(SEQ ID NO: 2604)

[0151] In some embodiments, anti-IL-23 antibody comprises a heavy chain variable domain comprises complementarity determining regions CDR-H1, CDR-H2, and CDR-H3 with sequences as shown in a table selected from Table 3C. In some embodiments, anti-IL-23 antibody comprises further comprise a light chain variable domain comprising complementarity determining regions CDR-L1, CDR-L2, and CDR-L3 with sequences as shown in the same table of Table 3C. In some embodiments, anti-IL-23 antibody comprises a heavy chain as shown in Table 3.1C and alight chain as shown in Table 3.1C. In some embodiments, an IL-23 binding protein is means for binding IL-23 with a Fc portion modified to increase half-life in humans compared to that antibody without such modification, e.g., M252Y, S254T, and T256E (YTE) and / or M428L and N434S (LS), for example an increase by a factor of at least two, or at least three, or at least four. In some embodiments the half-life extension modification is the YTE modification. In some embodiments the half-life extension modification is the LS modification.

[0152] Table 3C. Exemplary heavy chain variable domain, light chain variable domain, and complementarity-determining region sequences of anti-IL-23 antibodyAnti-IL-23Heavy chain variable domain Light chain variable domain antibodyClone EVQLLESGGGLVQPGGSLRLSCAA EIVMTQSPATLSVSPGERATLSCK MAb002 SGYTFTDQTIHWVRQAPGKGLEW ASRDVAIAVAWYQQKPGQAPRLL IGYIYPRDDSPKYNENFKGRATLS LFWASTRHTGIPARFSGSGSRTEFT ADNSKNTAYLQMNSLRAEDTAV LTISSLQSEDFAVYYCHQYSSYPFTFGGGTKVEIKACTIVE 717944506v1 95Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 YYC AIPDRS GYAWFIYWGQGTTV (SEQ ID NO: 2523)TVSS(SEQ ID NO: 2522)Kabat CDRsKabat CDRs CDR-L1: KASRDVAIAVACDR-H1: DQTIH (SEQ ID NO: 2500)(SEQ ID NO: 2524)CDR-L2: WASTRHTCDR-H2: YIYPRDDSPKYNENFKG (SEQ ID NO: 2501)(SEQ ID NO: 2525)CDR-L3: HQYSSYPFTCDR-H3: PDRSGYAWFIY (SEQ ID NO: 2502)(SEQ ID NO: 2526)IMGT CDRsIMGT CDRs CDR-L1: RDVAIACDR-H1: GYTFTDQT (SEQ ID NO: 2506)(SEQ ID NO: 2527)CDR-L2: WASCDR-H2: IYPRDDSP(SEQ ID NO: 2528)CDR-L3: HQYSSYPFTCDR-H3: AIPDRSGYAWFIY (SEQ ID NO: 2502)(SEQ ID NO: 2529)Chothia CDRsChothia CDRs CDR-L1: SRDVAIACDR-H1: GYTFTDQ (SEQ ID NO: 2510)(SEQ ID NO: 2530)CDR-H2: YPRDDS CDR-L2: WAS(SEQ ID NO: 2531)CDR-L3: YSSYPFCDR-H3: DRSGYAWFI (SEQ ID NO: 2511)(SEQ ID NO: 2521)

[0153] Table 3.1 C. Exemplary heavy and light chain amino acid sequences of anti-IL-23 antibodyAnti-IL-23Heavy chain Light chainantibodyACTIVE 717944506v1 96Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 MAb002 VQLLESGGGLVQPGGSLRLSCAAS EIVMTQSPATLSVSPGERATLSCK GYTFTDQTIHWVRQAPGKGLEWI ASRDVAIAVAWYQQKPGQAPRLL GYIYPRDDSPKYNENFKGRATLSA LFWASTRHTGIPARFSGSGSRTEFT DNSKNTAYLQMNSLRAEDTAVY LTISSLQSEDFAVYYCHQYSSYPFT YCATPDRSGYAWFIYWGQGTTVT FGGGTKVEIKRTVAAPSVFIFPPSD VSSASTKGPSVFPLAPSSKSTSGGT EQLKS GTAS VVCLLNNFYPREAK AALGCLVKDYFPEPVTVSWNSGA VQWKVDNALQSGNSQESVTEQDS LTSGVHTFPAVLQSSGLYSLSSVV KDSTYSLSSTLTLSKADYEKHKVY TVPSSSLGTQTYICNVNHKPSNTK ACEVTHQGLS SP VTKSFNRGEC VDKKVEPKSCDKTHTCPPCPAPEA (SEQ ID NO: 2607) AGGPSVFLFPPKPKDTLYITREPEV TCVVVDVSHEDPEVKFNWYVDG VEVHNAKTKPREEQYNSTYRVVS VLTVLHQDWLNGKEYKCKVSNK ALPAPIEKTISKAKGQPREPQVYTL PPSRDELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVL DSDGSFFLYSKLTVDKSRWQQGN VFSCSVMHEALHNHYTQKSLSLSP GK(SEQ ID NO: 2606)

[0154] In some embodiments, anti-IL-23 antibody comprises a heavy chain variable domain comprises complementarity determining regions CDR-H1, CDR-H2, and CDR-H3 with sequences as shown in a table selected from Table 3D. In some embodiments, anti-IL-23 antibody comprises further comprise a light chain variable domain comprising complementarity determining regions CDR-L1, CDR-L2, and CDR-L3 with sequences as shown in the same table of Table 3D. In some embodiments, anti-IL-23 antibody comprises a heavy chain as shown in Table 3. ID and a light chain as shown in Table 3. ID. In some embodiments, an IL-23 binding protein is means for binding IL-23 with a Fc portion modified to increase half-life in humans compared to that antibody without such modification, e.g., M252Y, S254T, and T256E (YTE) and / or M428L and N434S (LS), for example an increase by a factor of at least two, or at least three, or at least four. In some embodiments the half-life extension modification is the YTE modification. In some embodiments the half-life extension modification is the LS modification.

