EP4792139A1 - Biomarkers for eribulin-based antibody-drug conjugates and methods of use - Google Patents

Biomarkers for eribulin-based antibody-drug conjugates and methods of use

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Publication number
EP4792139A1
EP4792139A1 EP24799728.1A EP24799728A EP4792139A1 EP 4792139 A1 EP4792139 A1 EP 4792139A1 EP 24799728 A EP24799728 A EP 24799728A EP 4792139 A1 EP4792139 A1 EP 4792139A1
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seq
level
cancer
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antibody
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French (fr)
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Yan Jane ZHANG
Keiji FURUUCHI
Toshimitsu Uenaka
Xin Cheng
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Eisai R&D Management Co Ltd
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Eisai R&D Management Co Ltd
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Abstract

Biomarkers and methods of using them in treating folate receptor alpha-expressing cancers, such as platinum resistant ovarian cancer, are disclosed herein.

Description

Finngean Reference: 15648.0053-00304 BIOMARKERS FOR ERIBULIN-BASED ANTIBODY-DRUG CONJUGATES AND METHODS OF USE BACKGROUND AND SUMMARY OF THE INVENTION [0001] This application claims the benefit of priority of U.S. Provisional Application No. 63/590,173, filed October 13, 2023, the contents of which are incorporated herein by reference in its entirety. [0002] The present disclosure relates to biomarkers and methods of treating a folate receptor alpha (FRA)-expressing cancer using an antibody drug conjugate (ADC) that binds folate receptor alpha and provides anti-tubulin drug activity. [0003] Cancer is among the leading causes of morbidity and mortality worldwide, with approximately 10 million cancer-related deaths in 2020. The most common causes of cancer death are cancers of: lung (1.8 million deaths); colon and rectum (916,000), liver (830,000 deaths); stomach (769,000 deaths); and breast (685,000 deaths). Additionally, about 207,000 women died from ovarian cancer in 2020. The number of new cancer cases is expected to rise by about 70% over the next two decades, to approximately 22 million new cancer cases per year (World Cancer Report 2014). [0004] Microtubules are dynamic filamentous cytoskeletal proteins that are involved in a variety of cellular functions, including intracellular migration and transport, cell signaling, and the maintenance of cell shape. Microtubules also play a critical role in mitotic cell division by forming the mitotic spindle required to segregate chromosomes into two daughter cells. The biological functions of microtubules in all cells are regulated in large part by their polymerization dynamics, which occurs by the reversible, non-covalent addition of α and β tubulin dimers at both ends of microtubules. This dynamic behavior and resulting control over microtubule length is vital to the proper functioning of the mitotic spindle. Even minor alteration of microtubule dynamics can engage the spindle checkpoint, arrest cell cycle progression at mitosis, and subsequently lead to cell death (Mukhtar et al. (2014) Mol. Cancer Ther.13:275-84). Due to their rapid cell division, cancer cells are generally more sensitive to compounds that bind to tubulin and disrupt its normal function, as compared to normal cells. For this reason, tubulin inhibitors and other microtubule-targeted agents have become a promising class of drugs for the treatment of cancer (Dumontet and Jordan (2010) Nat. Rev. Drug Discov.9:790-803). [0005] Folate receptor alpha (FRA) is a glycophosphatidylinositol (GPI)-linked membrane protein that binds folate. While the role of FRA in the biology of normal and cancerous tissue is not fully understood, it is highly over-expressed on a high percentage of ovarian cancers of epithelial origin (O'Shannessy et al. (2013) Int. J. Gynecol. Pathol.32(3):258-68), as well as in a percentage of non- small cell lung carcinomas (Christoph et al. (2014) Clin. Lung Cancer 15(5):320-30). FRA also has limited expression in normal tissues. These properties make FRA an attractive target for cancer immunotherapy. Finngean Reference: 15648.0053-00304 [0006] Effective treatment of a folate receptor alpha (FRA)-expressing cancer has previously been demonstrated using compounds, e.g., ADCs, with biological activity against FRA-expressing tumor cells, e.g., an anti-FRA ADC, e.g., MORAb-202, also referred to as farletuzumab ecteribulin (FZEC). MORAb-202 has also been shown to be an effective treatment of FRA-expressing cancer when dosed based on body surface area, as disclosed in PCT/US2023/018214, which is incorporated herein by reference in its entiry. There remains a need, however, for more refined methods and dosing regimens for treating subjects having an FRA-expressing cancer with an anti-FRA ADC, e.g., MORAb-202, e.g., to reduce side effects of treatment and/or to ensure treatment is better targeted to those responding to the ADC therapy. [0007] In various embodiments, the present disclosure provides a method of treating a folate receptor alpha (FRA)-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to a subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen-binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8, (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) administering a further dose of the antibody-drug conjugate if a change in the level is detected. [0008] In some embodiments, the present disclosure provides a method of reducing risk of interstitial lung disease (ILD) in a subject being treated for an FRA-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to the subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) Finngean Reference: 15648.0053-00304 wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen-binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8. (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) administering a further dose of the antibody-drug conjugate if a change in the level is detected. [0009] In some embodiments, the level of surfactant protein D (SP-D) in a sample taken from the subject after administration is increased relative to the level of SP-D in the baseline sample. In some embodiments, the level of SP-D is increased at least 100% relative to the level of SP-D in the baseline sample. In some embodiments, the level of kallikrein related peptidase 7 (KLK-7) in a sample taken from the subject after administration is reduced relative to the level of KLK-7 in the baseline sample. In some embodiments, the level of KLK-7 is reduced at least 30% relative to the level of KLK-7 in the baseline sample. In some embodiments, the level of monocyte chemoattractant protein-1 (MCP-1) in a sample taken from the subject after administration is reduced relative to the level of MCP-1 in the baseline sample. In some embodiments, the level of MCP-1 is reduced at least 15% relative to the level of MCP-1 in the baseline sample. In some embodiments, the level of angiopoietin 2 (ANG-2) in a sample taken from the subject after administration is reduced relative to the level of ANG-2 in the baseline sample. In some embodiments, the level of ANG-2 is reduced at least 30% relative to the level of ANG-2 in the baseline sample. In some embodiments, the level of kallikrein related peptidase 5 (KLK-5) in a sample taken from the subject after administration is reduced relative to the level of KLK-5 in the baseline sample. In some embodiments, the level of KLK-5 is reduced at least 40% relative to the level of KLK-5 in the baseline sample. In some embodiments, the level of matrix metalloproteinase 12 (MMP12) in a sample taken from the subject after administration is reduced relative to the level of MMP12 in the baseline sample. In some embodiments, the level of MMP12 is reduced at least 40% relative to the level of MMP12 in the baseline sample. In some embodiments, the level of ferritin (FRTN) in a sample taken from the subject after administration is reduced relative Finngean Reference: 15648.0053-00304 to the level of FRTN in the baseline sample. In some embodiments, the level of FRTN is reduced at least 40% relative to the level of FRTN in the baseline sample. In some embodiments, the level of insulin like growth factor binding protein 2 (IGFBP-2) in a sample taken from the subject after administration is reduced relative to the level of IGFBP-2 in the baseline sample. In some embodiments, the level of IGFBP-2 is reduced at least 30% relative to the level of IGFBP-2 in the baseline sample. [0010] In some embodiments, the present disclosure provides a method of treating a folate receptor alpha (FRA)-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to a subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen-binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8, (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) administering a further dose of the antibody-drug conjugate if a change in the level is not detected, wherein the biomarker is one or more of IGFBP-1, FLT3L, and VEGF-D. In some embodiments, the biomarker of tumor response is insulin like growth factor binding protein 1 (IGFBP-1). In some embodiments, the biomarker of tumor response is fms related receptor tyrosine kinase 3 ligand (FLT3LG). In some embodiments, the biomarker of tumor response is vascular endothelial growth factor D (VEGF-D). [0011] In some embodiments, the present disclosure provides a method of treating a folate receptor alpha (FRA)-expressing cancer, comprising Finngean Reference: 15648.0053-00304 (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to a subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen-binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8, (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) determining the efficacy of the antibody-drug conjugate based on a level change in the one or more biomarkers of tumor response. [0012] In some embodiments, the antibody or antigen-binding fragment comprises a heavy chain comprising an amino acid sequence of SEQ ID NO: 15, and a light chain comprising an amino acid sequence of SEQ ID NO: 16. In some embodiments, the antibody-drug conjugate is MORAb-202. In some embodiments, p is from 3 to 5. [0013] In some embodiments, the dose is 8 mg to 44 mg per m2 of the subject’s BSA. In some embodiments, the dose is 0.3 mg/kg to 1.2 mg/kg of the subject’s bodyweight. In some embodiments, the antibody-drug conjugate is administered once every three weeks. In some embodiments, the antibody-drug conjugate is administered once every two weeks. In some embodiments, the antibody- drug conjugate is administered once per week. In some embodiments, the method further comprising administering a corticosteroid. In some embodiments, the antibody-drug conjugate is administered intravenously. [0014] In some embodiments, the FRA-expressing cancer is selected from: gastric cancer, ovarian cancer, serous ovarian cancer, serous high-grade ovarian cancer, clear cell ovarian cancer, platinum resistant ovarian cancer, lung cancer, non-small cell lung cancer, metastatic non-small cell lung cancer, lung carcinoid, colorectal cancer, breast cancer, triple negative breast cancer, hormone Finngean Reference: 15648.0053-00304 receptor (HR)-positive and HER2-low breast cancer, endometrial cancer, serous endometrial carcinoma, peritoneal cancer, primary peritoneal cancer, fallopian tube cancer, pancreatic cancer, kidney cancer, renal cell cancer, cervical cancer, esophageal cancer, osteosarcoma, chorid plexus carcinoma ependymoma, epedymoblastoma, medulloblastoma, Wilms tumor, acute myeloid leukemia, and head and neck cancer. In some embodiments, the FRA-expressing cancer is ovarian cancer. In some embodiments, the ovarian cancer is platinum resistant ovarian cancer (PROC). In some embodiments, the FRA-expressing cancer is a refractory cancer. In some embodiments, the refractory cancer is non-responsive to a targeted treatment. In some embodiments, the targeted treatment is a targeted treatment against any one of the following genes or variants thereof: EGFR, ALK, BRAF, RET, MET, NTRK, and ROS1.In some embodiments, the refractory cancer is non- responsive to a platinum-based treatment and an immunotherapy-based treatment, wherein the treatments are administered concurrently or sequentially. In some embodiments, the platinum-based treatment is a platinum-doublet chemotherapy, and wherein the immunotherapy-based treatment is a PD-1 inhibitor or a PD-L1 inhibitor. In some embodiments, the subject at the start of treatment does not have one or more of: interstitial lung disease (ILD) and/or pneumonitis, a history of ILD and/or pneumonitis, a lung-specific clinically significant illness, pleural effusion, pericardial effusion, prior pneumonectomy, a history of chest radiotherapy within the past 2 years, autoimmune disorder with pulmonary involvement, connective tissue disorder with pulmonary involvement, or inflammatory disorder with pulmonary involvement. In some embodiments, the subject does not have one or more of: a history of more than three prior therapies for the FRA-expressing cancer, a high neutrophil-to- lymphocyte ratio, or a serum albumin level at the start of treatment of less than 3 g/dL. BRIEF DESCRIPTION OF THE DRAWINGS Fig.1 shows a biomarker study design. C#: dosing cycle after first administration, e.g., every three week period; D#: day after most recent administration; FZEC: farletuzumab ecteribulin; IV: intravenous; MoA: mechanism of action; Q3W: every three weeks. [0015] Fig.2 shows changes in certain biomarker levels in responders (blue) and nonresponders (purple) in the MORAb-202 combined cohort. C#: cycle #; D#: day #. [0016] Fig.3 shows the change in certain biomarker levels in responders (blue) and nonresponders (purple) in the MORAb-2020.9 mg/kg cohort. C#: cycle #; D#: day #. [0017] Fig.4 shows the cytotoxic and potential noncytotoxic bystander effects of MORAb-202 administration. ECM: extracellular matrix; EMT: epithelial-mesenchymal transition; FRα: folate receptor-alpha; FZEC: farletuzumab ecteribulin; MET: mesenchymal-epithelial transition. DETAILED DESCRIPTION [0018] The disclosed methods may be understood more readily by reference to the following detailed description taken in connection with the accompanying figures, which form a part of this disclosure. It is to be understood that the disclosure is not limited to the specific methods disclosed Finngean Reference: 15648.0053-00304 and/or shown herein, and that the terminology used herein is for the purpose of disclosing particular embodiments by way of example only and is not intended to be limiting of the claimed methods. [0019] Throughout this text, the descriptions refer to methods of using compositions, e.g., an anti- FRA ADC, e.g., MORAb-202. Where the disclosure describes or claims a feature or embodiment associated with a method of using said compositions, such a feature or embodiment is equally applicable to the composition. [0020] When a range of values is expressed, it includes embodiments using any particular value within the range. Further, reference to values stated in ranges includes each and every value within that range. All ranges are inclusive of their endpoints and combinable. When values are expressed as approximations, by use of the antecedent “about,” it will be understood that the particular value forms another embodiment. Reference to a particular numerical value includes at least that particular value, unless the context clearly dictates otherwise. The use of “or” will mean “and/or” unless the specific context of its use dictates otherwise. All references cited herein are incorporated by reference for any purpose. Where a reference and the specification conflict, the specification will control. [0021] It is to be appreciated that certain features of the disclosed methods, which are, for clarity, disclosed herein in the context of separate embodiments, may also be provided in combination in a single embodiment. Conversely, various features of the disclosed methods that are, for brevity, disclosed in the context of a single embodiment, may also be provided separately or in any subcombination. [0022] Various terms relating to aspects of the description are used throughout the specification and claims. Such terms are to be given their ordinary meaning in the art unless otherwise indicated. Other specifically defined terms are to be construed in a manner consistent with the definitions provided herein. [0023] As used herein, the singular forms “a,” “an,” and “the” include plural forms unless the context clearly dictates otherwise. [0024] The terms "about" or "approximately" in the context of numerical values and ranges refers to values or ranges that approximate or are close to the recited values or ranges such that the embodiment may perform as intended, such as having a desired amount of nucleic acids or polypeptides in a reaction mixture, as is apparent to the skilled person from the teachings contained herein. This is due, at least in part, to the varying properties of nucleic acid compositions, age, race, gender, anatomical and physiological variations and the inexactitude of biological systems. Thus, these terms encompass values beyond those resulting from systematic error. It should be understood that this definition of “about” applies to the entirety of the present disclosure, unless otherwise specified in certain contexts, e.g., in descriptions of average number of drug moieties per individual antibody moiety or within a mixture of ADCs. [0025] The term “agent” is used herein to refer to a chemical compound, a mixture of chemical compounds, a biological macromolecule, an extract made from biological materials or a combination Finngean Reference: 15648.0053-00304 thereof. The term “therapeutic agent,” “drug,” or “drug moiety” refers to an agent that is capable of modulating a biological process and/or has biological activity. [0026] The term "antibody" is used in the broadest sense to refer to an immunoglobulin molecule that recognizes and specifically binds to a target, such as a protein, polypeptide, carbohydrate, polynucleotide, lipid, or combinations of the foregoing through at least one antigen recognition site within the variable region of the immunoglobulin molecule. The heavy chain of an antibody comprises a heavy chain variable domain (VH) and a heavy chain constant region (CH). The light chain comprises a light chain variable domain (VL) and a light chain constant domain (CL). For the purposes of this application, the mature heavy chain and light chain variable domains each comprises three complementarity determining regions (CDR1, CDR2 and CDR3) within four framework regions (FR1, FR2, FR3 and FR4) arranged from N-terminus to C-terminus: FR1, CDR1, FR2, CDR2, FR3, CDR3 and FR4. An "antibody" can be naturally occurring or man-made, such as monoclonal antibodies produced by conventional hybridoma technology. The term “antibody” includes full- length monoclonal antibodies and full-length polyclonal antibodies, as well as antibody fragments such as Fab, Fab’, F(ab’)2, Fv, and single chain antibodies. An antibody can be any one of the five major classes of immunoglobulins: IgA, IgD, IgE, IgG, and IgM, or subclasses thereof (e.g., isotypes IgG1, IgG2, IgG3, IgG4). The term further encompasses human antibodies, chimeric antibodies, humanized antibodies and any modified immunoglobulin molecule containing an antigen recognition site, so long as it demonstrates the desired biological activity. [0027] The term “chimeric antibody,” as used herein, refers to antibodies wherein the amino acid sequence of the immunoglobulin molecule is derived from two or more species. In some instances, the variable regions of both heavy and light chains corresponds to the variable regions of antibodies derived from one species with the desired specificity, affinity, and activity while the constant regions are homologous to antibodies derived from another species (e.g., human) to minimize an immune response in the latter species. [0028] The term “human antibody,” as used herein, refers an antibody produced by a human or an antibody having an amino acid sequence of an antibody produced by a human. [0029] As used herein, the term "humanized antibody" refers to forms of antibodies that contain sequences from non-human (e.g., murine) antibodies as well as human antibodies. Such antibodies are chimeric antibodies which contain minimal sequence derived from non-human immunoglobulin. In general, the humanized antibody will comprise substantially all of at least one, and typically two, variable domains, in which all or substantially all of the hypervariable loops correspond to those of a non-human immunoglobulin and all or substantially all of the framework (FR) regions are those of a human immunoglobulin sequence. The humanized antibody optionally also will comprise at least a portion of an immunoglobulin constant region (Fc), typically that of a human immunoglobulin. The humanized antibody can be further modified by the substitution of residues, either in the Fv Finngean Reference: 15648.0053-00304 framework region and/or within the replaced non-human residues to refine and optimize antibody specificity, affinity, and/or activity. [0030] The term "monoclonal antibody," as used herein, refers to an antibody obtained from a population of substantially homogeneous antibodies, i.e., the individual antibodies comprising the population are identical except for possible naturally occurring mutations that may be present in minor amounts. Monoclonal antibodies are highly specific, being directed against a single antigenic epitope. In contrast, conventional (polyclonal) antibody preparations typically include a multitude of antibodies directed against (or specific for) different epitopes. The modifier "monoclonal" indicates the character of the antibody as being obtained from a substantially homogeneous population of antibodies, and is not to be construed as requiring production of the antibody by any particular method. For example, the monoclonal antibodies to be used in accordance with the present disclosure may be made by the hybridoma method first described by Kohler et al. (1975) Nature 256:495, or may be made by recombinant DNA methods (see, e.g., U.S. Pat. No.4,816,567). Monoclonal antibodies may also be isolated from phage antibody libraries using the techniques described in Clackson et al. (1991) Nature 352:624-8, and Marks et al. (1991) J. Mol. Biol.222:581-97, for example. [0031] The monoclonal antibodies disclosed herein specifically include "chimeric" antibodies, in which a portion of the heavy and/or light chain is identical with or homologous to corresponding sequences in antibodies derived from a particular species or belonging to a particular antibody class or subclass, while the remainder of the chain(s) is identical with or homologous to corresponding sequences in antibodies derived from another species or belonging to another antibody class or subclass, as well as fragments of such antibodies, so long as they specifically bind the target antigen and/or exhibit the desired biological activity. [0032] The terms “antibody-drug conjugate,” “antibody conjugate,” “conjugate,” “immunoconjugate,” and “ADC” are used interchangeably, and refer to a compound (e.g., eribulin) or derivative thereof that is linked to an antibody (e.g., an anti-FRA antibody) and is defined by the generic formula: Ab-(L-D)p (Formula I), wherein Ab = an antibody moiety (i.e., antibody or antigen- binding fragment), L = a linker moiety, D = a drug moiety, and p = the number of drug moieties per antibody moiety. [0033] The term "antigen-binding fragment" or "antigen-binding portion" of an antibody, as used herein, refers to one or more fragments of an antibody that retain the ability to specifically bind to an antigen (e.g., FRA). Antigen-binding fragments preferably also retain the ability to internalize into an antigen-expressing cell. In some embodiments, antigen-binding fragments also retain immune effector activity. It has been shown that fragments of a full-length antibody can perform the antigen- binding function of a full-length antibody. Examples of binding fragments encompassed within the term "antigen-binding fragment" or "antigen-binding portion" of an antibody include (i) a Fab fragment, a monovalent fragment consisting of the VL, VH, CL, and CH1 domains; (ii) a F(ab')2 fragment, a bivalent fragment comprising two Fab fragments linked by a disulfide bridge at the hinge Finngean Reference: 15648.0053-00304 region; (iii) a Fd fragment consisting of the VH and CH1 domains; (iv) a Fv fragment consisting of the VL and VH domains of a single arm of an antibody; (v) a dAb fragment, which comprises a single variable domain, e.g., a VH domain (see, e.g., Ward et al. (1989) Nature 341:544-6; and Winter et al., WO 90/05144); and (vi) an isolated complementarity determining region (CDR). Furthermore, although the two domains of the Fv fragment, VL and VH, are coded for by separate genes, they can be joined, using recombinant methods, by a synthetic linker that enables them to be made as a single protein chain in which the VL and VH regions pair to form monovalent molecules (known as single chain Fv (scFv)). See, e.g., Bird et al. (1988) Science 242:423-6; and Huston et al. (1988) Proc. Natl. Acad. Sci. USA 85:5879-83. Such single chain antibodies are also intended to be encompassed within the term "antigen-binding fragment" or "antigen-binding portion" of an antibody, and are known in the art as an exemplary type of binding fragment that can internalize into cells upon binding. See, e.g., Zhu et al. (2010) 9:2131-41; He et al. (2010) J. Nucl. Med.51:427-32; and Fitting et al. (2015) MAbs 7:390-402. In certain embodiments, scFv molecules may be incorporated into a fusion protein. Other forms of single chain antibodies, such as diabodies are also encompassed. Diabodies are bivalent, bispecific antibodies in which VH and VL domains are expressed on a single polypeptide chain, but using a linker that is too short to allow for pairing between the two domains on the same chain, thereby forcing the domains to pair with complementary domains of another chain and creating two antigen binding sites (see e.g., Holliger et al. (1993) Proc. Natl. Acad. Sci. USA 90:6444-8; and Poljak et al. (1994) Structure 2:1121-3). Antigen-binding fragments are obtained using conventional techniques known to those of skill in the art, and the binding fragments are screened for utility (e.g., binding affinity, internalization) in the same manner as are intact antibodies. Antigen-binding fragments may be prepared by cleavage of the intact protein, e.g., by protease or chemical cleavage. [0034] "Biomarker of tumor response” as used herein refers to the following measurable substances from an organism that are indicators of a biological process that relates to tumor biology: SP-D, ANG-2, IGFBP-1, IgFBP-2, TNF-α, IL-10, ICAM-1, TGFA, VEGF, IL-6, IP-10, KLK-5, KLK-7, MCP-1, MMP12, Eotaxin-1, IL17C, EGF, FLT3LG, VEGF-D, HGF, OSM, CCL13, MIP-1 β, CCL8, HER-2, FRTN, IL-18, and TIMP1. Biomarkers of tumor response may also include additional biomarkers in combination with those listed above, e.g., from a broader biomarker panel, such as the Rules-Based Medicine (RBM) panel or the OLINK® Target-48 Cytokine panel. [0035] “Biological sample” as used herein refers to a biological material collected from a living organism. Exemplary biological samples include blood, blood components, tumor biopsy, urine, tissue, cell collection, and saliva. [0036] “Body surface area” or “BSA” as used herein refers to the total surface area of a subject being treated with the methods disclosed herein. A subject’s body surface area may be calculated to determine the most appropriate dosage for a compound, e.g., an antibody-drug conjugate, e.g., an anti- Finngean Reference: 15648.0053-00304 FRA ADC, to be administered to the subject. In general, values for a subject’s body surface area may be derived from calculations based on the subject’s body weight. [0037] The term “cancer” refers to a physiological condition in a mammal in which a population of cells is characterized by unregulated cell growth. Examples of cancers include, but are not limited to, carcinoma, lymphoma, blastoma, sarcoma, leukemia, ovarian cancer (e.g., platinum resistant ovarian cancer), breast cancer (e.g., triple negative breast cancer), non-small cell lung cancer, endometrial cancer, peritoneal cancer, and fallopian tube cancer. Triple negative breast cancer refers to breast cancer that is negative for expression of the genes for estrogen receptor (ER), progesterone receptor (PR), and Her2/neu. More particular examples of such cancers include squamous cell cancer, small cell lung cancer, adenocarcinoma of the lung, squamous carcinoma of the lung, cancer of the peritoneum, hepatocellular cancer, gastrointestinal cancer, pancreatic cancer, glioblastoma, cervical cancer, liver cancer, bladder cancer, hepatoma, osteosarcoma, melanoma, colon cancer, colorectal cancer, uterine cancer, salivary gland carcinoma, kidney cancer, liver cancer, prostate cancer, vulval cancer, thyroid cancer, hepatic carcinoma, peritoneal cancer, fallopian tube cancer, and various types of head and neck cancers. [0038] The terms “cancer cell” and “tumor cell” refer to individual cells or the total population of cells derived from a tumor, including both non-tumorigenic cells and cancer stem cells. As used herein, the term “tumor cell” will be modified by the term “non-tumorigenic” when referring solely to those tumor cells lacking the capacity to renew and differentiate to distinguish those tumor cells from cancer stem cells. [0039] The term "chemotherapeutic agent" or “anti-cancer agent” is used herein to refer to all chemical compounds that are effective in treating cancer regardless of mechanism of action. Inhibition of metastasis or angiogenesis is frequently a property of a chemotherapeutic agent. Non- limiting examples of chemotherapeutic agents include alkylating agents, for example, nitrogen mustards, ethyleneimine compounds, and alkyl sulphonates; antimetabolites, for example, folic acid, purine or pyrimidine antagonists; anti-mitotic agents, for example, anti-tubulin agents such as eribulin or eribulin mesylate (Halaven™) or derivatives thereof, vinca alkaloids, and auristatins; cytotoxic antibiotics; compounds that damage or interfere with DNA expression or replication, for example, DNA minor groove binders; and growth factor receptor antagonists. In addition, chemotherapeutic agents include antibodies, biological molecules, and small molecules. A chemotherapeutic agent may be a cytotoxic or cytostatic agent. The term “cytostatic agent” refers to an agent that inhibits or suppresses cell growth and/or multiplication of cells. [0040] The term “co-administration” or administration “in combination with” one or more therapeutic agents includes concurrent and consecutive administration in any order. [0041] “Corticosteroid,” as used herein, is any compound belonging to a class of steroid hormones that are typically produced in the adrenal cortex of vertebrates. The term as used herein also encompasses synthetic analogs of such hormones, e.g., pharmaceutical compositions which mimic the Finngean Reference: 15648.0053-00304 actions of naturally occurring corticosteroids. Dexamethasone is an exemplary embodiment of a corticosteroid. Prednisone is also an exemplary embodiment of a corticosteroid. Methylprednisolone is another exemplary embodiment of a corticosteroid. [0042] The term "cytotoxic agent" refers to a substance that causes cell death primarily by interfering with a cell’s expression activity and/or functioning. Examples of cytotoxic agents include, but are not limited to, anti-mitotic agents, such as eribulin, auristatins (e.g., monomethyl auristatin E (MMAE), monomethyl auristatin F (MMAF)), maytansinoids (e.g., maytansine), dolastatins, duostatins, cryptophycins, vinca alkaloids (e.g., vincristine, vinblastine), taxanes, taxols, and colchicines; anthracyclines (e.g., daunorubicin, doxorubicin, dihydroxyanthracindione); cytotoxic antibiotics (e.g., mitomycins, actinomycins, duocarmycins (e.g., CC-1065), auromycins, duomycins, calicheamicins, endomycins, phenomycins); alkylating agents (e.g., cisplatin); intercalating agents (e.g., ethidium bromide); topoisomerase inhibitors (e.g., etoposide, tenoposide); radioisotopes, such as At211, I131, I125, Y90, Re186, Re188, Sm153, Bi212 or 213, P32, and radioactive isotopes of lutetium (e.g., Lu177); and toxins of bacterial, fungal, plant or animal origin (e.g., ricin (e.g., ricin A-chain), diphtheria toxin, Pseudomonas exotoxin A (e.g., PE40), endotoxin, mitogellin, combrestatin, restrictocin, gelonin, alpha-sarcin, abrin (e.g., abrin A-chain), modeccin (e.g., modeccin A-chain), curicin, crotin, Sapaonaria officinalis inhibitor, glucocorticoid). [0043] The term “dose” as used herein refers to an amount of a medicine or drug taken at a particular time. A dose may provide an effective amount of an ADC. The medicine or drug can be an ADC. [0044] An “effective amount” of an ADC as disclosed herein is an amount sufficient to perform a specifically stated purpose, for example to produce a therapeutic effect after administration, such as a reduction in tumor growth rate or tumor volume, a reduction in a symptom of cancer, or some other indicia of treatment efficacy. An effective amount can be determined in a routine manner in relation to the stated purpose. The term “therapeutically effective amount” refers to an amount of an ADC effective to treat a disease or disorder in a subject. In the case of cancer, a therapeutically effective amount of ADC can reduce the number of cancer cells, reduce tumor size, inhibit (e.g., slow or stop) tumor metastasis, inhibit (e.g., slow or stop) tumor growth, and/or relieve one or more symptoms. Treatment and therapeutically effective amounts for treatment encompass but do not require complete treatment. For instance, the term encompasses but does not require complete stopping of tumor growth. [0045] The term “epitope” refers to the portion of an antigen capable of being recognized and specifically bound by an antibody. When the antigen is a polypeptide, epitopes can be formed from contiguous amino acids or noncontiguous amino acids juxtaposed by tertiary folding of the polypeptide. The epitope bound by an antibody may be identified using any epitope mapping technique known in the art, including X-ray crystallography for epitope identification by direct visualization of the antigen-antibody complex, as well as monitoring the binding of the antibody to Finngean Reference: 15648.0053-00304 fragments or mutated variations of the antigen, or monitoring solvent accessibility of different parts of the antibody and the antigen. Exemplary strategies used to map antibody epitopes include, but are not limited to, array-based oligo-peptide scanning, limited proteolysis, site-directed mutagenesis, high- throughput mutagenesis mapping, hydrogen-deuterium exchange, and mass spectrometry (see, e.g., Gershoni et al. (2007) 21:145-56; and Hager-Braun and Tomer (2005) Expert Rev. Proteomics 2:745- 56). [0046] The term “eribulin,” as used herein, refers to a synthetic analog of halichondrin B, a macrocyclic compound that was originally isolated from the marine sponge Halichondria okadais. The term “eribulin drug moiety” refers to the component of an ADC that has the structure of eribulin, and is attached to the linker of the ADC via its C-35 amine. Eribulin is a microtubule dynamics inhibitor, which is thought to bind tubulin and induce cell cycle arrest at the G2/M phase by inhibiting mitotic spindle assembly. The term “eribulin mesylate” refers to the mesylate salt of eribulin, which is marketed under the trade name Halaven™. [0047] The term “folate receptor alpha” or “FRA,” as used herein, refers to any native form of human FRA. The term encompasses full-length FRA (e.g., NCBI Reference Sequence: NP_000793; SEQ ID NO: 37), as well as any form of human FRA that results from cellular processing. The term also encompasses naturally occurring variants of FRA, including but not limited to splice variants, allelic variants, and isoforms. FRA can be isolated from a human, or may be produced recombinantly or by synthetic methods. [0048] The term "anti-FRA antibody" or “antibody that specifically binds FRA” refers to any form of antibody or fragment thereof that specifically binds FRA, and encompasses monoclonal antibodies (including full length monoclonal antibodies), polyclonal antibodies, and biologically functional antibody fragments so long as they specifically bind FRA. Preferably the anti-FRA antibody used in the ADCs disclosed herein is an internalizing antibody or internalizing antibody fragment. MORAb- 003 is an exemplary internalizing anti-human FRA antibody that may be used in the present disclosure, e.g., as part of an anti-FRA ADC. As used herein, the terms "specific," "specifically binds," and "binds specifically" refer to the selective binding of the antibody to the target antigen epitope. Antibodies can be tested for specificity of binding by comparing binding to appropriate antigen to binding to irrelevant antigen or antigen mixture under a given set of conditions. If the antibody binds to the appropriate antigen with at least 2, 5, 7, and preferably 10 times more affinity than to irrelevant antigen or antigen mixture, then it is considered to be specific. In one embodiment, a specific anti-FRA antibody is one that only binds the FRA antigen, but does not bind (or exhibits minimal binding) to other antigens. [0049] “Internalizing” as used herein in reference to an antibody or antigen-binding fragment refers to an antibody or antigen-binding fragment that is capable of being taken through the cell’s lipid bilayer membrane to an internal compartment (i.e., “internalized”) upon binding to the cell, preferably Finngean Reference: 15648.0053-00304 into a degradative compartment in the cell. For example, an internalizing anti-FRA antibody is one that is capable of being taken into the cell after binding to FRA on the cell membrane. [0050] The term “interstitial lung disease” refers to any one of a group of lung diseases characterized by inflammation which may lead to pulmonary fibrosis. Interstitial lung disease (ILD) is known to be a potential adverse effect associated with immunotherapy treatment. An “adverse effect” or “AE” is any untoward medical occurrence in a subject administered a compound, and does not necessarily implicate a causal relationship with the administered compound or indicate that the compound cannot be used in treatment, but may present a limitation on the compound’s use. Methods of identifying and diagnosing interstitial lung disease are well known in the art, for example, evaluating oxygen saturation using pulse oximetry, and assessing ILD-related lung damage using chest computed tomography (CT) scans. [0051] A “linker” or “linker moiety” is any chemical moiety that is capable of covalently joining a compound, usually a drug moiety such as a chemotherapeutic agent, to another moiety such as an antibody moiety. Linkers can be susceptible to or substantially resistant to acid-induced cleavage, peptidase-induced cleavage, light-based cleavage, esterase-induced cleavage, and/or disulfide bond cleavage, at conditions under which the compound or the antibody remains active. [0052] The term “p” or “antibody:drug ratio” or “drug-to-antibody ratio” or “DAR” refers to the number of drug moieties per antibody moiety, i.e., drug loading, or the number of -L-D moieties per antibody or antigen-binding fragment (Ab) in ADCs of Formula I. In compositions comprising multiple copies of ADCs of Formula I, “p” refers to the average number of -L-D moieties per antibody or antigen-binding fragment, also referred to as average drug loading. [0053] "Pharmaceutically acceptable" means approved or approvable by a regulatory agency of the Federal or a state government, or listed in the U.S. Pharmacopeia or other generally recognized pharmacopeia, for use in animals, and more particularly in humans. [0054] A “pharmaceutical composition” refers to a preparation which is in such form as to permit administration and subsequently provide the intended biological activity of the active ingredient(s) and/or to achieve a therapeutic effect, and which contains no additional components which are unacceptably toxic to a subject to which the formulation would be administered. The pharmaceutical composition may be sterile. [0055] A "pharmaceutical excipient" comprises a material such as an adjuvant, a carrier, pH- adjusting and buffering agents, tonicity adjusting agents, wetting agents, preservative, and the like. [0056] By "protein," as used herein, is meant at least two covalently attached amino acids. The term encompasses polypeptides, oligopeptides, and peptides. In some embodiments, the two or more covalently attached amino acids are attached by a peptide bond. The protein may be made up of naturally occurring