[0155] Table 3D. Exemplary heavy chain variable domain, light chain variable domain, and complementarity-determining region sequences of anti-IL-23 antibodyAnti-IL-23Heavy chain variable domain Light chain variable domain antibodyMAb004 QVQLVQSGAEVKKPGSSVKVSCK EIVMTQSPATLSVSPGERATLSCK ASGYTFTAQTMHWMRQAPGQGL ASRDVAIAVAWYQQKPGQAPRLLEWIGYIYPRDGSTKYNENFKGKVT LFWASTRHTGIPARFSGSGSRTEFT ACTIVE 717944506v1 97Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 ITADKSTSTAYMELSSLRSEDTAV LTISSLQSEDFAVYYCHQYSSYPFT YYC AIPDRS GYAWFI V WGQGTLV FGGGTKVEIK TVSS (SEQ ID NO: 2523)(SEQ ID NO: 2532)Kabat CDRs Kabat CDRsCDR-H1: AQTMH CDR-L1: KASRDVAIAVA(SEQ ID NO: 2533) (SEQ ID NO: 2500)CDR-H2: YIYPRDGSTKYNENFKG CDR-L2: WASTRHT (SEQ ID NO: 2498) (SEQ ID NO: 2501)CDR-L3: HQYSSYPFTCDR-H3: PDRSGYAWFIV (SEQ ID NO: 2502)(SEQ ID NO: 2534)IMGT CDRs IMGT CDRsCDR-H1: GYTFTAQT CDR-L1: RDVAIA(SEQ ID NO: 2535) (SEQ ID NO: 2506)CDR-H2: IYPRDGST CDR-L2: WAS(SEQ ID NO: 2504)CDR-H3: AIPDRS GY AWFIV CDR-L3: HQYSSYPFT (SEQ ID NO: 2536) (SEQ ID NO: 2502)Chothia CDRs Chothia CDRsCDR-H1: GYTFTAQ CDR-L1: SRDVAIA(SEQ ID NO: 2537) (SEQ ID NO: 2510)CDR-H2: YPRDGS CDR-L2: WAS(SEQ ID NO: 2508)CDR-H3: DRSGYAWFI CDR-L3: YSSYPF(SEQ ID NO: 2521) (SEQ ID NO: 2511)

[0156] Table 3.1 D. Exemplary heavy and light chain amino acid sequences of anti-IL-23 antibodyAnti-IL-23Heavy chain Light chainantibodyMAb004 FPLAPSSKSTSGGTAALGCLVKDY EIVMTQSPATLSVSPGERATLSCKFPEPVTVSWNSGALTSGVHTFPAV ASRDVAIAVAWYQQKPGQAPRLL ACTIVE 717944506v1 98Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 LQSSGLYSLSSVVTVPSSSLGTQTY LFWASTRHTGIPARFSGSGSRTEFT ICNVNHKPSNTKVDKKVEPKSCD LTISSLQSEDFAVYYCHQYSSYPFT KTHTCPPCPAPEAAGGPSVFLFPP FGGGTKVEIKRTVAAPSVFIFPPSD KPKDTLYITREPEVTCVVVDVSHE EQLKS GTAS VVCLLNNFYPREAK DPEVKFNWYVDGVEVHNAKTKP VQWKVDNALQSGNSQESVTEQDS REEQYNSTYRVVSVLTVLHQDWL KDSTYSLSSTLTLSKADYEKHKVY NGKEYKCKVSNKALPAPIEKTISK ACEVTHQGLS SP VTKSFNRGEC AKGQPREPQVYTLPP SRDELTKNQ (SEQ ID NO: 2603) VSLTCLVKGFYPSDIAVEWESNGQ PENNYKTTPPVLDSDGSFFLYSKL TVDKSRWQQGNVFSCSVMHEAL HNHYTQKSLSLSPGK(SEQ ID NO: 2602)EXEMPLARY EMBODIMENTS

[0157] Embodiment 1. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising: administering to the subject an effective amount of a TL1A inhibitor, wherein administration of the effective amount of the TL1 A inhibitor results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, or a combination thereof, compared to no treatment.

[0158] Embodiment 2. A method for treating skin inflammation and / or skin fibrosis in a subject in need thereof, comprising administering to the subject an effective amount of a TL1A inhibitor, wherein administration of the effective amount of the TL1A inhibitor results in reduction in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, or a combination thereof.

[0159] Embodiment 3. The method of embodiment 1 or embodiment 2, wherein the TL1A inhibitor is an anti-TLl A antibody.

[0160] Embodiment 4. The method of embodiment 3, wherein the anti-TLl A antibody is modified to be half-life extended.

[0161] Embodiment 5. The method of embodiment 3 or embodiment 4, wherein the anti-TLl A antibody comprises a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.1 A. TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE 1.1 B, and TABLE 1.1 C, and (iii) aCDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; b) alight chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to ACTIVE 717944506v1 99Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; and c) a modified Fc that extends half-life of the anti-TLIA antibody as compared to an anti-TLl A antibody that does not comprise the modified Fc.

[0162] Embodiment 6. The method of embodiment 5, wherein the modified Fc comprises M252Y, S254T, and T256E (YTE) according to the EU numbering system.

[0163] Embodiment 7. The method of any one of embodiments 3-6, wherein the anti-TLIA antibody binds TL1A with a dissociation constant (KD) less than about 0.5 nanomolar (nM).

[0164] Embodiment 8. The method of any one of embodiments 3-6, wherein the anti-TLIA antibody binds TL1A with a dissociation constant (KD) less than about 0.4 nanomolar (nM).

[0165] Embodiment 9. The method of any one of embodiments 1-8, wherein treatment with the TL1A inhibitor is as effective as treatment with a TNF inhibitor for treating the inflammatory dermatologic disease.

[0166] Embodiment 10. The method of any one of embodiments 1-8, wherein treatment with the TL1A inhibitor is more effective than treatment with of a TNF inhibitor for treating the inflammatory dermatologic disease.

[0167] Embodiment 11. The method of any one of embodiments 1-8, wherein the effective amount of the TL1 A inhibitor is administered to the subject at disease onset.

[0168] Embodiment 12. The method of any one of embodiments 1-8, wherein the effective amount of the TL1 A inhibitor is administered after onset of symptoms of the inflammatory dermatologic disease.

[0169] Embodiment 13. The method of any one of embodiments 1-12, wherein the subject is a human.

[0170] Embodiment 14. The method of any one of embodiments 1-13, wherein the inflammatory dermatologic disease is eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Erythematosus, alopecia areata, vitiligo or pemphigus.

[0171] Embodiment 15. The method of any one of embodiments 3-14, wherein administration of the effective amount of the anti-TLIA antibody to the subject results in changes of serum cytokines, modulation of fibroblast or fibroblast-like cells, modified histopathology, and / or altered RNA expression in peripheral blood cells and / or skin cells compared to no treatment.

[0172] Embodiment 16. A method for treating inflammatory dermatologic diseases in a subject in need thereof, comprising: administering to the subject an effective amount of an anti-TLIA antibody.ACTIVE 717944506v1 100Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0173] Embodiment 17. The method of embodiment 16, wherein administration of the effective amount of the anti-TLl A antibody results in improvement of inflammation, skin fibrosis, skin barrier disruption, redness, pain, swelling, itching, plaques, rashes, and / or blisters.

[0174] Embodiment 18. The method of embodiment 16, wherein administration of the effective amount of the anti-TLl A antibody treats the inflammatory dermatologic diseases as effectively as TNF inhibitor administration.

[0175] Embodiment 19. The method of embodiment 16, wherein administration of the effective amount of the anti-TLl A antibody treats the inflammatory dermatologic diseases more effectively as TNF inhibitor administration.

[0176] Embodiment 20. The method of any one of embodiments 16-19, wherein the anti-TLIA antibody is modified to be half-life extended antibody.

[0177] Embodiment 21. The method of any one of embodiments 16-20, wherein the subject is a human.

[0178] Embodiment 22. The method of any one of embodiments 16-21, wherein administration of the effective amount of the anti-TLIA antibody to the subject results in changes of serum cytokines, modulation of fibroblast or fibroblast-like cells, modified histopathology, and / or altered RNA expression in peripheral blood cells and / or skin cells compared to no treatment.

[0179] Embodiment 23. The method of any one of embodiments 16-22, wherein the effective amount of the anti-TLIA antibody is administered to the subject at disease onset or after onset of symptoms of an inflammatory dermatologic disease.

[0180] Embodiment 24. The method of any one of embodiments 16-23, wherein administration of the effective amount of the anti-TLIA antibody to the subject results in reduction of TNFa, TL1A, IL-1, IL-4, IL- 5, IL- 6, IL-13, IL-17, and / or INFy.

[0181] Embodiment 25. The method of any one of embodiments 3-24, wherein the effective amount of the anti-TLIA antibody is administered intravenously.

[0182] Embodiment 26. The method of any one of embodiments 3-24, wherein the effective amount of the anti-TLIA antibody is administered subcutaneously.

[0183] Embodiment 27. The method of embodiment 25 or embodiment 26, wherein the anti-TLIA antibody comprises a) a heavy’ chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; b) a light chain variable region (VL) ACTIVE 717944506v1 101Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; and c) a modified Fc that extends half-life of the anti-TLIA antibody as compared to an anti-TLl A antibody that does not comprise the modified Fc.

[0184] Embodiment 28. The method of any one of embodiments 3-27, wherein the anti-TLIA antibody comprises a heavy chain variable region (VH) having an amino acid sequence according to Table 2.1 and a light chain variable region (VL) according to Table 2.1.

[0185] Embodiment 29. The method of any one of embodiments 3-27, wherein the anti-TLIA antibody comprises a heavy chain variable region (VH) having an amino acid sequence according to Table 2.2 and a light chain variable region (VL) according to Table 2.2.

[0186] Embodiment 30. A method of treating inflammatory dermatologic diseases in a subject in need thereof, the method comprising administering subcutaneously an effective amount of a long acting anti-TLIA antibody, wherein subcutaneous administration of the effective amount of the long acting anti-TLIA antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, or reduced lesions, or a combination thereof.

[0187] Embodiment 31. The method of embodiment 30, wherein the inflammatory' dermatologic diseases is selected from the group consisting of eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, and pemphigus.

[0188] Embodiment 32. The method of embodiment 30 or embodiment 31, wherein the anti-TLIA antibody comprises a) a heavy chain variable region (VH) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRH1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) a CDR2 having an amino acid sequence according to any one of CDRH2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any' one of CDRH3 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C; b) a light chain variable region (VL) comprising (i) a CDR1 having an amino acid sequence according to any one of CDRL 1 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, (ii) aCDR2 having an amino acid sequence according to any one of CDRL2 sequences listed in TABLE 1.1 A, TABLE LI B, and TABLE 1.1 C, and (iii) a CDR3 having an amino acid sequence according to any one of CDRL3 sequences listed in TABLE 1.1 A, TABLE 1.1 B, and TABLE 1.1 C; and c) a ACTIVE 717944506v1 102Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 modified Fc that extends half-life of the anti-TLIA antibody as compared to an anti-TLl A antibody that does not comprise the modified Fc.