amino acids and peptide bonds, for example when the protein is made recombinantly using expression systems and host cells. Alternatively, the protein may include Finngean Reference: 15648.0053-00304 synthetic amino acids (e.g., homophenylalanine, citrulline, ornithine, and norleucine), or peptidomimetic structures, i.e., "peptide or protein analogs," such as peptoids. [0057] For amino acid sequences, sequence identity and/or similarity may be determined using standard techniques known in the art, including, but not limited to, the local sequence identity algorithm of Smith and Waterman (1981) Adv. Appl. Math.2:482, the sequence identity alignment algorithm of Needleman and Wunsch (1970) J. Mol. Biol.48:443, the search for similarity method of Pearson and Lipman (1988) Proc. Nat. Acad. Sci. USA 85:2444, computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Drive, Madison, Wis.), the Best Fit sequence program described by Devereux et al. (1984) Nucl. Acid Res.12:387-95, preferably using the default settings, or by inspection. Preferably, percent identity is calculated by FastDB based upon the following parameters: mismatch penalty of 1; gap penalty of 1; gap size penalty of 0.33; and joining penalty of 30 ("Current Methods in Sequence Comparison and Analysis," Macromolecule Sequencing and Synthesis, Selected Methods and Applications, pp.127-149 (1988), Alan R. Liss, Inc). [0058] An example of a useful algorithm is PILEUP. PILEUP creates a multiple sequence alignment from a group of related sequences using progressive, pairwise alignments. It can also plot a tree showing the clustering relationships used to create the alignment. PILEUP uses a simplification of the progressive alignment method of Feng & Doolittle (1987) J. Mol. Evol.35:351-60; the method is similar to that described by Higgins and Sharp (1989) CABIOS 5:151-3. Useful PILEUP parameters including a default gap weight of 3.00, a default gap length weight of 0.10, and weighted end gaps. [0059] Another example of a useful algorithm is the BLAST algorithm, described in: Altschul et al. (1990) J. Mol. Biol.215:403-10; Altschul et al. (1997) Nucleic Acids Res.25:3389-402; and Karin et al. (1993) Proc. Natl. Acad. Sci. USA 90:5873-87. A particularly useful BLAST program is the WU- BLAST-2 program which was obtained from Altschul et al. (1996) Methods in Enzymology 266:460- 80. WU-BLAST-2 uses several search parameters, most of which are set to the default values. The adjustable parameters are set with the following values: overlap span=l, overlap fraction=0.125, word threshold (T)=II. The HSP S and HSP S2 parameters are dynamic values and are established by the program itself depending upon the composition of the particular sequence and composition of the particular database against which the sequence of interest is being searched; however, the values may be adjusted to increase sensitivity. [0060] An additional useful algorithm is gapped BLAST as reported by Altschul et al. (1993) Nucl. Acids Res.25:3389-402. Gapped BLAST uses BLOSUM-62 substitution scores; threshold T parameter set to 9; the two-hit method to trigger ungapped extensions, charges gap lengths of k a cost of 10+k; Xu set to 16, and Xg set to 40 for database search stage and to 67 for the output stage of the algorithms. Gapped alignments are triggered by a score corresponding to about 22 bits. Finngean Reference: 15648.0053-00304 [0061] Generally, the amino acid homology, similarity, or identity between proteins disclosed herein and variants thereof, including variants of FRA, and variants of antibody variable domains (including individual variant CDRs), are at least 80% to the sequences depicted herein, and more typically with preferably increasing homologies or identities of at least 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, and almost 100% or 100%. [0062] In a similar manner, "percent (%) nucleic acid sequence identity" with respect to the nucleic acid sequence of the antibodies and other proteins identified herein is defined as the percentage of nucleotide residues in a candidate sequence that are identical with the nucleotide residues in the coding sequence of the antigen binding protein. A specific method utilizes the BLASTN module of WU-BLAST-2 set to the default parameters, with overlap span and overlap fraction set to 1 and 0.125, respectively. [0063] The terms “subject,” “patient,” and “participant” are used interchangeably herein to refer to any animal, such as any mammal, including but not limited to, humans, non-human primates, rodents, and the like. In some embodiments, the mammal is a mouse. In some embodiments, the mammal is a human. [0064] The terms “tumor” and “neoplasm” refer to any mass of tissue that results from excessive cell growth or proliferation, either benign or malignant, including precancerous lesions. [0065] As used herein, "to treat" or "therapeutic" and grammatically related terms, refer to any improvement of any consequence of disease, such as prolonged survival, halted or delayed tumor growth, reduction in tumor size, less morbidity, and/or a lessening of side effects which are the byproducts of an alternative therapeutic modality. As is readily appreciated in the art, full eradication of disease is a preferred but albeit not a requirement for a treatment act. “Treatment” or “treat,” as used herein, refers to the administration of, e.g. a disclosed ADC, to a subject, e.g., a patient. The treatment can be to cure, heal, alleviate, relieve, alter, remedy, ameliorate, palliate, improve or affect the disorder, the symptoms of the disorder or the predisposition toward the disorder, e.g., a cancer. The terms “treatment” and “therapy” are used interchangeably herein. [0066] In various embodiments, provided herein is a method of reducing risk of interstitial lung disease (ILD) in a subject treated an anti-FRA ADC. “Reducing risk” as used herein refers to a change in incidence rate of ILD (for example, a change in number of subjects with ILD) relative to a comparative treatment. For example, a treatment with an anti-FRA ADC disclosed herein using a BSA-based dosing regimen may reduce the risk of ILD in certain subjects as compared to similar subjects administered the anti-FRA ADC at an equivalent body weight-based dose over a given time period. [0067] The term “upper quartile for weight” as used herein refers to a body weight value that is within the top 25% of all body weight values for a given group of subjects, e.g., a group of adults in a general population or a group of subjects with an FRA-expressing cancer. As used herein, the term is inclusive of the value representing the border of the top 25%. For example, the upper quartile for Finngean Reference: 15648.0053-00304 weight for a given group of subjects can be determined by first arranging the body weight values of the subjects in ascending order, then dividing the set of values into quarters (also known as quartiles), and lastly determining the value between the third and fourth quartiles. A subject who is in the upper quartile for weight has a body weight value that is at least equal to, if not greater than, the value between the third and fourth quartiles. In some embodiments, the value between the third and fourth quartiles for a given group of subjects is near or about 80 kilograms. Antibody-Drug Conjugates [0068] The methods of the present disclosure include the use of compounds with anti-cancer activity. In particular, the compounds include an antibody moiety (including an antigen-binding fragment thereof) conjugated (i.e., covalently attached by a linker) to a drug moiety, wherein the drug moiety, e.g., when not conjugated to an antibody moiety, has a cytotoxic or cytostatic effect. In various embodiments, the drug moiety exhibits reduced or no cytotoxicity when bound in a conjugate but resumes cytotoxicity after cleavage from the linker and antibody moiety. [0069] In some embodiments, the ADC comprises a peptide cleavable linker attaching eribulin to an anti-FRA ADC. In some embodiments, the linker comprises a val-cit moiety. In some embodiments, the linker comprises a PEG spacer. In some embodiments, the linker compriess a Mal-(PEG)2-Val- Cit-pAB linker joining eribulin to an anti-FRA antibody (e.g., an anti-FRA antibody such as MORAb- 003). In some embodiments, the anti-FRA ADC is MORAb-202. “MORAb-202” refers to an anti- FRA ADC, wherein the anti-FRA antibody or antigen-binding fragment comprises a heavy chain amino acid sequence of SEQ ID NO: 15 and a light chain amino acid sequence of SEQ ID NO: 16, wherein the linker moiety comprises Mal-(PEG)2-Val-Cit-pAB, and wherein the linker is attached to eribulin via a C-35 amine. In some embodiments, the structure of MORAb-202 (including the sequences of the anti-FRA antibody moiety in the ADC) are disclosed in PCT Application No. PCT/US2017/020529 (published as WO 2017/151979), which is incorporated herein by reference in its entiry. [0070] In some embodiments, the anti-FRA ADC (e.g., MORAb-202) exhibits particularly favorable properties across various categories, such as: (i) the ability to retain one or more therapeutic properties exhibited by the antibody and drug moieties in isolation, (ii) the ability to maintain the specific binding properties of the antibody moiety; (iii) optimal drug loading and drug-to-antibody ratios; (iv) the ability to allow delivery, e.g., intracellular delivery, of the drug moiety via stable attachment to the antibody moiety; (v) the ability to retain ADC stability as an intact conjugate until transport or delivery to a target site; (vi) minimal aggregation of the ADC prior to or after administration; (vii) the ability to allow for the therapeutic effect, e.g., cytotoxic effect, of the drug moiety after cleavage in the cellular environment; (viii) in vivo anti-cancer treatment efficacy comparable to or superior to that of the antibody and drug moieties in isolation; (ix) minimal off- Finngean Reference: 15648.0053-00304 target killing by the drug moiety; and/or (x) desirable pharmacokinetic and pharmacodynamics properties, formulatability, and toxicologic/immunologic profiles. [0071] An ADC compound of the present disclosure may selectively deliver an effective dose of a cytotoxic or cytostatic agent to FRA-expressing cancer cells or to FRA-expressing tumor tissue. It has been discovered that the disclosed ADCs have potent cytotoxic and/or cytostatic activity against cells expressing FRA. Exemplary FRA-expressing cancers include but are not limited to ovarian cancer (e.g., serous ovarian cancer, clear cell ovarian cancer, or platinum resistant ovarian cancer), lung cancer (e.g., non-small cell lung cancer, e.g., metastatic non-small cell lung cancer), breast cancer (e.g., triple negative breast cancer), and endometrial cancer. [0072] An exemplary ADC has Formula I: Ab-(L-D)p (I) wherein Ab = internalizing anti-folate receptor alpha antibody or internalizing antigen-binding fragment thereof, L = cleavable linker moiety, D = drug moiety, and p = the number of drug moieties per antibody moiety. Antibodies [0073] In various embodiments, the antibody moiety (Ab) of the ADC of Formula I includes within its scope any antibody or antigen-binding fragment that specifically binds to FRA on a cancer cell. The antibody or antigen-binding fragment may bind to FRA with a dissociation constant (KD) of ≤1 mM, ≤100 nM or ≤10 nM, or any amount in between, as measured by, e.g., BIAcore® analysis. In certain embodiments, the KD is 1 pM to 500 pM. In some embodiments, the KD is between 500 pM to 1 µM, 1 µM to 100 nM, or 100 mM to 10 nM. [0074] In some embodiments, the antibody moiety is a four-chain antibody (also referred to as an immunoglobulin), comprising two heavy chains and two light chains. In some embodiments the antibody moiety is a two-chain half body (one light chain and one heavy chain), or an antigen-binding fragment of an immunoglobulin. [0075] In some embodiments, the antibody moiety is an internalizing antibody or internalizing antigen-binding fragment thereof. In some embodiments, the internalizing antibody binds to FRA expressed on the surface of a cell and enters the cell upon binding. In some embodiments, the FRA- targeting antibody moiety is MORAb-003. In some embodiments, the drug moiety of the ADC is released from the antibody moiety of the ADC after the ADC enters and is present in a cell expressing the target cancer antigen (i.e., after the ADC has been internalized). [0076] Amino acid and nucleic acid sequences of exemplary antibodies that may be used in the ADCs disclosed herein are set forth in Tables 1-9. Finngean Reference: 15648.0053-00304 Table 1. Antibodies Table 2. Amino acid sequences of mAb variable regions Table 3. Nucleic acid sequences encoding mAb variable regions Finngean Reference: 15648.0053-00304 Table 4. Amino acid sequences of mAb Kabat CDRs Table 5. Nucleic acid sequences encoding mAb Kabat CDRs Table 6. Amino acid sequences of mAb IMGT CDRs Finngean Reference: 15648.0053-00304 Table 7. Nucleic acid sequences encoding mAb IMGT CDRs Table 8. Amino acid sequences of full-length mAb Ig chains Finngean Reference: 15648.0053-00304 Table 9. Nucleic acid sequences encoding full-length mAb Ig chains+ Finngean Reference: 15648.0053-00304 Finngean Reference: 15648.0053-00304 + Nucleic acid sequences listed do not include leader sequences. [0077] In various embodiments, an ADC disclosed herein may comprise the set of MORAb-003 heavy and light chain variable domains listed in the tables above, or a set of six MORAb-003 CDR sequences (Kabat and/or IMGT) from the heavy and light chains listed in the tables above. In some embodiments, the ADC further comprises human heavy and light chain constant domains or fragments thereof. For instance, the ADC may comprise a human IgG heavy chain constant domain (such as an IgG1) and a human kappa or lambda light chain constant domain. In various embodiments, the antibody moiety of the disclosed ADCs comprises a human immunoglobulin G subtype 1 (IgG1) heavy chain constant domain with a human Ig kappa light chain constant domain. In some embodiments, the anti-FRA antibody moiety in the ADC comprises the full heavy and light chain sequences listed in the tables above. [0078] In various embodiments, the anti-FRA antibody or antigen-binding fragment thereof comprises three heavy chain CDRs and three light chain CDRs as follows: heavy chain CDR1 (HCDR1) comprising SEQ ID NO: 1, heavy chain CDR2 (HCDR2) comprising SEQ ID NO: 2, heavy chain CDR3 (HCDR3) comprising SEQ ID NO: 3; light chain CDR1 (LCDR1) comprising SEQ ID NO: 4, light chain CDR2 (LCDR2) comprising SEQ ID NO: 5, and light chain CDR3 (LCDR3) comprising SEQ ID NO: 6, as defined by the Kabat numbering system (Kabat, Sequences of Proteins of Immunological Interest (National Institutes of Health, Bethesda, Md. (1987 and 1991))). [0079] In some embodiments, the anti-FRA antibody or antigen-binding fragment thereof comprises three heavy chain CDRs and three light chain CDRs as follows: heavy chain CDR1 comprising SEQ ID NO: 7, heavy chain CDR2 comprising SEQ ID NO: 8, heavy chain CDR3 comprising SEQ ID NO: 9; light chain CDR1 comprising SEQ ID NO: 10, light chain CDR2 comprising SEQ ID NO: 11, and light chain CDR3 comprising SEQ ID NO: 12, as defined by the IMGT numbering system (International ImMunoGeneTics Information System (IMGT®)). [0080] In various embodiments, the anti-FRA antibody or antigen-binding fragment thereof comprises a heavy chain variable region comprising the amino acid sequence of SEQ ID NO: 13, and a light chain variable region comprising the amino acid sequence of SEQ ID NO: 14. In some embodiments, the anti-FRA antibody or antigen-binding fragment thereof comprises the heavy chain variable region amino acid sequence of SEQ ID NO: 13 and the light chain variable region amino acid sequence of SEQ ID NO: 14, or sequences that are at least 95% identical to the above-mentioned Finngean Reference: 15648.0053-00304 sequences. In some embodiments, the anti-FRA antibody or antigen-binding fragment thereof has a heavy chain variable region amino acid sequence that is at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 13 and a light chain variable region amino acid sequence that is at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 14. [0081] In various embodiments, the anti-FRA antibody comprises a human IgG1 heavy chain constant domain with a human Ig kappa light chain constant domain. [0082] In various embodiments, the anti-FRA antibody comprises the heavy chain amino acid sequence of SEQ ID NO: 15 or a sequence that is at least 95% identical to SEQ ID NO: 15, and the light chain amino acid sequence of SEQ ID NO: 16 or a sequence that is at least 95% identical to SEQ ID NO: 16. In particular embodiments, the antibody comprises the heavy chain amino acid sequence of SEQ ID NO: 15 and the light chain amino acid sequence of SEQ ID NO: 16, or sequences that are at least 95% identical to the above-mentioned sequences. In some embodiments, the anti-FRA antibody has a heavy chain amino acid sequence that is at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 15 and/or a light chain amino acid sequence that is at least 96%, at least 97%, at least 98%, or at least 99% identical to SEQ ID NO: 16. In some embodiments, the anti- FRA antibody comprises the heavy chain amino acid sequence of SEQ ID NO: 15 and the light chain amino acid sequence of SEQ ID NO: 16. In some embodiments, the anti-FRA antibody comprises a heavy chain encoded by the nucleotide sequence of SEQ ID NO: 35 (with the nucleotides encoding the leader sequence), or SEQ ID NO: 31 (without the nucleotides encoding the leader sequence); and a light chain encoded by the nucleotide sequence of SEQ ID NO: 36 (with the nucleotides encoding the leader sequence), or SEQ ID NO: 32 (without the nucleotides encoding the leader sequence). In some embodiments, the heavy chain amino acid sequence lacks the C-terminal lysine. In various embodiments, the anti-FRA antibody has the amino acid sequence of the antibody produced by a cell line deposited under terms in accordance with the Budapest Treaty with the American Type Culture Collection (ATCC, 10801 University Blvd., Manassas, Va.20110-2209) on Apr.24, 2006, under the Accession No. PTA-7552, or such sequences lacking the heavy chain C-terminal lysine. In various embodiments, the anti-FRA antibody is MORAb-003 (USAN name: farletuzumab) (Ebel et al. (2007) Cancer Immunity 7:6), or an antigen-binding fragment thereof. [0083] In various embodiments, amino acid substitutions are of single residues. Insertions usually will be on the order of from about 1 to about 20 amino acid residues, although considerably larger insertions may be tolerated as long as anti-FRA biological function is retained. Deletions usually range from about 1 to about 20 amino acid residues, although in some cases deletions may be much larger. Substitutions, deletions, insertions, or any combination thereof may be used to arrive at a final derivative or variant. Generally these changes are done on a few amino acids to minimize the alteration of the molecule, particularly the immunogenicity and specificity of the antigen binding protein. However, larger changes may be tolerated in certain circumstances. Conservative substitutions are generally made in accordance with the following chart depicted as Table 10. Finngean Reference: 15648.0053-00304 Table 10 [0084] In some embodiments, the FRA-targeting antibody moiety is MORAb-003. In some embodiments, FRA-targeting antibody moieties such as MORAb-003 provide particularly improved drug:antibody ratio, tumor targeting, bystander killing, treatment efficacy, and reduced off-target killing. Improved treatment efficacy can be measured in vitro or in vivo, and may include reduced tumor growth rate and/or reduced tumor volume. Linkers [0085] In various embodiments, the linker in an anti-FRA ADC, e.g., an ADC of formula I, is stable extracellularly in a sufficient manner to be therapeutically effective. In some embodiments, the linker is stable outside a cell, such that the ADC remains intact when present in extracellular conditions (e.g., prior to transport or delivery into an FRA-expressing cell). The term “intact,” used in the context of an ADC, means that the antibody moiety remains attached to the drug moiety. As used herein, “stable,” in the context of a linker or ADC comprising a linker, means that no more than 20%, Finngean Reference: 15648.0053-00304 no more than about 15%, no more than about 10%, no more than about 5%, no more than about 3%, or no more than