[0189] Embodiment 33: A method for treating inflammatory dermatologic diseases in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody that binds to a TL1 A trimer to form an antibody-TLl A complex, wherein the antibody-TL1A complex, when comprises 3:1 ratio of the anti-TLIA antibody to the TL1A trimer, exhibits at least 10% faster rate of clearance relative to an antibody-TLIA complex comprising less than 3:1 ratio of the anti-TLIA antibody to the TL1 A trimer.

[0190] Embodiment 34: The method of embodiment 33, wherein the anti-TLIA antibody, upon selectively binding to a TL1 A trimer, decreases rate of dissociation of the TL1A trimer into TL1 A monomer by at least 10% compared to no treatment.

[0191] Embodiment 35: The method of embodiment 34, wherein the anti-TLIA antibody binds an epitope that includes at least 5 amino acid residues selected from VallOl, Arg 103, Gin 104, Thrl05, Thrl07, Hisll8, Glul20, Hisl21, Glul22, Leul23, Argl56, Metl58, Ser234, Tyr238, and Thr239 of a TL1 A polypeptide comprising SEQ ID NO: 2493.

[0192] Embodiment 36: The method of embodiment 33, wherein the anti-TLIA antibody, upon binding to TL1A trimer, increases rate of dissociation of the TL1A trimer into TL1A monomer by at least 10% compared to no treatment.

[0193] Embodiment 37: The method of embodiment 36, wherein the anti-TLIA antibody binds an epitope that includes at least 5 amino acid residues selected from Argl03, Thrl05, Pro 106, Thrl07, Glnl08, Hisl09, Argl56, Asp232, Ile233, Ser234, Leu235. Asp237, Tyr238, Thr239, Lys240, and Glu241 of a TL1 A polypeptide comprising SEQ ID NO: 2493.

[0194] Embodiment 38: Use of a half-life extended anti-TLIA antibody for treating inflammatory’ dermatologic diseases in a subject in need thereof, comprising administering subcutaneously an effective amount of the half-life extended anti-TLIA antibody, wherein subcutaneous administration of the effective amount of the half-life extended anti-TLIA antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, or reduced lesions, or a combination thereof.

[0195] Embodiment 39: Use of a half-life extended anti-TLIA antibody for treating inflammatory dermatologic diseases in a subject in need thereof, comprising administering an effective amount of the half-life extended anti-TLIA antibody, wherein administration of the effective amount of the half-life extended anti-TLIA antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, or reduced lesions, or a combination thereof.ACTIVE 717944506v1 103Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0196] Embodiment 40. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising: administering subcutaneously to the subject an effective amount of a half-life extended anti-TLIA antibody, wherein administration of the effective amount of the half-life extended anti-TLIA antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, improvement in PASI score, or a combination thereof, compared to no treatment.

[0197] Embodiment 41. A method for treating skin inflammation and / or skin fibrosis in a subject in need thereof, comprising administering subcutaneously to the subject an effective amount of a half-life extended anti-TLIA antibody, wherein administration of the effective amount of the half-life extended anti-TLIA antibody results in reduction in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, improvement in PASI score, or a combination thereof.

[0198] Embodiment 42. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising a heavy chain variable region (VH) sequence and a light chain variable region (VL), wherein the VH sequence has at least 95% sequence identity with an amino acid sequence according to any one of the amino acid sequences listed in Table 2.1, and wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1 A (sTLl A) in the subject compared to no treatment, thereby treating the inflammatory’ dermatologic disease.

[0199] Embodiment 43. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising a heavy chain variable region (VH) sequence and a light chain variable region (VL), wherein the VH sequence has at least 95% sequence identity' with an amino acid sequence according to any one of the amino acid sequences listed in Table 2.2, andwherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory' dermatologic disease.

[0200] Embodiment 44. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody, comprising: (a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, and ACTIVE 717944506v1 104Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A; and (c) a modified Fc domain that extends half-life of the anti-TLl A antibody as compared to an anti-TLl A antibody that does not comprise the modified Fc domain, wherein administration of the effective amount of the anti-TLl A antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

[0201] Embodiment 45. A method for treating an inflammatory' dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody, comprising: (a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE LI B, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE LI B, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE LI B;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE LI B,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE LI B, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE LI B; and (c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain, wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

[0202] Embodiment 46. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody, comprising: (a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 C;(b) a light chain variable region (VL) comprising:ACTIVE 717944506v1 105Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 (i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 C,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 C; and (c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain, wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1 A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

[0203] Embodiment 47. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising:(a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 A, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 A;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 A, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 A; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain,ACTIVE 717944506v1 106Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLl A) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

[0204] Embodiment 48. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising:(a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 ammo acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE LI B, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE LI B. and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE LI B;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE LI B, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE LI B, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE LI B; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain,wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLl A) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.ACTIVE 717944506v1 107Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026

[0205] Embodiment 49. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising:(a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 C, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 C:(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 C, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 C; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain,wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLl A) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.EXAMPLES

[0206] The disclosure now being generally described, will be more readily understood by reference to the following examples, which are included merely for purposes of illustration of certain aspects and embodiments of the present disclosure, and is not intended to limit the ACTIVE 717944506v1 108Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 disclosure.EXAMPLE 1. Rat Collagen-Induced Arthritis (CIA) Model to Compare Anti-TLIA Antibody AbX to TNF Inhibitor Positive Control

[0207] Rat CIA models have been widely used as a model of human eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, and pemphigus (RA) and psoriatic arthritis (PsA), as they share joint pathological features of similar to that of RA and PsA.

[0208] The in vivo biological activity of anti-TLl A antibody AbX, a fully human anti-TLIA antibody with LALA and YTE modifications of the Fc region, was evaluated in two versions of a collagen-induced arthritis (CIA) model in rats: the semi-established model and the therapeutic model (FIG. 1). In order to induce arthritis, 6-8 week old female Wistar rats were subcutaneously injected in the tail with 200 pL of a bovine type II collagen emulsion in Freund’s incomplete adjuvant (IF A) on study days 0 and 7. The collagen-IFA emulsion was prepared by dissolving bovine type II collagen in 100 mM acetic acid at 4 mg / mL, mixing with IFA in a 1: 1 (vol / vol) ratio and homogenizing the mixture for 1 hour on ice.