about 1% of the linkers (or any percentage in between) in a sample of ADC are cleaved (or in the case of an overall ADC are otherwise not intact) when the ADC is present in extracellular conditions. [0086] Whether a linker is stable extracellularly can be determined, for example, by including an anti-FRA ADC in plasma for a predetermined time period (e.g., 2, 4, 6, 8, 16, or 24 hours) and then quantifying the amount of free drug moiety present in the plasma. Stability may allow the ADC time to localize to target tumor cells and prevent the premature release of the drug, which could lower the therapeutic index of the ADC by indiscriminately damaging both normal and tumor tissues. In some embodiments, the linker is stable outside of a target cell and releases the drug moiety from the ADC once inside of the cell, such that the drug moiety can bind to its target (e.g., to microtubules). Thus, an effective linker will: (i) maintain the specific binding properties of the antibody moiety; (ii) allow delivery, e.g., intracellular delivery, of the drug moiety via stable attachment to the antibody moiety; (iii) remain stable and intact until the ADC has been transported or delivered to its target site; and (iv) allow for the therapeutic effect, e.g., cytotoxic effect, of the drug moiety after cleavage. [0087] A linker may be “cleavable” or “non-cleavable” (Ducry and Stump, Bioconjugate Chem. (2010) 21:5-13). Cleavable linkers are designed to release the drug when subjected to certain environment factors, e.g., when internalized into the target cell, whereas non-cleavable linkers generally rely on the degradation of the antibody moiety itself. [0088] In some embodiments, the linker is a cleavable linker. A cleavable linker refers to any linker that comprises a cleavable moiety. As used herein, the term “cleavable moiety” refers to any chemical bond that can be cleaved. Suitable cleavable chemical bonds are well known in the art and include, but are not limited to, acid labile bonds, protease/peptidase labile bonds, photolabile bonds, disulfide bonds, and esterase labile bonds. Linkers comprising a cleavable moiety can allow for the release of the drug moiety from the ADC via cleavage at a particular site in the linker. In various embodiments, cleavage of the anti-FRA antibody from the linked toxin activates or increases the activity of the toxin. [0089] In some embodiments, the linker is cleavable by a cleaving agent, e.g., an enzyme, that is present in the intracellular environment (e.g., within a lysosome or endosome or caveolea). The linker can be, e.g., a peptide linker that is cleaved by an intracellular peptidase or protease enzyme, including, but not limited to, a lysosomal or endosomal protease. In some embodiments, the linker is a cleavable peptide linker. As used herein, a cleavable peptide linker refers to any linker that comprises a cleavable peptide moiety. The term “cleavable peptide moiety” refers to any chemical bond linking amino acids (natural or synthetic amino acid derivatives) that can be cleaved by an agent that is present in the intracellular environment. For instance, a linker may comprise a valine-citrulline (Val-Cit) sequence that is cleavable by a peptidase such as cathepsin, e.g., cathepsin B. Finngean Reference: 15648.0053-00304 [0090] In some embodiments, the linker is an enzyme-cleavable linker and a cleavable peptide moiety in the linker is cleavable by the enzyme. In some embodiments, the cleavable peptide moiety is cleavable by cathepsin B. An exemplary dipeptide that may be cleaved by cathepsin B is valine- citrulline (Val-Cit) (Dubowchik et al. (2002) Bioconjugate Chem.13:855-69). [0091] In some embodiments, the linker or the cleavable peptide moiety in the linker comprises an amino acid unit. In some embodiments, the amino acid unit allows for cleavage of the linker by a protease, thereby facilitating release of the drug moiety from the ADC upon exposure to one or more intracellular proteases, such as one or more lysosomal enzymes (Doronina et al. (2003) Nat. Biotechnol.21:778-84; Dubowchik and Walker (1999) Pharm. Therapeutics 83:67-123). Exemplary amino acid units include, but are not limited to, dipeptides. Exemplary dipeptides include, but are not limited to, valine-citrulline (Val-Cit). In some embodiments, the amino acid unit in the linker comprises Val-Cit. An amino acid unit may comprise amino acid residues that occur naturally and/or minor amino acids and/or non-naturally occurring amino acid analogs, such as citrulline. [0092] In some embodiments, the linker in an anti-FRA ADC disclosed herein comprises at least one spacer unit joining the antibody moiety to the drug moiety. In some embodiments, the spacer unit joins a cleavage site (e.g., a cleavable peptide moiety) in the linker to the antibody moiety. In some embodiments, the linker comprises one or more polyethylene glycol (PEG) moieties, e.g., 1, 2, 3, 4, 5, or 6 PEG moieties. In some embodiments, the linker comprises 2 PEG moieties. [0093] In some embodiments, the spacer unit in the linker comprises one or more PEG moieties. In some embodiments, the spacer unit comprises –(PEG)m-, and m is 2. In some preferred embodiments, the spacer unit comprises (PEG)2. [0094] In some embodiments, the spacer unit links the antibody moiety to the drug moiety indirectly. In some embodiments, the spacer unit links the antibody moiety to the drug moiety indirectly through a cleavable peptide moiety and an attachment moiety to join the spacer unit to the antibody moiety, e.g., a maleimide moiety. [0095] The spacer unit, in various embodiments, attaches to an anti-FRA antibody moiety (i.e., an anti-FRA antibody or antigen-binding fragment thereof) via a maleimide moiety (Mal). [0096] A spacer unit that attaches to the antibody or antigen-binding fragment via a Mal is referred to herein as a “Mal-spacer unit.” The term “maleimide moiety,” as used herein, means a compound that contains a maleimide group and that is reactive with a sulfhydryl group, e.g., a sulfhydryl group of a cysteine residue on the antibody moiety. In some embodiments, the Mal-spacer unit is reactive with a cysteine residue on the antibody or antigen-binding fragment. In some embodiments, the Mal- spacer unit is joined to the antibody or antigen-binding fragment via the cysteine residue. In some embodiments, the Mal-spacer unit comprises a (PEG)2 moiety. [0097] In certain embodiments, the linker comprises the Mal-spacer unit and a cleavable peptide moiety. In some embodiments, the cleavable peptide moiety comprises an amino acid unit. In some Finngean Reference: 15648.0053-00304 embodiments, the amino acid unit comprises Val-Cit. In some embodiments, the linker comprises Mal-(PEG)2 and Val-Cit. [0098] In some embodiments, the Mal-spacer unit attaches an anti-FRA antibody moiety (i.e., an anti-FRA antibody or antigen-binding fragment thereof) to the cleavable moiety in the linker. In some embodiments, the Mal-spacer unit attaches the antibody or antigen-binding fragment to a cleavable peptide moiety. In some embodiments, the cleavable peptide moiety comprises an amino acid unit. In some embodiments, the linker comprises Mal-spacer unit-amino acid unit. In some embodiments, the Mal-spacer unit comprises a PEG moiety. In some embodiments, the amino acid unit comprises Val-Cit. [0099] In some embodiments, the linker comprises the structure: Mal-spacer unit-Val-Cit. In some embodiments, the linker comprises the structure: Mal-(PEG)2-Val-Cit. In some embodiments, the linker comprises the structure: Mal-(PEG)2-Val-Cit-pAB. [00100] In some embodiments, another spacer unit is used to attach the cleavable moiety in the linker to the drug moiety, e.g., eribulin. In some embodiments, the eribulin is attached to the cleavable moiety in the linker by a self-immolative spacer unit. In certain embodiments, the eribulin is attached to the cleavable moiety in the linker by a self-immolative spacer unit, the cleavable moiety comprises Val-Cit, and a further spacer unit comprising (PEG)2 joins the cleavable moiety to an anti- FRA antibody moiety. In certain embodiments, the eribulin is joined to an anti-FRA antibody via a Mal-spacer unit in the linker joined to a Val-Cit cleavable moiety and a pAB self-immolative spacer unit. [00101] A spacer unit may be “self-immolative” or “non-self-immolative.” A “non-self- immolative" spacer unit is one in which part or all of the spacer unit remains bound to the drug moiety upon cleavage of the linker. Examples of non-self-immolative spacer units include, but are not limited to, a glycine spacer unit and a glycine-glycine spacer unit. Non-self-immolative spacer units may eventually degrade over time but do not readily release a linked native drug entirely under cellular conditions. A "self-immolative" spacer unit allows for release of the native drug moiety under intracellular conditions. A “native drug” is one where no part of the spacer unit or other chemical modification remains after cleavage/degradation of the spacer unit. [00102] Self-immolation chemistry is known in the art and could be readily selected for the disclosed ADCs. In various embodiments, the spacer unit attaching the cleavable moiety in the linker to the drug moiety (e.g., eribulin) is self-immolative, and undergoes self-immolation concurrently with or shortly before/after cleavage of the cleavable moiety under intracellular conditions. [00103] In certain embodiments, the self-immolative spacer unit in the linker comprises a p- aminobenzyl unit. In some embodiments, a p-aminobenzyl alcohol (pABOH) is attached to an amino acid unit or other cleavable moiety in the linker via an amide bond, and a carbamate, methylcarbamate, or carbonate is made between the pABOH and the drug moiety (Hamann et al. (2005) Expert Opin. Ther. Patents 15:1087-103). In some embodiments, the self-immolative spacer Finngean Reference: 15648.0053-00304 unit is or comprises p-aminobenzyloxycarbonyl (pAB). Without being bound by theory, it is thought that the self-immolation of pAB involves a spontaneous 1,6-elimination reaction (Jain et al. (2015) Pharm Res 32:3526-40). [00104] In various embodiments, the structure of the p-aminobenzyloxycarbonyl (pAB) used in the disclosed ADCs is shown below: [00105] In various embodiments, the self-immolative spacer unit attaches the cleavable moiety in the linker to the C-35 amine on eribulin. In some embodiments, the self-immolative spacer unit is pAB. In some embodiments, the pAB attaches the cleavable moiety in the linker to the C-35 amine on eribulin. In some embodiments, the pAB undergoes self-immolation upon cleavage of the cleavable moiety, and eribulin is released from the ADC in its native, active form. In some embodiments, an anti-FRA antibody (e.g., MORAb-003) is joined to the C-35 amine of eribulin by a linker comprising Mal-(PEG)2-Val-Cit-pAB. [00106] In some embodiments, the pAB undergoes self-immolation upon cleavage of a cleavable peptide moiety in the linker. In some embodiments, the cleavable peptide moiety comprises an amino acid unit. In some embodiments, the linker comprises amino acid unit-pAB. In some embodiments, the amino acid unit is Val-Cit. In some embodiments, the linker comprises Val-Cit-pAB (VCP). In various aspects, the antibody moiety of the ADC is conjugated to the drug moiety via a linker, wherein the linker comprises a Mal-spacer unit, a cleavable amino acid unit, and a pAB. In some embodiments, the spacer unit comprises a PEG moiety. In some embodiments, the linker comprises Mal-(PEG)2-Val-Cit-pAB. [00107] In some embodiments, the antibody moiety is conjugated to the drug moiety via a linker comprising a maleimide moiety (Mal), a polyethylene glycol (PEG) moiety, valine citrulline (Val-Cit or "vc"), and a pAB. In these embodiments, the maleimide moiety covalently attaches the linker-drug moiety to the antibody moiety, and the pAB acts as a self-immolative spacer unit. Such linker may be referred to as the "m-vc-pAB” linker, the “Mal-VCP” linker, the “Mal-(PEG)2-VCP” linker, or the “Mal-(PEG)2-Val-Cit-pAB” linker. In some embodiments, the drug moiety is eribulin. The structure of Mal-(PEG)2-Val-Cit-pAB-eribulin is provided below. The pAB of the Mal-(PEG)2-Val-Cit-pAB linker is attached to the C-35 amine on eribulin. Finngean Reference: 15648.0053-00304 [00108] It has been discovered that ADCs comprising Mal-(PEG)2-Val-Cit-pAB-eribulin demonstrate a particular combination of desirable properties, particularly when paired with an anti- FRA antibody such as MORAb-003 or an antigen-binding fragment thereof. These functional properties are also exemplified in the Examples provided in PCT Application No. PCT/US2017/020529 (published as WO 2017/151979), which is incorporated herein by reference in its entirety. [00109] In some embodiments, an ADC comprises Mal-(PEG)2-Val-Cit-pAB-eribulin and an antibody moiety comprising an internalizing anti-FRA antibody or an antigen-binding fragment thereof that retains the ability to target and internalize in a tumor cell. In some embodiments, the ADC comprises Mal-(PEG)2-Val-Cit-pAB-eribulin and an internalizing anti-FRA antibody or internalizing antigen-binding fragment thereof that targets a FRA-expressing tumor cell. In some embodiments, the internalizing antibody or internalizing antigen-binding fragment thereof that targets an FRA-expressing tumor cell comprises three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system. In some embodiments, the internalizing antibody or internalizing antigen-binding fragment thereof that targets an FRA-expressing tumor cell comprises a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 13, and a light chain variable region comprising an amino acid sequence of SEQ ID NO: 14. In some embodiments, the internalizing antibody or internalizing antigen-binding Finngean Reference: 15648.0053-00304 fragment thereof that targets an FRA-expressing tumor cell comprises a human IgG1 heavy chain constant domain and an Ig kappa light chain constant domain. [00110] In some embodiments, the ADC has Formula I: Ab-(L-D)p (I) wherein: (i) Ab is an internalizing anti-folate receptor alpha (FRA) antibody or internalizing antigen-binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 20. [00111] In some embodiments, the internalizing antibody or internalizing antigen-binding fragment thereof comprises a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 13, and a light chain variable region comprising an amino acid sequence of SEQ ID NO: 14. In some embodiments, the internalizing antibody is MORAb-003. In some embodiments, p is from 1 to 8, or 1 to 6. In some embodiments, p is from 2 to 8, or 2 to 5. In some embodiments, p is from 3 to 4. In some embodiments, p is 4. Drug Moieties [00112] In various embodiments, the drug moiety (D) of the ADCs disclosed herein, e.g., the ADC of formula I, is an anti-tubulin agent, e.g., eribulin. [00113] In some embodiments, the drug moiety is eribulin and the linker of the ADC is attached via the C-35 amine on eribulin. [00114] In various embodiments, the natural form of eribulin used for joining to the linker and antibody moiety is shown below: Finngean Reference: 15648.0053-00304 [00115] In certain embodiments, an ADC is prepared by reacting an intermediate, which is the precursor of a linker, with eribulin under appropriate conditions. In certain embodiments, reactive groups are used on eribulin and/or the intermediate or linker. The product of the reaction between eribulinand the intermediate is subsequently reacted with an anti-FRA antibody or antigen-binding fragment under appropriate conditions. Alternatively, the linker or intermediate may first be reacted with the antibody or a derivatized antibody, and then reacted with eribulin. [00116] A number of different reactions are available for covalent attachment of eribulin and/or linkers to the antibody moiety. This is often accomplished by reaction of one or more amino acid residues of the antibody molecule, e.g., the sulfhydryl groups of cysteine. For instance, non-specific covalent attachment may be undertaken using a carbodiimide reaction to link a carboxy (or amino) group on a compound to an amino (or carboxy) group on an antibody moiety. Additionally, bifunctional agents such as dialdehydes or imidoesters may also be used to link the amino group on a compound to an amino group on an antibody moiety. Also available for attachment of drugs to binding agents is the Schiff base reaction. This method involves the periodate oxidation of a drug that contains glycol or hydroxy groups, thus forming an aldehyde which is then reacted with the binding agent. Attachment occurs via formation of a Schiff base with amino groups of the binding agent. Isothiocyanates may also be used as coupling agents for covalently attaching drugs to binding agents. Other techniques are known to the skilled artisan and within the scope of the present disclosure. Drug Loading [00117] Drug loading is represented by p, and is also referred to herein as the drug-to-antibody ratio (DAR). Drug loading may range from 1 to 20 drug moieties per antibody moiety. In some embodiments, p is an integer from 1 to 20. In some embodiments, p is an integer from 1 to 10, 1 to 9, 1 to 8, 1 to 7, 1 to 6, 1 to 5, 1 to 4, 1 to 3, or 1 to 2. In some embodiments, p is an integer from 2 to 10, 2 to 9, 2 to 8, 2 to 7, 2 to 6, 2 to 5, 2 to 4, or 2 to 3. In some embodiments, p is an integer from 3 to 4. In other embodiments, p is 1, 2, 3, 4, 5, or 6, preferably 3 or 4. [00118] Drug loading may be limited by the number of attachment sites on the antibody moiety. In some embodiments, the linker moiety (L) of the ADC attaches to the antibody moiety through a chemically active group on one or more amino acid residues on the antibody moiety. For example, Finngean Reference: 15648.0053-00304 the linker may be attached to the antibody moiety via a free amino, imino, hydroxyl, thiol, or carboxyl group (e.g., to the N- or C-terminus, to the epsilon amino group of one or more lysine residues, to the free carboxylic acid group of one or more glutamic acid or aspartic acid residues, or to the sulfhydryl group of one or more cysteine residues). The site to which the linker is attached can be a natural residue in the amino acid sequence of the antibody moiety, or it can be introduced into the antibody moiety, e.g., by DNA recombinant technology (e.g., by introducing a cysteine residue into the amino acid sequence) or by protein biochemistry (e.g., by reduction, pH adjustment, or hydrolysis). [00119] In some embodiments, the number of drug moieties that can be conjugated to an anti-FRA antibody moiety is limited by the number of free cysteine residues. For example, where the attachment is a cysteine thiol group, an anti-FRA antibody may have only one or a few cysteine thiol groups, or may have only one or a few sufficiently reactive thiol groups through which a linker may be attached. Generally, antibodies do not contain many free and reactive cysteine thiol groups that may be linked to a drug moiety. Indeed, most cysteine thiol residues in antibodies exist as disulfide bridges. Over-attachment of linker-toxin to an antibody may destabilize the antibody by reducing the cysteine residues available to form disulfide bridges. Therefore, an optimal drug:antibody ratio should increase potency of the ADC (by increasing the number of attached drug moieties per antibody) without destabilizing the antibody moiety. In some embodiments, an optimal ratio may be about 3-4. [00120] In some embodiments, a linker attached to an antibody moiety through a Mal moiety provides a ratio of about 3-4. In some embodiments, a linker comprising a short spacer unit (e.g., a short PEG spacer unit such as (PEG)2) provides a ratio of about 3-4. In some embodiments, a linker comprising a peptide cleavable moiety provides a ratio of about 3-4. In some embodiments, an ADC comprising Mal-(PEG)2-Val-Cit-pAB-eribulin joined to an anti-FRA antibody such as MORAb-003 has a ratio of about 3-4. [00121] In some embodiments, an antibody moiety, e.g., MORAb-003, is exposed to reducing conditions prior to conjugation in order to generate one or more free cysteine residues. In some embodiments, the antibody may be reduced with a reducing agent such as dithiothreitol (DTT) or tris(2-carboxyethyl)phosphine (TCEP), under partial or total reducing conditions, to generate reactive cysteine thiol groups. In certain embodiments, the antibody may be subjected to denaturing conditions to reveal reactive nucleophilic groups on amino acid residues, such as lysine or cysteine. [00122] Where more than one nucleophilic group reacts with a drug-linker intermediate or a linker moiety reagent followed by drug moiety reagent, in a reaction mixture comprising multiple copies of the antibody moiety and linker moiety, then the resulting product may be a mixture of ADC compounds with a distribution of one or more drug moieties attached to each copy of the antibody moiety in the mixture. In some embodiments, the drug loading in a mixture of ADCs resulting from a conjugation reaction ranges from 1 to 20 drug moieties attached per antibody moiety. The average number of drug moieties per antibody moiety (i.e., the average drug loading, or average p) may be Finngean Reference: 15648.0053-00304 calculated by any conventional method known in the art, e.g., by mass spectrometry (e.g., reverse- phase LC-MS), and/or high-performance liquid chromatography (e.g., HIC-HPLC). In some embodiments, the average number of drug moieties per antibody moiety is determined by hydrophobic interaction chromatography-high performance liquid chromatography (HIC-HPLC). In some embodiments, the average number of drug moieties per antibody moiety is determined by reverse-phase liquid chromatography-mass spectrometry (LC-MS). In some embodiments, the average number of drug moieties per antibody moiety is from about 3 to about 4; from about 3.1 to about 3.9; from about 3.2 to about 3.8; from about 3.2 to about 3.7; from about 3.2 to about 3.6; from about 3.3 to about 3.8; or from about 3.3 to about 3.7. In some embodiments, the average number of drug moieties per antibody moiety is from about 3.2 to about 3.8. In some embodiments, the average number of drug moieties per antibody moiety is about 3.8. In some embodiments, the average number of drug moieties per antibody moiety is from 3 to 4; from 3.1 to 3.9; from 3.2 to 3.8; from 3.2 to 3.7; from 3.2 to 3.6; from 3.3 to 3.8; or from 3.3 to 3.7. In some embodiments, the average number of drug moieties per antibody moiety is from 3.2 to 3.8. In some embodiments, the average number of drug moieties per antibody moiety is 3.8. [00123] In some embodiments, the average number of drug moieties per antibody moiety is from about 3.5 to about 4.5; from about 3.6 to about 4.4; from about 3.7 to about 4.3; from about 3.7 to about 4.2; or from about 3.8 to about 4.2. In some embodiments, the average number of drug moieties per antibody moiety is from about 3.6 to about 4.4. In some embodiments, the average number of drug moieties per antibody moiety is about 4.0. In some embodiments, the average number of drug moieties per antibody moiety is from 3.5 to 4.5; from 3.6 to 4.4; from 3.7 to 4.3; from 3.7 to 4.2; or from 3.8 to 4.2. In some embodiments, the average number of drug moieties per antibody moiety is from 3.6 to 4.4. In some embodiments, the average number of drug moieties per antibody moiety is 4.0. [00124] In various embodiments, the term “about” as used with respect to the average number of drug moieties per individual antibody moiety or within a mixture of ADCs, means +/- 10%. It should be understood that this definition of “about” applies to all descriptions of average number of drug moieties per individual antibody moiety or within a mixture of ADCs, within the present disclosure. [00125] Individual ADC compounds having particular DAR ratios, or “species,” may be identified in the mixture by mass spectroscopy and separated by UPLC or HPLC, e.g., hydrophobic interaction chromatography (HIC-HPLC). In certain embodiments, a homogeneous or nearly homogenous ADC with a single loading value may be isolated from the conjugation mixture, e.g., by electrophoresis or chromatography. [00126] In some embodiments, drug loading and/or average drug loading in an ADC (e.g., in MORAb-202) is about 4. In some embodiments, a drug loading and/or an average drug loading of about 4 provides beneficial properties. See, e.g., PCT/US2017/020529 (published as WO 2017/151979), which is incorporated herein by reference in its entirety. Finngean Reference: 15648.0053-00304 [00127] In some embodiments, an ADC has Formula I: Ab-(L-D)p (I) wherein: (i) Ab is an internalizing anti-folate receptor alpha antibody or antigen-binding fragment thereof comprising a heavy chain variable region comprising an amino acid sequence of SEQ ID NO: 13, and a light chain variable region comprising an amino acid sequence of SEQ ID NO: 14; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8. [00128] In some embodiments, an ADC has Formula I: Ab-(L-D)p (I) wherein: (i) Ab is an internalizing anti-folate receptor alpha antibody or antigen-binding fragment thereof comprising a heavy chain amino acid sequence of SEQ ID NO: 15, and a light chain amino acid sequence of SEQ ID NO: 16; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer of about 4. Therapeutic Uses [00129] In various embodiments, disclosed herein are methods of using the disclosed anti-FRA ADCs, e.g., ADCs comprising the the six CDR amino acid sequences of MORAb-003 attached to a linker comprising Mal-(PEG)2-Val-Cit-pAB, e.g., MORAb-202, in treating a subject for a disorder, e.g., an oncologic disorder, e.g., a FRA-expressing cancer such as ovarian cancer (e.g., platinum- resistant ovarian cancer). ADCs may be administered alone or in conjunction (e.g., simultaneously or sequentially) with a second therapeutic agent (e.g., a corticosteroid, e.g., dexamethasone, prednisone, or methylprednisolone), and may be administered in any pharmaceutically acceptable formulation. In particular, the methods disclosed herein provide uses of the disclosed anti-FRA ADCs for treating a subject having an FRA-expressing cancer, wherein the dosage of the ADC is based on the subject’s body surface area (BSA). In some embodiments, methods of treatment employing a BSA-dosing may reduce risk of interstitial lung disease (ILD) in a subject in need of treatment with an anti-FRA ADC. In some embodiments, the methods disclosed herein provide uses of the disclosed anti-FRA ADCs for treating a subject who has previously received at least one systemic anticancer therapy (e.g., cytotoxic Finngean Reference: 15648.0053-00304 or targeted anti-cancer agent). In some embodiments, the methods disclosed herein provide uses of the disclosed anti-FRA ADCs for treating a subject with a metastatic cancer, e.g., a metastatic non-small cell lung cancer. In some embodiments, a subject with a metastatic non-small cell lung cancer treated according to the disclosed methods has no genomic alterations. In some embodiments, a subject with a metastatic FRA-expressing cancer (e.g., a metastatic non-small cell lung cancer) has at least one genomic alteration (e.g., at least one unknown or known genomic alteration). Examples of known genomic alterations include, but are not limited to, genomic alterations in any one of the following genes: EGFR, ALK, PI3K, AKT, mTOR, RET, MET, BRAF, NTRK, ROS1, and any gene involved in the RAS-MAPK pathway. In some embodiments, a subject with a metastatic FRA-expressing cancer has at least one known genomic alteration in at least one of any of the aforementioned genes. As used herein, “genomic alteration” refers to any change to the genome, including, but not limited to, a somatic mutation, a copy number variation, and a gene fusion. In some embodiments, the methods disclosed herein provide uses of the disclosed anti-FRA ADCs for treating a subject with a refractory cancer. As used herein, a “refractory cancer” is a cancer that is non-responsive, i.e., that has not responded, to at least one prior therapy. In some embodiments, a subject with a refractory cancer is non-responsive to a targeted treatment, e.g., a treatment specifically targeted against any one of the following genes or variants thereof: epidermal growth factor receptor (EGFR), anaplastic lymphoma kinase (ALK), v-raf murine sarcoma viral oncogene homolog 1 (BRAF), ret proto-oncogene (RET), MET proto-oncogene, receptor tyrosine kinase (MET), neurotrophic receptor tyrosine kinase (NTRK) and receptor tyrosine kinase (ROS1). As used herein, a “targeted treatment” is a cancer treatment that targets certain genes and/or proteins that are involved in the growth and/or survival of cancer cells. As used herein, the term “variant” is used to refer to any naturally-occurring variant of a gene, including but not limited to splice variants, allelic variants, isoforms, and homologs (e.g., paralogs or orthologs). In contrast to a gene comprising a genomic alteration, a variant of a gene is not linked to or associated with a disease or disorder, e.g., a cancer. In some embodiments, any one of the aforementioned genes (or variants thereof) against which a targeted treatment is specifically targeted may comprise at least one genomic alteration. For example, a targeted treatment may be specific against a mutation in NTRK1, while another targeted treatment may be specific against a mutation in NTRK2. [00130] In some embodiments, a subject with a refractory cancer is non-responsive to a platinum- based treatment (e.g., platinum-doublet chemotherapy) and/or an immunotherapy-based treatment (e.g., an immune checkpoint inhibitor, e.g., a PD-1 inhibitor or a PD-L1 inhibitor). In some embodiments, a subject with a refractory cancer is non-responsive to treatment with platinum-doublet chemotherapy and an immune checkpoint inhibitor (e.g., a PD-1 inhibitor or a PD-L1 inhibitor), wherein the platinum-doublet chemotherapy and immune checkpoint inhibitor are administered concurrently or sequentially. In various embodiments, a subject with a refractory cancer is non- responive to not more than 3 prior systemic therapies, e.g., not more than 2 prior systemic therapies. Finngean Reference: 15648.0053-00304 In some embodiments, a subject with a refractory cancer is non-responsive to not more than 1 prior chemotherapy. [00131] In various embodiments, ADC treatment efficacy may be evaluated by measuring one or more biomarkers. In some embodiments, treatment is adjusted accordingly based on detected levels or changes in biomarker levels. As explained in more detail beow, in some embodiments, one or more biomarkers are measured before administration of an ADC and after administration of the ADC. In some embodiments, any change in the level of the one or more biomarkers is indicative of treatment efficacy. In some embodiments, treatment is adjusted after evaluating a change in biomarker before and after administration of the ADC (e.g., altering the dose or dosing regimen of an ADC, continuing treatment with an ADC, or discontinuing treatment). In some embodiments, ADC treatment efficacy may be evaluated for toxicity or other indicators of efficacy in conjunction with the measurement of one or more of the biomarkers disclosed herein. Efficacy measures include, but are not limited to, objective response rate (ORR). ORR may be measured after a given time period after treatment, e.g., at or after 24 weeks after the start of treatment. ORR may be determined based on tumor assessments according to RECIST, e.g., RECIST 1.1. As used herein, “RECIST” refers to the Response Evaluation Criteria in Solid Tumors (RECIST), a set of standardized guidelines used to measure how well a cancer patient responds to a treatment (Therass et al. (2000) J Natl Cancer Inst.92:205-16). As used herein, “RECIST 1.1” refers to version 1.1 of RECIST, in which the guidelines are revised and updated relative to an earlier version of RECIST (Eisenhauer et al. (2009) Eur J Cancer.45:228-47). [00132] In some embodiments, the methods disclosed herein for treating a FRA-expressing cancer comprise administering to a subject in need thereof a therapeutically effective amount of an ADC of Formula (I) as disclosed herein, e.g., MORAb-202, wherein the ADC is administered to the subject at a dose based on the subject’s body surface area (BSA). [00133] In some embodiments, the methods disclosed herein for reducing risk of ILD in a subject being treated for an FRA-expressing cancer comprise administering to the subject an ADC of Formula (I) as disclosed herein, e.g., MORAb-202, wherein the ADC is administered to the subject at a dose based on the subject’s BSA. [00134] In some embodiments, an ADC disclosed herein, e.g., MORAb-202, is administered at a dose of 0.3-1.2 mg/kg. In some embodiments, the ADC is administered at a dose of 0.3 mg/kg. In some embodiments, the ADC is administered at a dose of 0.45 mg/kg. In some embodiments, the ADC is administered at a dose of 0.68 mg/kg. In some embodiments, the ADC is administered at a dose of 0.9 mg/kg. In some embodiments, the ADC is administered at a dose of 1.2 mg/kg. [00135] In some embodiments, an ADC disclosed herein, e.g., MORAb-202, is administered at a dose of 8 mg to 50 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 8 mg to 44 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 11 mg to 44 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 8 mg to 10 mg per square Finngean Reference: 15648.0053-00304 meter (m2) of the subject’s BSA. In some embodiments, the dose is 5-75, 10-60, 15-45, or 20-40, or 25-35 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 33 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 25 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 17 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 15 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 12 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 10 mg per square meter (m2) of the subject’s BSA. In some embodiments, the ADC is administered at a dose of 8 mg per square meter (m2) of the subject’s BSA. Any of these doses may be administered once per week, once every two weeks, or once every three weeks. [00136] BSA may be calculated using any accepted method known in the art. Formulas for calculating a subject’s body surface area (BSA) include, for example, the Dubois and Dubois formula (or any variation thereof) (Dubois D, Dubois EF. (1916) Arch Intern Med.1916; 17:863-871), the Mosteller formula (or any variation thereof) (Mosteller RD. (1987) N Engl J Med.22;317(17):1098), or the Haycock formula (Haycock GB et al. (1978) J Pediatr. Jul;93(1):62-6). Exemplary formulas for calculating BSA are provided below: (II) BSA (m2) = 0.20247 × Height (m)0.725 × Weight (kg)0.425 (DuBois and DuBois); (III) BSA (m2) = 0.007184 × Height (cm)0.725 × Weight (kg)0.425 (variation of Dubois and Dubois); (IV) BSA (m2) = ([Height (cm) × Weight (kg)]/3600)½ (Mosteller); or (V) BSA (m2) = 0.024265 × Height (cm)0.3964 × BW (kg)0.5378 (Haycock). [00137] In some embodiments, the actual dose of the ADC to be administered to a subject may be calculated as shown below: (VI) Scheduled dose (mg/m2) × body surface area (BSA) (m2) = Actual dose (mg) As used herein, “scheduled dose” refers to a dose selected from the range of doses provided above, e.g., 8 mg to 50 mg, to be administered to a subject. For example, the ADC may be administered at a scheduled dose of 33 mg/m2 to a subject with an exemplary BSA of 1.8 square meters (m2), as calculated by Formula III above using hypothetical values of a height of 160 cm and a BW of 80 kg. In this particular example, according to Formula VI provided above, the amount of ADC administered to the subject, or actual dose, is 60.5 mg. [00138] In some embodiments, the treatment dose may be recalculated on the first day of each treatment cycle, using the subject’s height measured at intake, and the subject’s weight measured on or prior to the first day of each treatment cycle, e.g., two days prior to the first day of each treatment cycle. Finngean Reference: 15648.0053-00304 [00139] In some embodiments, the ADC is administered weekly, every two weeks, every three weeks, monthly, or any time period in between. In some embodiments, the ADC is administered once every three weeks. In some embodiments, the ADC may be administered on a 21-day cycle. A treatment cycle of once every three weeks or a 21-day cycle may also be referred to as “Q3W.” In some embodiments, the ADC is administered once every two weeks. In some embodiments, the ADC may be administered on a 14-day cycle. A treatment cycle of once every two weeks or a 14-day cycle may also be referred to as “Q2W.” In some embodiments, the ADC is administered once per week. In some embodiments, the ADC may be administered on a 7-day cycle. A treatment cycle of once per week or a 7-day cycle may also be referred to as “QW.” [00140] In some embodiments, the ADC is administered once every three weeks at a bodyweight- dose of 0.3-1.2 mg/kg. In some embodiments, the ADC is administered once every three weeks at a dose of 0.3-1.2 mg/kg. In some embodiments, the ADC is administered once every three weeks at a dose of 0.3 mg/kg. In some embodiments, the ADC is administered once every three weeks at a dose of 0.45 mg/kg. In some embodiments, the ADC is administered once every three weeks at a dose of 0.68 mg/kg. In some embodiments, the ADC is administered once every three weeks at a dose of 0.9 mg/kg. In some embodiments, the ADC is administered once every three weeks at a dose of 1.2 mg/kg. [00141] In some embodiments, the ADC is administered once every three weeks at a BSA- dependent dose of 8 mg/m2 to 50 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA-dependent dose of 8 mg/m2 to 50 mg/m2. In some embodiments, the ADC is administered once per week at a BSA-dependent dose of 8 mg/m2 to 50 mg/m2. In some embodiments, the ADC is administered once every three weeks at a BSA-dependent dose of 33 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA-dependent dose of 33 mg/m2. In some embodiments, the ADC is administered once per week at a BSA- dependent dose of 33 mg/m2. In some embodiments, the ADC is administered once every three weeks at a BSA-dependent dose of 17 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA-dependent dose of 17 mg/m2. In some embodiments, the ADC is administered once per week at a BSA-dependent dose of 17 mg/m2. In some embodiments, the ADC is administered once every three weeks at a BSA-dependent dose of 15 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA-dependent dose of 15 mg/m2. In some embodiments, the ADC is administered once per week at a BSA-dependent dose of 15 mg/m2. In some embodiments, the ADC is administered once every three weeks a BSA-dependent dose of 8 mg/m2 to 10 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA- dependent dose of 8 mg/m2 to 10 mg/m2. In some embodiments, the ADC is administered once per week at a BSA-dependent dose of 8 mg/m2 to 10 mg/m2. In some embodiments, the ADC is administered once every three weeks at a BSA-dependent dose of 10 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA-dependent dose of 10 mg/m2. In some Finngean Reference: 15648.0053-00304 embodiments, the ADC is administered once per week at a BSA-dependent dose of 10 mg/m2. In some embodiments, the ADC is administered once every three weeks at a BSA-dependent dose of 8 mg/m2. In some embodiments, the ADC is administered once every two weeks at a BSA-dependent dose of 8 mg/m2. In some embodiments, the ADC is administered once per week at a BSA-dependent dose of 8 mg/m2. In some embodiments, the ADC is administered on the first day and the eighth day of every three-week cycle at a BSA-dependent dose of 12 mg/m2. [00142] In some embodiments, a subject treated with an anti-FRA ADC as disclosed herein has a body weight value that is in the upper quartile of weight. In some embodiments, a subject treated with an anti-FRA ADC as disclosed herein has a body weight of at least 80 kg. [00143] In some embodiments, a risk of ILD in a subject treated with an anti-FRA ADC as disclosed herein is reduced by at least 5%, at least 10%, at least 15%, at least 16%, at least 17%, at least 18%, at least 19%, or at least 20% following administration of the ADC at a BSA-based dose, as compared to a treatment in which the ADC is administered on a body weight (BW)-based dose. In some embodiments, the comparative treatment is administered at a dose of 0.5 to 2 mg per kilogram of the subject’s body weight (BW), e.g., at a dose of 0.9 mg to 1.2 mg per kilogram of BW. For example, in some embodiments, a comparative treatment may be administered at a dose of 0.9 mg per kilogram of a subject’s BW, which is comparable to a dose of 33 mg per square meter of the subject’s BSA. In some embodiments, for a subject with an exemplary BW of 80 kg, administration of the ADC at a BW-based dose of 0.9 mg/kg would result in an actual dose of 72 mg; in comparison, administration of the ADC to the same subject at a BSA-based dose of 33 mg/m2 would result in an actual dose of 59.4 mg. [00144] In some embodiments, the