[0209] Binding of AbX to rat TL1 A was evaluated to ensure appropriateness of the rat CIA model. Using surface plasmon resonance (SPR), the following binding values were determined: ka (M-ls-1) of 1.38x105; kd (s-1) of 5.87x10-4; and KD (M) of 4.27x10-9 (FIG. 2). Enteracept has previously been shown to be active in rats as an anti-arthritic agent in the collagen-induced model (Lon, et al., Pharm Res 28:1622-1630 [20-11] doi 10.1007 / s 11095-011-0396-7).

[0210] In the semi-established CIA model, dosing of test articles was started on study day 6 prior to the second injection of collagen and before the beginning of observable symptoms.Anti- TL1A antibody AbX was diluted into phosphate-buffered saline (PBS) and dosed intravenously on study days 6, 13 and 20. The comparator TNF inhibitor, Etanercept, was diluted into PBS and dosed intraperitoneally every' three days starting on day 6 until the end of the study (day 25). Etanercept is a dimeric fusion protein consisting of the extracellular ligandbinding portion of the human 75 kilodalton (p75) tumor necrosis factor receptor (TNFR) linked to the Fc portion of human IgGl.

[0211] In the therapeutic CIA model, dosing of the test articles was started on study day 13 after the rats started showing symptoms of arthritis. Anti-TLIA antibody AbX was diluted into PBS and dosed intravenously on study days 13 and 20. Etanercept was diluted into PBS and dosed intraperitoneally every three days starting on day 13 until the end of the study (day 25).

[0212] Control populations including healthy untreated animals, animals treated with vehicle ACTIVE 717944506v1 109Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 but no active, and animals treated with an isotype-matched (IgGl) nonspecific antibody (RecombiMAb human IgGl isotype control, anti-hen egg lysozyme (BioXCell)) as the same dosing schedules as the test articles.

[0213] The volumes of both hind paws were measured twice per week using plethysmography. Each rat paw was evaluated for disease severity twice per week and was given a score based upon the following observations: score 0 - no arthritis, score 1 - swelling and / or redness of one to two interphalangeal (IP) joints, score 2 - involvement to three to four IP joints or one large joint, score 3 - more than four joints red or swollen, score 4 - severe arthritis of entire paw. The arthritis score is the sum of the scores for all four paws. In the semi-established model, AbX reduced arthritis score better than etanercept (FIG. 3). Both actives showed significant improvement compared to controls (FIG. 3). AbX and etanercept both reduced the arthritis score relative to the vehicle and isotype controls in the therapeutic model, with no difference in arthritis score comparing etanercept monotherapy with AbX monotherapy (FIG.4). Both AbX and enteracept reduced the increase in foot volume relative to vehicle and isotype controls in both models. AbX reduced the increase in foot volume compared to etanercept in the semiestablished model (FIG.5), and there was no difference in foot volume measurement comparing etanercept with AbX in the therapeutic model (Fig. 6).

[0214] Both AbX and etanercept significantly reduced the hind paw x-ray score relative to vehicle and isotype controls in both then semi-established CIA model and the therapeutic CIA model (FIG. 7 and FIG. 8). AbX reduced more the hind paw x-ray score compared to etanercept in the semi-established model (Fig. 7), and there w as no significant difference in hind paw x-ray score comparing etanercept with AbX in the therapeutic model (Fig. 8). AbX significantly reduced the histopathological scores (infiltration of cells (FIG. 9A), pannus severity grade (FIG.9B), cartilage lesion severity grade (FIG. 9C), bone resorption severity grade (FIG. 9D)) relative to the vehicle in the semi-established CIA model. There was not statistical difference in histopathological scores comparing etanercept relative to the vehicle or to the isotype control in the semi-established CIA model. (FIGs. 9A-9D).

[0215] Anti-TLl A antibody Abx treatment reduced disease symptoms and macroscopic and microscopic pathology in the semi-established and therapeutic rat CIA models. Treatment with Abx resulted in superior efficacy relative to etanercept treatment in the semi-established CIA model, and the treatments showed comparable efficacy in the therapeutic CIA model.

[0216] In sum, the data show that anti-TLl A antibody AbX, a fully human anti-TLl A antibody with LALA and YTE modifications of the Fc region, w as effective in treating inflammatory ACTIVE 717944506v1 110Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 dermatologic diseases as demonstrated in two versions of a collagen-induced arthritis (CIA) model in rats: the semi- established model and the therapeutic model. In some instances, AbX was more effective than etanercept.EXAMPLE 2. Treatment of a mouse model of psoriasis using a combination of anti-TLIA antibody and anti-IL-23 antibody

[0217] A method of treating psoriasis using a combination of anti-TLIA antibody and anti-IL-23 antibody was studied in female humanized TL1A / IL23A / IL12B transgenic mice. Briefly, two days before the study (day -2), the transgenic mice had their backs shaved with an electric razor, and the remaining hairs were removed with the application of depilatory cream. On study days 0 to 7, the backs of the mice were smeared with imiquimod (IMQ) cream two times per day.Healthy control mice had their backs smeared with the same amount of petroleum jelly. Mice (n=8 per cohort) were intravenously (IV) injected with 25 mg / kg or 5 mg / kg anti-TLIA antibody or anti -IL-23 antibody on study days -1, 2 and 5. Healthy control and vehicle control mice received IV PBS. A Psoriasis Area and Severity Index (PASI) score, which consisted of measurements for skin erythema, scaling and thickness, was measured each day during the study. On Day 7, mice were euthanized, and skin samples were collected, fixed in formalin and processed for histopathological examination by a blinded pathologist. PASI scores for anti-TLIA antibody / anti-IL-23 antibody for 25 mg / kg or 5 mg / kg are provided in FIG. 10A and FIG. 10B, respectively. Likewise, PASI scores for the combination of anti-TLIA antibody and anti-IL-23 antibody for 25 mg / kg or 5 mg / kg are provided in FIG. 11A and FIG. 11B, respectively.Histopathology scores for anti-TLIA antibody / anti-IL-23 antibody for 25 mg / kg or 5 mg / kg are provided in FIG. 12A. Likewise, histopathology scores for the combination of anti-TLIA antibody and anti-IL-23 antibody for 25 mg / kg and 5 mg / kg are provided in FIG. 12B and FIG.12C, respectively.EXAMPLE 3. Treatment of a model of psoriasis using an anti-TLIA antibody