methods as disclosed herein may further comprise administration of one or more additional therapeutic agents, e.g., one or more additional oncologic agents. In some embodiments, the additional agent comprises a corticosteroid. [00145] In some embodiments, a corticosteroid may be administered prophylactically. As used herein, “administered prophylactically” refers to the administration of a treatment, e.g., a corticosteroid, to a subject prior to the subject having or developing symptoms of ILD. In some embodiments, a corticosteroid is administered concurrently or sequentially with an ADC. In some embodiments, a corticosteroid is administered before or after an ADC is administered. In some embodiments, a corticosteroid is dexamethasone. In some embodiments, a corticosteroid is prednisone. In some embodiments, a corticosteroid is methylprednisolone. In some embodiments, the corticosteroid (e.g., dexamethasone, prednisone, or methylprednisolone), may be administered orally or intravenously. In some embodiments, when the corticosteroid (e.g., dexamethasone or prednisone) is administered orally, it may be administered in an amount of 1-10 mg, e.g., 0.5-2 mg, e.g., 2-5 mg, e.g., at 0.5 mg, at 1 mg, at 2 mg, or at 4 mg. In some embodiments, the dexamethasone is administered at a dose determined to be therapeutically effective, e.g., at 4 mg of dexamethasone. In some embodiments, the dexamethasone is administered at least once a day, e.g., two times a day. In Finngean Reference: 15648.0053-00304 some embodiments, the dexamethasone is administered for several days (e.g., 1, 2, 3, 4, 5, or more) before or at the start of treatment with an ADC. In some embodiments, the dexamethasone is administered for at least three days at the start of treatment with an ADC. In some embodiments, the dexamethasone is administered orally. In some embodiments, the prednisone is administered at a dose determined to be therapeutically effective, e.g., at 0.5 mg, at 1 mg, or at 2 mg of prednisone. In some embodiments, the prednisone is administered at 0.5 mg of prednisone. In some embodiments, the prednisone is administered at 1 mg of prednisone. In some embodiments, the prednisone is administered at 2 mg of prednisone. In some embodiments, the prednisone is administered at least once a day. In some embodiments, the prednisone is administered for several days (e.g., 10, 11, 12, 13, 14, or more) before or at the start of treatment with an ADC. In some embodiments, the prednisone is administered for at least 14 days before the start of treatment with an ADC. In some embodiments, the prednisone is administered orally. In some embodiments, when the corticosteroid (e.g., methylprednisolone) is administered intravenously, it may be administered in an amount of 300- 1200 mg, e.g., 400-1100 mg, e.g., 500-1000 mg, e.g., at 500 mg, at 750 mg, or at 1000 mg. In some embodiments, the methylprednisolone is administered in an amount of 30-130 mg, e.g., 40-125 mg. In some embodiments, the methylprednisolone is administered at 1 mg per kg of a subject’s body weight. In some embodiments, the methylprednisolone is administered at 2 mg per kg of a subject’s body weight. In some embodiments, the methylprednisolone is administered intravenously. In some embodiments, the methylprednisolone is administered orally. In some embodiments, when the methylprednisolone is administered orally, it may be administered in an amount of 5-100 mg, e.g., 5- 90 mg, e.g., 5-80 mg, e.g., 10-80 mg, e.g., e.g., 10-70 mg, e.g., 10-60 mg. In some embodiments, the methylprednisolone is administered orally at 0.5-1.5 mg per kg of a subject’s body weight. In some embodiments, the methylprednisolone is administered orally at 0.5 mg per kg of a subject’s body weight. In some embodiments, the methylprednisolone is administered orally at 1 mg per kg of a subject’s body weight. In some embodiments, the methylprednisolone is administered orally at 1.5 mg per kg of a subject’s body weight. In some embodiments, the methylprednisolone is administered at least once a day. In some embodiments, the methylprednisolone is administered for several days (e.g., 1, 2, 3, 4, 5, or more) before or at the start of treatment with an ADC. In some embodiments, the methylprednisolone is administered for at least three days before the start of treatment with an ADC. [00146] The methods of the present disclosure may be applied to a human subject in need of treatment, e.g., a subject suffering from a cancer, e.g., an FRA-expressing cancer. In some embodiments, the methods disclosed herein may be applied to a non-human mammal having an FRA- expressing cancer for veterinary purposes or as an animal model of human disease. Regarding the latter, such animal models may be useful for evaluating the therapeutic efficacy of the disclosed methods (e.g., testing of dosages and time courses of administration). Finngean Reference: 15648.0053-00304 [00147] The ADCs disclosed herein may be administered to a subject by any suitable administration route to have a therapeutic effect. In some embodiments, the ADC is administered to a subject intravenously. [00148] In some embodiments, the present disclosure features a method of treating a cancer that expresses FRA. The method may be used to treat any human or non-human mammal subject having an FRA-expressing cancer, e.g., those where disruption of tubulin provides a therapeutic benefit. Methods for identifying subjects having cancers that express FRA are known in the art and may be used to identify suitable subjects for treatment with a disclosed ADC. An FRA-expressing cancer may be a primary or metastatic FRA-expressing cancer, or an FRA-expressing cancer which is resistant to a platinum-based therapy, e.g., a platinum resistant cancer. Non-limiting examples of FRA-expressing cancers include gastric cancer, ovarian cancer (e.g., serous ovarian cancer, clear cell ovarian cancer, or platinum resistant ovarian cancer), lung cancer (e.g., non-small cell lung cancer, e.g., metastatic non-small cell lung cancer), lung carcinoid, colorectal cancer, breast cancer (e.g., triple negative breast cancer or hormone receptor (HR)-positive and HER2-low breast cancer), endometrial cancer (e.g., serous endometrial carcinoma), peritoneal cancer (e.g., primary peritoneal cancer), fallopian tube cancer, pancreatic cancer, kidney cancer (e.g., renal cell cancer), cervical cancer, esophageal cancer, and osteosarcoma. [00149] In some embodiments, the FRA-expressing cancer is gastric cancer, ovarian cancer, serous ovarian cancer, serous high-grade ovarian cancer, clear cell ovarian cancer, platinum resistant ovarian cancer, lung cancer, non-small cell lung cancer, metastatic non-small cell lung cancer, lung carcinoid, colorectal cancer, breast cancer, triple negative breast cancer, hormone receptor (HR)-positive and HER2-low breast cancer, endometrial cancer, serous endometrial carcinoma, peritoneal cancer, primary peritoneal cancer, fallopian tube cancer, pancreatic cancer, kidney cancer, renal cell cancer, cervical cancer, esophageal cancer, osteosarcoma, chorid plexus carcinoma ependymoma, epedymoblastoma, medulloblastoma, Wilms tumor, acute myeloid leukemia, or head and neck cancer. [00150] In some embodiments, the FRA-expressing cancer is gastric cancer, ovarian cancer, serous ovarian cancer, serous high-grade ovarian cancer, clear cell ovarian cancer, platinum resistant ovarian cancer, lung cancer, non-small cell lung cancer, metastatic non-small cell lung cancer, lung carcinoid, breast cancer, triple negative breast cancer, hormone receptor (HR)-positive and HER2-low breast cancer, endometrial cancer, serous endometrial carcinoma, peritoneal cancer, primary peritoneal cancer, fallopian tube cancer, pancreatic cancer, cervical cancer, esophageal cancer, osteosarcoma, chorid plexus carcinoma ependymoma, epedymoblastoma, medulloblastoma, Wilms tumor, acute myeloid leukemia, or head and neck cancer. [00151] In some embodiments, the FRA-expressing cancer is gastric cancer, ovarian cancer, serous ovarian cancer, serous high-grade ovarian cancer, clear cell ovarian cancer, platinum resistant ovarian cancer, lung cancer, non-small cell lung cancer, metastatic non-small cell lung cancer, lung carcinoid, colorectal cancer, breast cancer, triple negative breast cancer, hormone receptor (HR)-positive and Finngean Reference: 15648.0053-00304 HER2-low breast cancer, endometrial cancer, serous endometrial carcinoma, peritoneal cancer, primary peritoneal cancer, fallopian tube cancer, pancreatic cancer, kidney cancer, renal cell cancer, cervical cancer, esophageal cancer, osteosarcoma, and head and neck cancer. [00152] In some embodiments, the FRA-expressing cancer is ovarian cancer, e.g., platinum resistant ovarian cancer. In some embodiments, the FRA-expressing cancer is breast cancer, e.g., triple negative breast cancer (TNBC). In some embodiments, the FRA-expressing cancer is non-small cell lung cancer (NSCLC), e.g., metastatic non-small cell lung cancer. In some embodiments, the FRA- expressing cancer is endometrial cancer. [00153] In some embodiments, the present disclosure features a method of reducing risk of ILD in a subject having an FRA-expressing cancer, wherein the subject is in need of treatment. The method may be used with any human or non-human mammal subject having an FRA-expressing cancer for the purpose of reducing ILD risk. An FRA-expressing cancer may be a primary or metastatic FRA- expressing cancer, or an FRA-expressing cancer which is resistant to a platinum-based therapy, e.g., a platinum resistant cancer. Non-limiting examples of FRA-expressing cancers include gastric cancer, ovarian cancer (e.g., serous ovarian cancer, clear cell ovarian cancer, or platinum resistant ovarian cancer), lung cancer (e.g., non-small cell lung cancer, e.g., metastatic non-small cell lung cancer), lung carcinoid, colorectal cancer, breast cancer (e.g., triple negative breast cancer or hormone receptor (HR)-positive and HER2-low breast cancer), endometrial cancer (e.g., serous endometrial carcinoma), peritoneal cancer (e.g., primary peritoneal cancer), fallopian tube cancer, pancreatic cancer, kidney cancer (e.g., renal cell cancer), cervical cancer, esophageal cancer, and osteosarcoma. In some embodiments, the FRA-expressing cancer is ovarian cancer, e.g., platinum resistant ovarian cancer. In some embodiments, the FRA-expressing cancer is breast cancer, e.g., triple negative breast cancer (TNBC). In some embodiments, the FRA-expressing cancer is non-small cell lung cancer (NSCLC), e.g., metastatic non-small cell lung cancer. In some embodiments, the FRA-expressing cancer is endometrial cancer. [00154] In various embodiments, the methods disclosed herein, e.g., the BSA-based dosing using an anti-FRA ADC such as MORAb-202, e.g., at a BSA-dependent dose of 8 to 50 mg/m2, are used to treat an ovarian cancer, platinum resistant ovarian cancer, breast cancer, triple negative breast cancer, non-small cell lung cancer, or endometrial cancer. In some embodiments, the methods disclosed herein are used to treat a primary peritoneal cancer or fallopian tube cancer. In some embodiments, a BSA-dependent dose of 33 mg/m2 administered once every three weeks (Q3W) is used to treat a platinum resistant ovarian cancer (PROC). In some embodiments, a BSA-dependent dose of 25 mg/m2 administered Q3W is used to treat a PROC. In some embodiments, a BSA-dependent dose of 17 mg/m2 administered Q3W is used to treat a PROC. In some embodiments, a BSA-dependent dose of 15 mg/m2 administered once every two weeks (Q2W) is used to treat a PROC. In some embodiments, a BSA-dependent dose of 8 mg/m2 to 10 mg/m2 administered once per week (QW) is used to treat a PROC. In some embodiments, the PROC is a serous ovarian cancer. In some embodiments, the PROC Finngean Reference: 15648.0053-00304 is a high-grade serous ovarian cancer. In some embodiments, a BSA-based dose of 33 mg/m2 Q3W is used to treat a primary peritoneal cancer. In some embodiments, a BSA-based dose of 25 mg/m2 Q3W is used to treat a primary peritoneal cancer. In some embodiments, a BSA-based dose of 17 mg/m2 Q3W is used to treat a primary peritoneal cancer. In some embodiments, a BSA-based dose of 15 mg/m2 Q2W is used to treat a primary peritoneal cancer. In some embodiments, a BSA-based dose of 8 mg/m2 to 10 mg/m2 QW is used to treat a primary peritoneal cancer. In some embodiments, a BSA- based dose of 33 mg/m2 Q3W is used to treat a fallopian tube cancer. In some embodiments, a BSA- based dose of 25 mg/m2 Q3W is used to treat a fallopian tube cancer. In some embodiments, a BSA- based dose of 17 mg/m2 Q3W is used to treat a fallopian tube cancer. In some embodiments, a BSA- based dose of 15 mg/m2 Q2W is used to treat a fallopian tube cancer. In some embodiments, a BSA- based dose of 8 mg/m2 to 10 mg/m2 QW is used to treat a fallopian tube cancer. In some embodiments, a subject treated according to the methods disclosed herein has a cancer which recurred within six months of receiving platinum-based therapy. [00155] In some embodiments, a subject who experiences a treatment-related adverse event (TRAE) may be subsequently administered a reduced dose level of MORAb-202. In some embodiments, a subject who is administered a BSA-based dose of 33 mg/m2 and experiences a TRAE may be subsequently administered a reduced dose of 25 mg/m2. In some embodiments, a subject who is administered a BSA-based dose of 25 mg/m2 and experiences a TRAE may be subsequently administered a reduced dose of 17 mg/m2. In some embodiments, a subject who is administered a BSA-based dose of 25 mg/m2 and experiences a TRAE may be subsequently administered a reduced dose of 15 mg/m2. In some embodiments, a subject who is administered a BSA-based dose of 25 mg/m2 and experiences a TRAE may be subsequently administered a reduced dose of 8 mg/m2 to 10 mg/m2. In some embodiments, a subject who is administered a BSA-based dose of 15 mg/m2 and experiences a TRAE may be subsequently administered a reduced dose of 8 mg/m2 to 10 mg/m2. In some embodiments, a TRAE is assessed according to NCI CTCAE v5 and assigned a certain grade level. As used herein, NCI CTCAE v5 refers to version 5 of the National Cancer Institute Common Terminology Criteria for Adverse Events, a descriptive terminology which is utilized for adverse event reporting, wherein a grading (severity) scale is provided for each adverse event term. In some embodiments, a TRAE is an infusion-related reaction of Grade 1 or higher (e.g., Grade 2, 3, or 4). In some embodiments, a TRAE is interstitial lung disease (ILD) or pneumonitis of Grade 1 or higher (e.g., Grade 2, 3, 4). In some embodiments, a TRAE is a decrease in neutrophil count of Grade 3 or 4 or equal to or below 1000 cells/µl of the subject’s blood sample. In some embodiments, a TRAE is febrile neutropenia of Grade 3 or higher. In some embodiments, a TRAE is a decrease in platelet count of Grade 2 or higher or equal to or below 75,000 cells/µl of the subject’s blood sample. In some embodiments, a TRAE is any symptomatic or asymptomatic laboratory result of Grade 3 or higher. In some embodiments, a TRAE is any non-hematologic toxicity of Grade 3 or higher. Finngean Reference: 15648.0053-00304 [00156] In some embodiments, the methods disclosed herein, e.g., the BSA-based dosing using an anti-FRA ADC such as MORAb-202, e.g., at a BSA-dependent dose of 8 to 50 mg/m2, reduces the risk of ILD. [00157] Prior to the start of treatment, subjects may be assessed by certain clinical criteria to identify those potentially at higher risk for severe respiratory complications. If a subject is determined to be potentially at higher risk for severe respiratory complications, the subject may be excluded from treatment with the methods disclosed herein. In some embodiments, a subject who is treated according to the foregoing methods is assessed by a pulmonary function test (PFT) prior to treatment. In some embodiments, a subject who is assessed by a PFT and subsequently treated does not have one or more of the following results: a FEV1/FVC ratio of less than 0.7, a FEV1 (forced expiratory volume in the first second) of less than 80%, a FVC (forced vital capacity) of less than 80%, or a DLCO (diffusing capacity of the lungs for carbon monoxide) of less than 80%. In some embodiments, a subject who is treated according to the foregoing methods does not have one or more of the following at the start of treatment: interstitial lung disease (ILD) and/or pneumonitis, a history of ILD and/or pneumonitis, a lung-specific clinically significant illness, pleural effusion, pericardial effusion, prior pneumonectomy, a history of chest radiotherapy within the past 2 years, autoimmune disorder with pulmonary involvement, connective tissue disorder with pulmonary involvement, or inflammatory disorder with pulmonary involvement. Exemplary lung-specific clinically significant illnesses include, but are not limited to, any underlying pulmonary disorder (e.g., pulmonary embolism), asthma, chronic obstructive pulmonary disease (COPD), restrictive lung disease, or any other lung-specific inflammatory disease or condition. [00158] In some embodiments, a subject who is treated according to the foregoing methods does not have one or more of the following: a history of more than three prior therapies for the FRA-expressing cancer, a high neutrophil-to-lymphocyte ratio, or a serum albumin level at the start of treatment of less than 3 g/dL. As used herein, a “high neutrophil-to-lymphocyte ratio” refers to a ratio of neutrophil cells to lymphocyte cells, or “neutrophil-to-lymphocyte ratio” (NLR), in a subject’s blood sample that is higher relative to an average NLR of a comparator population, e.g., a group of adults in a general population or a group of subjects with an FRA-expressing cancer. In some embodiments, a high NLR may be at least 3, at least 4, at least 5, at least 6, at least 7, at least 8, or at least 9. NLR may be calculated using any method known in the art. For example, NLR can be calculated by dividing the number of neutrophils by the number of lymphocytes. The number of neutrophils and number of lymphocytes may be measured from a subject’s peripheral blood sample. NLR may be calculated using absolute cell counts of neutrophils and/or lymphocytes, or using relative percentages of neutrophils and/or lymphocytes. Biomarkers of tumor response Finngean Reference: 15648.0053-00304 [00159] In various embodiments, one or more biomarkers of tumor response are measured in a subject in conjunction with the disclosed treatment methods, e.g., those using MORAb-202. In some embodiments, one or more biomarkers of tumor response is measured before and after administration of one or more doses of MORAb-202 to a subject. As used herein, “baseline” refers to a measurement at a timepoint before a specified intervention has occurred, e.g., the measured level of a biomarker of tumor response in a biological sample taken from a subject before administration of an ADC, e.g., MORAb-202. In some embodiments, comparing the baseline level of a biomarker and the biomarker level after administration of an ADC is used to evaluate treatment efficacy and/or to guide subsequent treatment decisions. [00160] Biomarkers are measureable substances in an organism that are indicators of a biological process. These measureable substances can include nucleic acids, proteins, or other aspects of cellular activity. Biomarkers of tumor response are measurable substances that are indicators of tumor biology. In some embodiments, biomarkers of tumor response are indicators of angiogenesis, cytokines, inflammation, and/or other aspects of cancer biology and growth. A physician or other medical practitioner can assess the impact of a drug or treatment on a subject with a tumor by assessesing one or more biomarkers of tumor response before and after administration of the drug or treatment, e.g., MORAb-202. Treatment decisions and changes in treatment, such as continuing or discontinuing treatment, may also be made after assessing the levels of one or more biomarkers of tumor response before and after administration of the drug or treatment, e.g., MORAb-202. A change in treatment can be made based on particular changes observed in biomarkers of tumor response, for example, a particular percent change in one or more biomarkers of tumor response after administration of a drug or treatment relative to a baseline level of the one or more biomarkers of tumor response. [00161] In various embodiments, a dose of a drug or treatment, e.g., MORAb-202, is administered to a