[0218] A method of treating psoriasis using an anti-TLIA antibody is studied in female humanized TL1A transgenic mice. Briefly, two days before the study (day -2), the transgenic mice have their backs shaved with an electric razor, and the remaining hairs are removed with the application of depilatory cream. On study days 0 to 7, the backs of the mice are smeared with imiquimod (IMQ) cream two times per day. Healthy control mice have their backs smeared with the same amount of petroleum jelly. Mice (n=8 per cohort) are intravenously (IV) injected with 25 mg / kg or 5 mg / kg anti-TLIA antibody on study days -1, 2 and 5. Healthy ACTIVE 717944506v1 111Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 control and vehicle control mice receives IV PBS. A Psoriasis Area and Severity Index (PASI) score, which consisted of measurements for skin erythema, scaling and thickness, is measured each day during the study. On Day 7, mice are euthanized, and skin samples are collected, fixed in formalin and processed for histopathological examination by a blinded pathologist. PASI scores for anti-TLIA antibody for 25 mg / kg or 5 mg / kg are determined. The anti-TLIA antibody treatment is expected to improve PASI75 and / or PASI90 scores.EXAMPLE 4. Modelling for dose selection of anti-TLIA antibody for treating inflammatory dermatologic disease

[0219] PK simulations for three regimens were generated for treating inflammatory dermatologic disease using the anti-TLIA antibody. The three regimens are summarized in Table 4.Table 4. Proposed regimens for treating inflammatory dermatologic disease using the anti-TLIA antibodyInduction Phase Maintenance PhaseRegimen 1 Wk 0, 4, and 8 Wk 12,36Regimen 2 Wk O Wk 12,36Regimen 3 Wk 0; wk 4 and 8 (50% of wk 0) Wk 12.36

[0220] The results were generated for reducing soluble TL1A level from 500 pg / mL in serum (baseline) to 100 pg / mL after week 12. The projected PK parameters are summarized in Table 5.Table 5. Pop PK Pop PK-PD Projected inflammatory dermatologic disease treatmentwkl2 wk36Serum sTLIA Tissue sTLIA Serum sTLIA Tissue sTLIA Regimen 1 100 100 91 89 Regimen 2 77 73 74 71Regimen 3 98 98 84 83

[0221] Projected Ctrough values for regimen 1, 2 and 3 at week 12 are expected to be 118, 25.1 and 73.3, respectively. Likewise, projected Ctrough values for regimen 1, 2 and 3 at week 36 are expected to be 7.6, 3.9 and 6.3, respectively.

[0222] Based on the analysis it was projected that Regimen 1 can achieve >90% target suppression in serum and in tissue in nearly all subjects during induction phase and in ~ 90% of subject during maintenance phase. The safety margin was projected to be about 1 for AUC0-12w. Likewise, Regimen 2 can achieve >90% target suppression in serum and in tissue in nearly all ACTIVE 717944506v1 112Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 subjects during induction phase and in at least 70% of subject during maintenance phase. The safety margin was projected to be about 2.4 for AUC0-12w.EXAMPLE 5. PK Modelling for anti-TLIA antibody for treating inflammatory dermatologic disease

[0223] To estimate human exposures to Antibody 63, a population PK model using Antibody 63 was developed based on interim data. The final model was a 2-compartment model with first-order absorption from the SC injection site and a first-order elimination from the central compartment. For atypical participant, the estimated CL with Antibody 63 was 70.4 mL / d (3 to 4-fold lower than the typical therapeutic IgG, half-life was -45.5 days [individual participant range 31.5 to 64.5 days], which is ~2-fold longer than the typical therapeutic IgG) and F was -60.2% (individual participant range 44.8% to 80.1%). Population Pharmacokinetics-Predicted Exposures in Humans (Median and 2.5-97.5th Percentile) are summarized in Table 6.Table 6. Estimated human exposures at the proposed dose regimens Median (2.5, 97.5 percentiles)AUC AUC Ctrough Ctrough Simulated Cm ax W12 W16 W12 / 16 W 36 / 40 Groups (gg / ml) (daygg / mL) (dayug / ml.) ug / mL jig / mL Healthy Participants (Day 1)621 15600 17500Group 1 (11800, (12700, 23300) NC NC (475, 791) 19700)412 10400 11700Group 2( (8270, 15300) NC NC (313, 542) 7700, 13000)34.1 20701810Group 3 (17.8, (1070, 3250) NC NC (949, 2760)54.3)Inflammatory dermatologic disease Participants - Primary Efficacy (Week 12)Group 4 88.6 19.54900 65Weeks 0, 4, 8; (43.7, NC (6.13,(2490. 7390) (31.7, 101)Weeks 12, 24, 36 136) 42.5) Group 5 44.1 3.112210 11.7Week 0; (22.3, NC (0.515.(1100, 3220) (4.34, 22.2)Weeks 12, 36 74.3) 10.8)AUC=area under the concentration-time curve from 0 to 12 or 16 weeks (AUC12 and AUC16); Cmax=maximum observed concentration; Ctrough=concentration trough (pre-dose); NC=not calculated; W=weekNote: Simulations were conducted for 1000 healthy participants and 2000 patients per regimen. ACTIVE 717944506v1 113Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 Note: Assumed that clearance was 15% higher for participants compared to healthy participants Note: Week 0=Day 1, Baseline (first dose of investigational product)EXAMPLE 6. Population PK-PD Modeling and Simulations

[0224] To support dosing of Antibody 63, a population PK-PD model was built using PK and PD data from the interim analysis. The sequential fitting method was used, with population PK parameters estimated as described in Example 5.