subject with a tumor, and biological samples, e.g., blood samples, are collected before and after administration. In some embodiments, treatment efficacy is determined by measuring a change in one or more biomarkers of tumor response in the samples taken before and after administration of the drug or treatment (or, in some instances, the absence of a change indicates treatment efficacy, whereas a change indicates a lack of response to treatment). A dose of a drug or treatment refers to the quantity of the drug or treatment given at a particular time. One or multiple doses may be administered between a baseline biomarker sampling and a subsequent sampling. In some emboidments, after assessing the levels of one or more biomarkers of tumor response before and after administration of the drug or treatment, a physician can adjust the dose or frequency at which a drug or treatment, e.g., MORAb-202, is administered. In some emboidments, a change (or lack thereof) in the level of a biomarker associated with tumor response results in administering a larger dose of the drug or treatment. In some embodiments, a change (or lack thereof) in the level of a biomarker associated with tumor response results in administering a smaller dose of the drug or treatment. In some Finngean Reference: 15648.0053-00304 embodiments, a change (or lack thereof) in the level of a biomarker associated with tumor response results in administering a drug or treatment less frequently. In some embodiments, a change (or lack thereof) in the level of a biomarker associated with tumor response results in administering a drug or treatment more frequently. In some embodiments, treatment is continued if a change (or lack thereof) in the level of one or more biomarkers of tumor response is detected. In some embodiments, treatment is discontinued if a change (or lack thereof) in the level of one or more biomarkers of tumor response is detected. [00162] In some embodiments, a baseline level of one or more biomarkers of tumor response is measured in a biological sample taken from a subject prior to starting treatment with MORAb-202. In some embodiments, a further level of one or more biomarkers of tumor response is measured in a biological sample taken from a subject after treatment, e.g., with MORAb-202. In some embodiments, additional samples are taken, e.g., after additional doses of MORAb-202 have been administered. [00163] In some embodiments, the biological sample taken from a subject is blood, blood components, tumor biopsy, urine, tissue, cell collection, or saliva. Methods of obtaining such samples are known in the art and may be used herein. In some embodiments, the biological sample taken from a subject is processed before the biomarker of tumor response is measured in the biological sample. In some embodiments, levels of one or more biomarkers of tumor response in samples are measured using methods known in the art, such as a Luminex-based platform, an OLINK-based multiplexing technology platform, or a SIMOA-based assay platform. [00164] In some embodiments, after a baseline measurement of one or more biomarkers of tumor response is obtained, a drug or treatment is administered to the subject, e.g, a treatment disclosed herein. In some embodiments, after the drug or treatment is administered to the subject, an additional measurement of the biomarker of tumor response is measured in a biological sample taken from the subject. In some embodiments, the additional measurement of the one or more biomarkers of tumor response after administration of the drug or treatment is compared to the baseline measurement of the one or more biomarkers of tumor response. The comparison may be used to determine the effect of the drug or treatment on the tumor biology of the subject. In some embodiments, more than one additional measurement of the one or more biomarkers of tumor response are taken to monitor changes in biomarker levels over the course of treatment. In some embodiments, additional measurements of the biomarker of tumor response are taken from the subject on a regular basis. In some embodiments, additional measurements of the biomarker of tumor response are taken from the subject until a particular change in the level of biomarker of tumor response is obtained. In some embodiments, once a particular level has been obtained, treatment is discontinued. [00165] In various embodiments, the ADCs and treatment methods discussed above may be monitored and/or guided by the changes in one or more biomarkers measured in samples taken from a patient (e.g., before and after dosing with an ADC disclosed herein, e.g., MORAb-202). Finngean Reference: 15648.0053-00304 [00166] In some embodiments, an ADC is administered until a change in the level of a biomarker in a sample is observed relative to the level of the biomarker in a sample taken from the subject prior to administration. Without being bound by theory, biomarker changes may reflect processes associated with cancer or the tumor microenvironment. In some embodiments, the biomarker relates to angiogenesis, cytokines, inflammation, and/or cancer. [00167] In some embodiments, a level of a biomarker in a sample is increased relative to the level of the biomarker in a sample taken from the subject prior to administration (the baseline level). In some embodiments, treatment with the ADC is continued if the measured level of a biomarker is increased releative to the baseline level. In some embodiments, the level of a biomarker in a sample is decreased relative to the baseline level. In some embodiments, treatment with the ADC is continued if the measured level of a biomarker is decreased releative to the baseline level. [00168] A subject that receives a dose of an ADC, e.g., MORAb-202, may be a responder or nonresponder to the ADC treatment. Tumor response can be assessed by guidelines known in the art. In some embodiments, tumor response is assessed using Response Evaluation Criteria in Solid Tumors (RECIST) v1.1 guidelines. In some embodiments, tumor response as assessed by guidelines are used to determine the overall response rate of a subject or the best overall response rate of a subject. In some embodiments, the best overall response rate of a subject is either a complete response, partial response, steady disease, or progressive disease. In some embodiments, response may be supplemented or replaced by measurement of one or more of the biomarkers discussed herein. [00169] In some embodiments, a subject is a responder because, after receiving the ADC dose, the subject exhibits either a complete response or partial response to the ADC treatment. If a subject is a responder to the ADC treatment, in some embodiments the subject continues to receive the ADC treatment. In some embodiments, a subject is a nonresponder because after the ADC dose the subject exhibts either a stable disease state or progressive disease state. If a subject is a nonresponder to the ADC treatment, in some embodiments the subject discontinues the ADC treatment. In some embodiments, the nonresponder received a different dose of the ADC, e.g., MORAb-202. In some embodiments, the nonresponder subject is switched to a different tumor treatment. [00170] In some embodiments, the biomarker is surfactant protein D (SP-D, NCBI Gene ID: 6441, SEQ ID NO:39). In some embodiments, the level of SP-D is increased after administration of an ADC, e.g., MORAb-202, relative to the baseline level in a subject responding to treatment. In some embodiments, the level of SP-D is increased at least 80-120%, e.g., at least 100% relative to the baseline level in a subject responding to treatment. Without being bound by theory, an increase in SP- D after administration of an ADC may indicate an improvement in the tumor microenvironment, for example, reduced immune suppression and a reduction in cancer growth and metastasis. [00171] In some embodiments, the biomarker is a form of kallikrein related peptidase isoform. In some embodiments, the biomarker is kallikrein related peptidase 5 (KLK-5, NCBI Gene ID:25818, SEQ ID NO:40). In some embodiments, the level of KLK-5 is decreased after administration of an Finngean Reference: 15648.0053-00304 ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of KLK-5 is decreased at least 20-60%, e.g., at least 40% relative to the baseline level in a subject responding to treatment. In some embodiments, the biomarker is kallikrein related peptidase 7 (KLK-7, NCBI Gene ID:5650; SEQ ID NO:41). In some embodiments, the level of KLK-7 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of KLK-7 is decreased at least 10-40%, e.g., at least 30% relative to the baseline level in a subject responding to treatment. Without being bound by theory, decreases in KLK-5 and/or KLK-7 after administration of an ADC may indicate an improvement in the tumor microenvironment, for example, reduction in production of abnormal blood vessels, reduced immune suppression, reduction in tumorigenic stroma and extracellular matrix remodeling, and a reduction in cancer growth and metastasis. [00172] In some embodiments, the biomarker is a C-C motif chemokine ligand isoform. In some embodiments, the biomarker is C-C motif chemokine ligand 2 (MCP-1, NCBI Gene ID:6347, SEQ ID NO:42). In some embodiments, the level of MCP-1 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of MCP-1 is decreased at least 5-25%, e.g., at least 15% relative to the baseline level in a subject responding to treatment. Without being bound by theory, a decrease in MCP-1 after administration of an ADC may indicates an improvement in the tumor microenvironment, for example, reduction in production of abnormal blood vessels, improvement in the epithelial-mesenchymal transition, reduced immune suppression, and a reduction in cancer growth and metastasis. In some embodiments, the biomarker is C-C motif chemokine ligand 4 (MIP-1 β, NCBI Gene ID:6351, SEQ ID NO:43). In some embodiments, the level of MIP-1 β is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of MIP-1 β is increased in nonresponders after administration of an ADC relative to the baseline level. In some embodiments, the biomarker is C-C motif chemokine ligand 8 (CCL8, NCBI Gene ID:6355, SEQ ID NO:44). In some embodiments, the level of CCL8 is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of CCL8 is increased in nonresponders after administration of an ADC relative to the baseline level. In some embodiments, the biomarker is C-C motif chemokine ligand 10 (IP-10, NCBI Gene ID:3627, SEQ ID NO:45). In some embodiments, the level of IP-10 is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of IP-10 is increased in nonresponders after administration of an ADC relative to the baseline level. In some embodiments, the biomarker is C-C motif chemokine ligand 11 (Eotaxin-1, NCBI Gene ID:6356, SEQ ID NO:46). In some embodiments, the level of Eotaxin-1 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the biomarker is C-C motif chemokine ligand 13 (CCL13, NCBI Gene ID:6357, SEQ ID NO:47). In some embodiments, the level of CCL13 is unchanged after administration of an ADC relative to the baseline level in a Finngean Reference: 15648.0053-00304 subject responding to treatment, while the level of CCL13 is increased in nonresponders after administration of an ADC relative to the baseline level. [00173] In some embodiments, the biomarker is angiopoietin 2 (ANG-2, NCBI Gene ID:285, SEQ ID NO:48). In some embodiments, the level of ANG-2 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of ANG-2 is decreased at least 20-40%, e.g., at least 30% relative to the baseline level in a subject responding to treatment. Without being bound by theory, a decrease in ANG-2 after administration of an ADC may indicate an improvement in the tumor microenvironment, for example, reduction in production of abnormal blood vessels, reduction of hypoxia, and a reduction in cancer growth and metastasis. [00174] In some embodiments, the biomarker is matrix metallopeptidase 12 (MMP12, NCBI Gene ID:4321, SEQ ID NO:49). In some embodiments, the level of MMP12 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of MMP12 is decreased at least 20-60%, e.g., at least 40% relative to the baseline level in a subject responding to treatment. Without being bound by theory, a decrease in MMP12 after administration of an ADC may indicate an improvement in the tumor microenvironment, for example, a reduction in tumorigenic stroma and extracellular matrix remodeling and a reduction in cancer growth and metastasis. [00175] In some embodiments, the biomarker is ferritin (FRTN). In some embodiments, the ferritin is ferritin light chain (FTL, NCBI Gene ID:2512, SEQ ID NO:68). In some embodiments, the ferritin is ferritin heavy chain (FTH1, NCBI Gene ID:2495, SEQ ID NO:69). In some embodiments, the measured biomarker comprises a mixture of both the heavy and light chain of FRTN. In some embodiments, the level of FRTN is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of FRTN is decreased at least 20-60%, e.g., at least 40% relative to the baseline level in a subject responding to treatment. Without being bound by theory, a decrease in FRTN after administration of an ADC may indicate an improvement in the tumor microenvironment, for example, reduction in production of abnormal blood vessels, reduced immune suppression, and a reduction in cancer growth and metastasis. [00176] In some embodiments, the biomarker is an insulin like growth factor binding protein isoform. In some embodiments, the biomarker is insulin like growth factor binding protein 1 (IGFBP- 1, NCBI Gene ID:3484, SEQ ID NO:51). In some embodiments, the level of IGFBP-1 is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of IGFBP-1 is increased in nonresponders after administration of an ADC relative to the baseline level. In some embodiments, the biomarker is insulin like growth factor binding protein 2 (IGFBP-2, NCBI Gene ID:3485, SEQ ID NO:52). In some embodiments, the level of IGFBP-2 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the level of IGFBP-2 is decreased at least 20-40%, e.g., at least 30% Finngean Reference: 15648.0053-00304 relative to the baseline level in a subject responding to treatment. Without being bound by theory, a decrease in IGFBP-2 after administration of an ADC may indicate an improvement in the tumor microenvironment, for example, reduction in production of abnormal blood vessels, improvement in the epithelial-mesenchymal transition, reduced immune suppression, and a reduction in cancer growth and metastasis. [00177] In some embodiments, the biomarker is fms related receptor tyrosine kinase 3 ligand (FLT3LG, NCBI Gene ID:2323, SEQ ID NO:53). In some embodiments, the level of FLT3LG is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of FLT3LB is increased in nonresponders after administration of an ADC relative to the baseline level. [00178] In some embodiments, the biomarker is a vascular endothelial growth factor isoform. In some embodiments, the biomarker is vascular endothelial growth factor (VEGF, NCBI Gene ID:7422, SEQ ID NO:54). In some embodiments, the level of VEGF is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of VEGF is increased in nonresponders after administration of an ADC relative to the baseline level. In some embodiments, the biomarker is vascular endothelial growth factor D (VEGF-D, NCBI Gene ID:2277, SEQ ID NO:55). In some embodiments, the level of VEGF-D is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of VEGF-D is increased in nonresponders after administration of an ADC relative to the baseline level. [00179] In some embodiments, the biomarker is an interleukin isoform. In some embodiments, the biomarker is interleukin 17C (IL17C, NCBI Gene ID:27189, SEQ ID NO:56). In some embodiments, the level of IL17C is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the biomarker is interleukin 10 (IL-10, NCBI Gene ID:3586, SEQ ID NO:57). In some embodiments, the level of IL-10 is decreased after administration of an ADC relative to the baseline level in a subject responding to treatment. In some embodiments, the biomarker is interleukin 6 (IL-6, NCBI Gene ID:3569, SEQ ID NO:58). In some embodiments, the level of IL-6 is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of IL-6 is increased in nonresponders after administration of an ADC relative to the baseline level. In some embodiments, the biomarker is interleukin 18 (IL-18, NCBI Gene ID:3606, SEQ ID NO:59). In some embodiments, the level of IL- 18 is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of IL-18 is increased in nonresponders after administration of an ADC relative to the baseline level. [00180] In some embodiments, the biomarker is epidermal growth factor (EGF, NCBI Gene ID:1950, SEQ ID NO:60). In some embodiments, the level of EGF is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of EGF is increased in nonresponders after administration of an ADC relative to the baseline level. Finngean Reference: 15648.0053-00304 [00181] In some embodiments, the biomarker is a tumor necrosis factor isoform. In some embodiments, the biomarker is tumor necrosis factor alpha (TNF-α, NCBI Gene ID:7124, SEQ ID NO:61). In some embodiments, the level of TNF-α is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of TNF-α is increased in nonresponders after administration of an ADC relative to the baseline level. [00182] In some embodiments, the biomarker is intercellular adhesion molecule 1 (ICAM-1, NCBI Gene ID:3383, SEQ ID NO:62). In some embodiments, the level of ICAM-1is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of ICAM-1 is increased in nonresponders after administration of an ADC relative to the baseline level. [00183] In some embodiments, the biomarker is transforming growth factor alpha (TGFA, NCBI Gene ID:7039, SEQ ID NO:63). In some embodiments, the level of TGFA is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of TGFA is increased in nonresponders after administration of an ADC relative to the baseline level. [00184] In some embodiments, the biomarker is hepatocyte growth factor (HGF, NCBI Gene ID:3082, SEQ ID NO:64). In some embodiments, the level of HGF is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of HGF is increased in nonresponders after administration of an ADC relative to the baseline level. [00185] In some embodiments, the biomarker is oncostatin M (OSM, NCBI Gene ID:5008, SEQ ID NO:65). In some embodiments, the level of OSM is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of OSM is increased in nonresponders after administration of an ADC relative to the baseline level. [00186] In some embodiments, the biomarker is erb-b2 recetpor tyrosine kinase 2 (HER-2, NCBI Gene ID:2064, SEQ ID NO:66). In some embodiments, the level of HER-2 is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of HER-2 is increased in nonresponders after administration of an ADC relative to the baseline level. [00187] In some embodiments, the biomarker is TIMP metallopeptidase inhibitor 1 (TIMP1, NCBI Gene ID:7076, SEQ ID NO:67). In some embodiments, the level of TIMP1is unchanged after administration of an ADC relative to the baseline level in a subject responding to treatment, while the level of TIMP1 is increased in nonresponders after administration of an ADC relative to the baseline level. [00188] In some embodiments, the changes (or lack of change) in a combination of two or more of the biomarkers discussed above are used in assessing the impact of a drug or treatment, or assist a physician in adjusting treatment in a subject. In some embodiments, levels of two or more biomarkers associated with protumor functions are reduced after administration of an ADC, e.g., MORAb-202, Finngean Reference: 15648.0053-00304 relative to baseline levels in a subject responsive to treatment. In some embodiments, the level of two or more of, e.g., all of, ANG-2, KLK-5, KLK-7, MCP-1, FRTN, and MMP12, or any combination thereof, are reduced relative to baseline levels in a subject responding to treatment. Wtihout being bound by theory, a reduction in a combination of biomarkers associated with protumor functions may indicate a therapetutic improvement in the tumor microenvironment, for example, reduction in production of abnormal blood vessels, reduction in hypoxia, improvement in the epithelial- mesenchymal transition, reduced immune suppression, reduction in tumorigenic stroma and extracellular matrix remodeling, and a reduction in cancer growth and metastasis. [00189] In some embodiments, an increase in the level of SP-D after administration of an ADC relative