[0225] A population PK-PD antibody-antigen binding model was developed to describe the increase of serum total sTLl A following Antibody 63 administration. The Ab-Ag binding parameters were fixed based on measured value as described in Table 7.Table 7. Antibody 63 Binding Kinetics and Affinity to Human TL1A Method ka (1 / Ms) kd (1 / s) KD(M) Multi-cycle kinetics 1.7 x 1067.3 x 10-54.2 x 10’11Single-cycle kinetics 2.2 x 1064.3 x 10-51.9 x 10’11Average 2.0 x 1065.8 x 10’53.1 x 10’11Abbreviations: ka=association constant; kd=dissociation constant; KD= equilibrium dissociation constant between the antibody and its antigen

[0226] All other PD parameters were estimated. The population PK-PD model adequately captured the observed total sTLl A profiles in healthy participants and supported the notion that an increase in total soluble TL1A is attributed to longer apparent half-life of Ab-Ag complexes (11 days for a typical patient) compared to free sTLl A (~1 hour).

[0227] The population PK-PD model was used to predict the systemic and tissue exposure and free sTLIA. Specifically, for each dosing regimen, PK and PD endpoints were simulated for 2000 virtual subjects. The baseline sTLIA in serum and tissue of patients were assumed to be -500 pg / mL during induction and -100 pg / mL during the Extension Period (i.e., the rate of sTLIA production was assumed to be 5-fold lower compared to induction and equivalent to that in healthy levels, as measured with total sTLA1 assay in placebo participants (Table provided in Example 5). The serum to tissue partition coefficient for the antibody was assumed to be 0.35. The clearance of Antibody 63 was assumed to be 15% higher compared to healthy participants, as reported for mAbs in autoimmune conditions. The model-based predictions are shown in FIGS. 13A, 13B, 14A and 14B

[0228] Based on these simulations, Dosing Regimen 1 is projected to achieve >90% target suppression in serum and tissue in most participants at the primary efficacy endpoint (Week 12)ACTIVE 717944506v1 114Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 and in ~70 to 90% of participants during the Extension Period. Nearly all participants are projected to achieve 80% target suppression throughout the Extension Period.

[0229] Based on these simulations, Dosing Regimen 2 is projected to achieve >80% target suppression in serum and tissue in ~70 to 90% of the participants at the primary efficacy endpoint (Week 12) and throughout the Extension Period.INCORPORATION BY REFERENCE

[0230] All publications and patents cited throughout the text of this specification (including all patents, patent applications, scientific publications, manufacturer's specifications, instructions, etc. ), whether supra or infra, are hereby incorporated by reference in their entirety for all purposes. To the extent the material incorporated by reference contradicts or is inconsistent with this specification, the specification will supersede any such material.EQUIVALENTS

[0231] The disclosure may be embodied in other specific forms without departing from the spirit or essential characteristics thereof. The foregoing embodiments are therefore to be considered in all respects illustrative rather than limiting the disclosure described herein. Scope of the disclosure is thus indicated by the appended claims rather than by the foregoing description, and all changes that come within the meaning and range of equivalency of the claims are intended to be embraced therein.ACTIVE 717944506v1 115

Claims

Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 CLAIMSWhat is claimed is:

1. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody, comprising: (a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A; and (c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain, wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

2. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody, comprising: (a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE LI B, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE LI B, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE LI B;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE LI B,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE LI B, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE LI B; and (c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain, wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating ACTIVE 717944506v1 116Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 the inflammatory dermatologic disease.

3. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody, comprising: (a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 C;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 C,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 C, and (iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 C; and (c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain, wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

4. A method for treating an inflammatory' dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising:(a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 A.(ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 A, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 A;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 A, or ACTIVE 717944506v1 117Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 A, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 A, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 A; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain,wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

5. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising:(a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE LI B.(ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE LI B, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE LI B;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE LI B, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared ACTIVE 717944506v1 118Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 to a corresponding CDRL2 sequences listed in TABLE 1.1 B, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE LI B; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain,wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLl A) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

6. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering to the subject an effective amount of an anti-TLIA antibody comprising:(a) a heavy chain variable region (VH) comprising:(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 C, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 C;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 C, (ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 C, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 C; andACTIVE 717944506v1 119Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 (c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain.wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1 A (sTLl A) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

7. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody comprising a heavy chain variable region (VH) sequence and a light chain variable region (VL), wherein the VH sequence has at least 95% sequence identity with an amino acid sequence according to any one of the amino acid sequences listed in Table 2.1.wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1 A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

8. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering to the subject an effective amount of an anti-TLIA antibody comprising a heavy chain variable region (VH) sequence and a light chain variable region (VL), wherein the VH sequence has at least 95% sequence identity with an amino acid sequence according to any one of the amino acid sequences listed in Table 2.2,wherein administration of the effective amount of the anti-TLIA antibody reduces an amount of free soluble TL1A (sTLIA) in the subject compared to no treatment, thereby treating the inflammatory dermatologic disease.

9. The method of any one of claims 1-8, wherein administration of the effective amount of the anti-TLIA antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, improvement in PASI score, or a combination thereof, compared to no treatment.

10. The method of any one of claims 1-9. wherein the effective amount of the anti-TLIA antibody is administered intravenously.ACTIVE 717944506v1 120Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 11. The method of any one of claims 1-9, wherein the effective amount of the anti-TLIA antibody is administered subcutaneously.

12. A method for treating an inflammatory dermatologic disease in a subject in need thereof, comprising:administering subcutaneously to the subject an effective amount of a half-life extended anti-TLIA antibody, wherein administration of the effective amount of the half-life extended anti-TLIA antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, improvement in PASI score, or a combination thereof, compared to no treatment.

13. A method for treating skin inflammation and / or skin fibrosis in a subject in need thereof, comprising:administering subcutaneously to the subject an effective amount of a half-life extended anti-TLIA antibody, wherein administration of the effective amount of the half-life extended anti-TLIA antibody results in reduction in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, improvement in PASI score, or a combination thereof.

14. The method of claim 13, wherein the effective amount of the extended half-life anti-TLIA antibody is administered to the subject every 3 months (Q3M) or every 6 months (Q6M).

15. The method of any one of claims 12-13, wherein the anti-TLIA antibody comprises:(a) a heavy chain variable region (VH) comprising(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 A,(ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 A, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 A;(b) a light chain variable region (VL) comprising:ACTIVE 717944506v1 121Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 (i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL 1 sequences listed in TABLE 1.1 A,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 A, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 A, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 A; and(c) a modified Fc domain that extends half-life of the anti-TLl A antibody as compared to an anti-TLl A antibody that does not comprise the modified Fc domain.

16. The method of any one of claims 12-13, wherein the anti-TLIA antibody comprises:(a) a heavy chain variable region (VH) comprising(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE LI B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 B.(ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE LI B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE LI B, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE LI B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE LI B;(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE LI B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 B,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE LI B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE LI B, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE LI B, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE LI B; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an ACTIVE 717944506v1 122Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 anti-TLl A antibody that does not comprise the modified Fc domain.

17. The method of any one of claims 12-13, wherein the anti-TLIA antibody comprises:(a) a heavy chain variable region (VH) comprising(i) a CDR1 comprising any one of CDRH1 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH1 sequences listed in TABLE 1.1 C,(ii) a CDR2 comprising any one of CDRH2 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH2 sequences listed in TABLE 1.1 C, and(iii) a CDR3 comprising any one of CDRH3 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRH3 sequences listed in TABLE 1.1 C:(b) a light chain variable region (VL) comprising:(i) a CDR1 comprising any one of CDRL1 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL1 sequences listed in TABLE 1.1 C,(ii) a CDR2 comprising any one of CDRL2 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL2 sequences listed in TABLE 1.1 C, and(iii) a CDR3 comprising any one of CDRL3 sequences listed in TABLE 1.1 C, or a variant thereof that comprises 1 to 2 amino acid modifications as compared to a corresponding CDRL3 sequences listed in TABLE 1.1 C; and(c) a modified Fc domain that extends half-life of the anti-TLIA antibody as compared to an anti-TLIA antibody that does not comprise the modified Fc domain.

18. The method of any one of claims 1-6 and claims 15-17, wherein the modified Fc domain comprises M252Y, S254T, and T256E (YTE) according to EU numbering system.

19. The method of any one of claims 1-18, wherein the anti-TLIA antibody binds TL1 A with a dissociation constant (KD) less than about 0.5 nanomolar (nM).

20. The method of any one of claims 1-18, wherein the anti-TLIA antibody binds TL1A with a dissociation constant (KD) less than about 0.4 nanomolar (nM).ACTIVE 717944506v1 123Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 202621. The method of any one of claims 1-20, wherein treatment with the anti-TLl A antibody is as effective as treatment with a TNF inhibitor for treating the inflammatory dermatologic disease22. The method of any one of claims 1-21, wherein treatment with the anti-TLl A antibody is more effective than treatment with a TNF inhibitor for treating the inflammatory dermatologic disease.

23. The method of any one of claims 1-22, wherein the effective amount of the anti-TLl A antibody is administered to the subject at disease onset.

24. The method of any one of claims 1-22. wherein the effective amount of the anti-TLl A antibody is administered after onset of symptoms of the inflammatory dermatologic disease.

25. The method of any one of claims 1-24, wherein the subject is a human.

26. The method of any one of claims 1-25, wherein the inflammatory dermatologic disease is eczema, psoriasis, psoriasis vulgaris, scleroderma, dermatomyositis, hidradenitis suppurativa, Cutaneous Lupus Ery thematosus, alopecia areata, vitiligo or pemphigus.

27. The method of any one of claims 1-26, wherein administration of the effective amount of the anti-TLl A antibody to the subject results in changes of serum cytokines, modulation of fibroblast or fibroblast-like cells, modified histopathology, and / or altered RNA expression in peripheral blood cells and / or skin cells compared to no treatment.

28. The method of claim 1-27, wherein administration of the effective amount of the anti-TLl A antibody to the subject results in reduction of TNFa, TL1A, IL-1, IL-4, IL- 5, IL- 6, IL-13, IL-17, and / or INFy.

29. The method of any one of claims 1-28, wherein administration of the effective amount of the anti-TLl A antibody results in improvement of inflammation, skin fibrosis, skin barrier disruption, redness, pain, swelling, itching, plaques, rashes, and / or blisters.

30. Use of a half-life extended anti-TLl A antibody for treating an inflammatory dermatologic disease in a subject in need thereof, comprising administering subcutaneously an effective ACTIVE 717944506v1 124Attorney Docket No.: 220703-011801 / PCT Electronically Filed: January 11, 2026 amount of the half-life extended anti-TLl A antibody, wherein subcutaneous administration of the effective amount of the half-life extended anti-TLl A antibody results in improvement in inflammation, skin fibrosis, greater skin barrier, reduced redness, reduced pain, reduced swelling, reduced itching, reduced lesions, improvement in PASI score, or a combination thereof, compared to no treatment.ACTIVE 717944506v1 125

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