to baseline level, combined with a decrease in the level of IGFBP-2 and/or ANG-2 after administration of the ADC relative to baseline indicates a subject is responding to treatment. Without being bound by theory, changes in this combination of biomarkers may indicate that an ADC such as MORAb-202 exerts pharmacodynamic effects that trend with antitumor responses [00190] In some embodiments, a decrease in the level of IGFBP-2 and/or ANG-2 after administration of the ADC relative to baseline indicates a subject is responding to treatment. Without being bound by theory, changes in this combination of biomarkers may indicate that an ADC such as MORAb-202 exerts pharmacodynamic effects that trend with antitumor responses. [00191] In some embodiments, an increase in the level of SP-D after administration of the ADC relative to a baseline level, combined with a decrease in the level of KLK-7, MCP-1, MMP12, and/or IGFBP-2 indicates a subject is responding to treatment. Without being bound by theory, changes in this combination of biomarkes may not be confounded by drug exposure. [00192] In some embodiments, a decrease in the level of KLK-7, MCP-1, MMP12, and/or IGFBP-2 indicates a subject is responding to treatment. Without being bound by theory, changes in this combination of biomarkes may not be confounded by drug exposure. [00193] In some embodiments, an increase in the level of IGFBP-1, FLT3LB, MIP-1 β, CCL8, CCL13, IP-10, VEGF, IL-6, IL-18, EGF, TNFα, ICAM-1, TGFA, HGF, OSM, HER-2, TIMP1, and/or VEGF-D after administration of the ADC relative to a baseline level indicates a subject is not responding to treatment. Without being bound by theory, changes in this combination of biomarkers may indicate that an ADC such as MORAb-202 suppress protumor changes and/or may indicate drug- resistant pathways. Pharmaceutical compositions and formulations [00194] An ADC used in the practice of the foregoing methods may be formulated into a pharmaceutical composition suitable for administration to a subject, e.g., a human subject. In some embodiments, the pharmaceutical composition comprises the ADC and a pharmaceutically acceptable carrier suitable for the desired delivery method. Suitable carriers include any material that, when combined with an ADC disclosed herein, allows that ADC to retain its anti-tumor function and is Finngean Reference: 15648.0053-00304 generally non-reactive with the subject’s immune system. Pharmaceutically acceptable carriers may include any and all solvents, dispersion media, coatings, antibacterial and antifungal agents, isotonic and absorption delaying agents, and the like that are physiologically compatible. Examples of pharmaceutically acceptable carriers include one or more of water, saline, phosphate buffered saline, dextrose, glycerol, ethanol, mesylate salt, and the like, as well as combinations thereof. In some embodiments the formulation includes one or more isotonic agents, for example, sugars, polyalcohols such as mannitol, sorbitol, or sodium chloride. Pharmaceutically acceptable carriers may comprise minor amounts of auxiliary substances such as wetting or emulsifying agents, preservatives or buffers, which enhance the shelf life or effectiveness of the ADC. [00195] The pharmaceutical compositions disclosed herein may be in a variety of forms. These include, for example, liquid, semi-solid, and solid dosage forms, such as liquid solutions (e.g., injectable and infusible solutions), dispersions or suspensions, tablets, pills, powders, liposomes, and suppositories. The preferred form depends on the intended mode of administration and therapeutic application. [00196] Pharmaceutical compositions may be solubilized and administered via any route capable of delivering the composition to the tumor site. Potentially effective routes of administration include, but are not limited to, intravenous, parenteral, intraperitoneal, intramuscular, intratumor, intradermal, intraorgan, orthotopic, and the like. Pharmaceutical compositions can be lyophilized and stored as sterile powders, preferably under vacuum, and then reconstituted in bacteriostatic water (containing for example, benzyl alcohol preservative) or in sterile water prior to injection. Administration can be either systemic or local. Pharmaceutical compositions may comprise an ADC or a pharmaceutically acceptable salt thereof, e.g., a mesylate salt. Pharmaceutical compositions may further comprise a corticosteroid, e.g., dexamethasone, prednisone, or methylprednisolone. Alternatively, in some embodiments, a corticosteroid may be provided in a separate packaging. [00197] In various embodiments, kits for use in the therapeutic applications disclosed herein are within the scope of the present disclosure. Such kits may comprise an ADC disclosed herein and a carrier, package, or container. The carrier, package, or container may be compartmentalized to receive one or more containers such as vials, tubes, and the like, each of the container(s) comprising one of the separate elements to be used in a method disclosed herein, and/or a label or insert comprising instructions for use, such as a use disclosed herein. The carrier, packaging or container may also comprise a compartment for a corticosteroid. [00198] Kits may further comprise one or more other containers associated therewith that comprise materials desirable from a commercial and user standpoint, including buffers, diluents, filters, needles, syringes; carrier, package, container, vial and/or tube labels listing contents and/or instructions for use, and package inserts with instructions for use. [00199] A label may be present on or with the container to indicate that the composition is used for a specific therapy or non-therapeutic application, such as a prognostic, prophylactic, diagnostic, or Finngean Reference: 15648.0053-00304 laboratory application. A label may also indicate directions for either in vivo or in vitro use, such as those disclosed herein. Directions and or other information may also be included on an insert(s) or label(s), which is included with or on the kit. The label may be on or associated with the container. A label may be on a container when letters, numbers, or other characters forming the label are molded or etched into the container itself. A label may be associated with a container when it is present within a receptacle or carrier that also holds the container, e.g., as a package insert. The label may indicate that the composition is used for diagnosing or treating a condition, such as a cancer a disclosed herein. [00200] It will be readily apparent to those skilled in the art that other suitable modifications and adaptations of the methods of the invention disclosed herein are obvious and may be made using suitable equivalents without departing from the scope of the invention or the embodiments disclosed herein. Having now disclosed the invention in detail, the same will be more clearly understood by reference to the following examples, which are included for purposes of illustration only and are not intended to be limiting. EXAMPLE 1: Biomarker Analysis of FZEC (MORAb-202) Effects on Cancer Responses in Patients with Platinum Resistant Ovarian Cancer Introduction [00201] FZEC (farletuzumab ecteribulin, also MORAb-202) is an antibody-drug conjugate consisting of the humanized anti-folate receptor-alpha (FRα) monoclonal antibody, farletuzumab, and the potent microtubule dynamics inhibitor, eribulin, conjugated by a cathepsin B-cleavable linker. FZEC is cytotoxic to FRα-positive cancer cells (via direct binding) and to adjacent tumor cells (via bystander effects); it also exerts noncytotoxic bystander effects in the tumor microenvironment (TME). Association of the impacts of FZEC or eribulin on the tumor microenvironment (TME), e.g., effects on reversing tumor epithelial-mesenchymal transition, vascular normalization, and stromal differentiation with antitumor activities in preclinical tumor cell or patient-derived xenograft models were previously reported. Furthermore, the effects of eribulin on reversing epithelial-mesenchymal transition, improving vascular perfusion, and promoting immune responses in the TME have been reported in patients with cancer. A first-in-human dose-escalation followed by dose-expansion study (Study MORAb-202-J081-101 in Japanese patients with selected solid tumors to determine the safety and preliminary efficacy of FZEC is ongoing. Antitumor activity across several FZEC doses has been demonstrated in patients with platinum-resistant ovarian cancer (PROC) and across FRα-expression levels. An exploratory serum biomarker study was conducted to evaluate the association of FZEC– induced pharmacological effects and clinical responses in patients with PROC and to investigate the clinical mechanism of action of FZEC. Methods Finngean Reference: 15648.0053-00304 [00202] Patients with PROC from the dose-escalation and dose-expansion phases of Study 101 were treated with FZEC (at doses of 0.3, 0.45, 0.68, 0.9, or 1.2 mg/kg; all administered every 3 weeks) and were included in the biomarker analysis (Fig.1). In Study 101, bodyweight-based dosing at the doses listed above was utilized. Subsequent studies have led to body-surface-area–based dosing at a dose of 25 mg/m2 in ongoing trials. Biomarker Analyses [00203] Serum protein factors relating to angiogenesis, cytokines, inflammation, and cancer biology were analyzed. The study included 94 biomarkers that were analyzed by the Rules-Based Medicine (RBM) panels on either the Luminex-based or SIMOA-based assay platforms, and 45 biomarkers were analyzed by the OLINK® Target-48 Cytokine panel. [00204] An assay-specific lower limit of quantification (LLOQ) was established for each test. Biomarkers with ≥ 70% of data points above the LLOQ were included in the statistical analysis, while biomarkers that contained > 30% of data points below LLOQ were removed. The data points that appeared below LLOQ for any biomarker were replaced by one-half the value of the LLOQ for the corresponding biomarker (ie, if the output was “< 54” for a data point, a value of 27 was used for the statistical analysis). [00205] For analyses by confirmed best overall response (BOR) status, patients were dichotomized into responders (complete response [CR]/partial response [PR]) versus nonresponders (stable disease [SD]/progressive disease [PD]). [00206] At each postbaseline visit, a percentage change from baseline value was analyzed using the 1-sample Wilcoxon signed-rank test for each BOR group and compared using the 2-sample Wilcoxon signed-rank test at each visit between the 2 groups with a 1-sided alternative— one less and one greater. Alternatively, logistic regression was performed adjusting for FZEC exposure AUC; 1- sided P-values using the Wald test of the coefficient of the term of percentage change from baseline were computed. [00207] Fisher’s method was used to generate a combined P-value (also referred to as a meta P- value) to summarize statistical differences across visits between the 2 response groups. To determine the direction of differences between responders and nonresponders, a Wilcoxon test was utilized where the alternatives were greater or less rather than 2-sided. If consensus among all the tests was “greater,” then nonresponders had higher changes than responders. [00208] Assessments of the combined FZEC dose cohort (0.3, 0.45, 0.68, 0.9, and 1.2 mg/kg) were performed both with and without adjustments for area under the curve (AUC). Assessment of the 0.9 mg/kg cohort was done without adjustment for AUC. Results Finngean Reference: 15648.0053-00304 Patients [00209] For data generated by RBM panels, 58 patients with PROC from the dose-escalation and dose-expansion phases of Study 101 were included in the biomarker analysis (Table 11). Patient allocations were n = 1 in the FZEC 0.3 mg/kg group, n = 3 in the FZEC 0.45 mg/kg group, n = 2 in the FZEC 0.68 mg/kg group, n = 28 in the FZEC 0.9 mg/kg group, and n = 24 in the FZEC 1.2 mg/kg group. [00210] For data generated by the OLINK panel, 35 patients with PROC were included in the biomarker analysis from the FZEC 0.9 mg/kg (n = 22) and FZEC 1.2 mg/kg (n = 13) cohorts of the dose-escalation and dose-expansion phases of Study 101 (Table 11). Table 11. Patients Included in the Biomarker Analysis BOR, best overall response; C#D#, cycle # day #; CR, complete response; PD, progressive disease; PR, partial response; RBM, Rules-Based Medicine; SD, stable disease. Biomarker Changes Associated With Best Overall Response (BOR) [00211] Of the 139 biomarkers measured, 98 had ≥ 70% of data points evaluable and, thus, were included in the statistical analysis. The 139 biomarkers include overlaps in marker names between the 2 analytical platforms. [00212] We explored biomarkers with significant percentage changes between responders and nonresponders relative to baseline (1-sample Wilcoxon signed-rank P < 0.05). These changes were assessed over visit points C2D1 – C6D1 (i.e., second dose through sixth dose of FZEC). [00213] Percentage changes (P < 0.05) from baseline to at least 1 visit postdose in either BOR group, and differences (meta P < 0.05) between responders and nonresponders, were seen in 29 biomarkers in the combined-dose cohort (from analysis without AUC adjustment), and in 14 biomarkers in the FZEC 0.9 mg/kg cohort (Table 12). [00214] In addition to the overall difference in changes between responders and nonresponders (meta P < 0.05) (Table 12), decreases in the biomarkers ANG-2, KLK-5, KLK-7, MCP-1, FRTN, MMP12, and IGFBP-2, and increases in SP-D, were persistent (P < 0.05 at ≥ 3 visits) in responders in the combined cohort (Figure 2) or FZEC 0.9 mg/kg cohort (Figure 3), indicating that the changes were likely mediated by FZEC treatment and associated with cancer responses. Finngean Reference: 15648.0053-00304 [00215] Reductions in biomarkers with protumor functions (ANG-2, KLK-5, KLK-7, MCP-1, FRTN, MMP12) were observed in responders after FZEC treatment (Figs.2 and 3) and might have contributed to the antitumor effects of FZEC/eribulin (Fig.4). Reduction in FRTN in responders suggests an association of iron metabolism with FZEC-mediated cancer responses. Iron metabolism is involved in shaping the immune landscapes in cancer-associated inflammation. Increases in SP-D (a marker implicated in the immune surveillance against cancer and in induction of apoptosis in a variety of cancer cell lines and primary cancer cells derived from patients) following FZEC treatment (Figs.2 and 3) indicated that this marker might have contributed to the antitumor effects of FZEC/eribulin (Fig.4). Table 12. Biomarkers With Changes Associated With BOR Finngean Reference: 15648.0053-00304 Markers in shaded rows showed overlapping changes in the combined-dose cohort and the FZEC 0.9 mg/kg dose cohort. Markers in bold show changes (P < 0.05) starting on C2D1 in the combined-dose analysis. A dash indicates P > 0.05 for all the visits or meta P > 0.05 for the corresponding marker. Marker names from the OLINK panel were labeled accordingly if labels overlapped those from RBM panels. Arrows indicate direction of change. P values are not FDR adjusted. BOR, best overall response; C#D#, cycle # day #; FDR, false discovery rate; FZEC, farletuzumab; RBM, Rules-Based Medicine. [00216] There was an overlap of 11 markers, including SP-D, IGFBP-2, and ANG-2, in both the FZEC 0.9 mg/kg and combined-dose cohorts that showed a change (P < 0.05) from baseline in responders and/or nonresponders and differences in percentage changes (meta P < 0.05) between responders and nonresponders (Table 12). These results support the idea that FZEC exerts pharmacodynamic effects that trend with antitumor responses at the 0.9 mg/kg dose level. Although 0.9 mg/kg was originally selected as a clinical dose, this dose is no longer being used in ongoing studies. In the future, additional data will be generated in ongoing trials (using different dose levels) to confirm findings from the 0.9 mg/kg dose. [00217] Table 13 lists the markers that showed both more visits with changes (P < 0.05) in responders versus nonresponders and differences between BOR groups (meta P < 0.05) in at least 1 of the 3 analyses. The number of visits with significant change versus baseline (P < 0.05) for each marker within the subcohort responders or nonresponders is listed. [00218] Changes from baseline in some biomarkers (eg, SP-D, KLK-7, MCP-1, MMP12, IGFBP-2) occurred in the combined-cohort analyses irrespective of adjustment by AUC (Table 13), indicating that the association of these biomarkers with tumor responses may not be confounded by the association of the biomarker expression changes with drug exposure. This will be further explored at the lower dose currently being investigated in clinical trials. Finngean Reference: 15648.0053-00304 [00219] Although levels of ANG-2 and KLK-5 appeared to be different between responders and nonresponders after treatment with FZEC in the combined-dose cohort, these differences were not apparent when adjusted for FZEC AUC (Table 13). While hypotheses generated from this study need to be verified in further clinical studies, this may be because both changes in biomarker expression and association with responders are highly linked with drug exposure. It is also possible that the observed associations of biomarkers with cancer responses are confounded by their association with drug exposure. [00220] Biomarkers such as IGFBP-1, FLT3LG, and VEGF-D showed increases (P < 0.05) in nonresponders (Table 12). This may indicate that FZEC suppressed protumor changes (Fig.4), or the changes may indicate drug-resistant pathways. Table 13. Comparison of Biomarkers Associated With Tumor Responders Listed are markers that showed (1) more visits with changes (P < 0.05) in responders than those in nonresponders and (2) difference between BOR groups (meta P < 0.05) in at least 1 of the 3 analyses. The number of visits for which the responder cohort was significant changed from baseline (P < 0.05) for each marker are listed. A dash indicates P > 0.05 at all visits or meta P > 0.05 for the corresponding marker. AUC, area under the curve; BOR, best overall response; FZEC, farletuzumab ecteribulin. Summary and Conclusions Finngean Reference: 15648.0053-00304 [00221] The persistent responder-associated biomarker changes suggest that FZEC may modulate functions associated with these markers (eg, vascular remodeling, immune regulation, stroma/extracellular matrix remodeling, iron metabolism, reversing epithelial-mesenchymal transition), and this may contribute to the antitumor effect of FZEC in addition to its cytotoxic effects on cancer cells in patients with PROC (Fig.4). [00222] In the limited number of patients analyzed, preliminary pharmacodynamic effects trended with the antitumor effects previously observed with FZEC 0.9 mg/kg.
Finngean Reference: 15648.0053-00304 Selected sequences: SEQ ID NO: 1 (MORAb-003 HC CDR1; Kabat): GYGLS SEQ ID NO: 2 (MORAb-003 HC CDR2; Kabat): MISSGGSYTYYADSVKG SEQ ID NO: 3 (MORAb-003 HC CDR3; Kabat): HGDDPAWFAY SEQ ID NO: 4 (MORAb-003 LC CDR1; Kabat): SVSSSISSNNLH SEQ ID NO: 5 (MORAb-003 LC CDR2: Kabat): GTSNLAS SEQ ID NO: 6 (MORAb-003 LC CDR3; Kabat): QQWSSYPYMYT SEQ ID NO: 7 (MORAb-003 HC CDR1; IMGT): GFTFSGYG SEQ ID NO: 8 (MORAb-003 HC CDR2; IMGT): ISSGGSYT SEQ ID NO: 9 (MORAb-003 HC CDR3; IMGT): ARHGDDPAWFAY SEQ ID NO: 10 (MORAb-003 LC CDR1; IMGT): SSISSNN SEQ ID NO: 11 (MORAb-003 LC CDR2; IMGT): GTS SEQ ID NO: 12 (MORAb-003 LC CDR3; IMGT): QQWSSYPYMYT SEQ ID NO: 13 (MORAb-003 Heavy chain variable domain (VH)): 1 EVQLVESGGG VVQPGRSLRL SCSASGFTFS GYGLSWVRQA PGKGLEWVAM 51 ISSGGSYTYY ADSVKGRFAI SRDNAKNTLF LQMDSLRPED TGVYFCARHG 101 DDPAWFAYWG QGTPVTVSSA SEQ ID NO: 14 (MORAb-003 Light chain variable domain (VL)): QQWSSYPYMYT 1 DIQLTQSPSS LSASVGDRVT ITCSVSSSIS SNNLHWYQQK PGKAPKPWIY 51 GTSNLASGVP SRFSGSGSGT DYTFTISSLQ PEDIATYYCQ QWSSYPYMYT 101 FGQGTKVEIK SEQ ID NO: 15 (MORAb-003 Heavy chain (HC)) 1 EVQLVESGGG VVQPGRSLRL SCSASGFTFS GYGLSWVRQA PGKGLEWVAM 51 ISSGGSYTYY ADSVKGRFAI SRDNAKNTLF LQMDSLRPED TGVYFCARHG Finngean Reference: 15648.0053-00304 101 DDPAWFAYWG QGTPVTVSSA STKGPSVFPL APSSKSTSGG TAALGCLVKD 151 YFPEPVTVSW NSGALTSGVH TFPAVLQSSG LYSLSSVVTV PSSSLGTQTY 201 ICNVNHKPSN TKVDKKVEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK 251 DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS 301 TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV 351 YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL 401 DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGK SEQ ID NO: 16 (MORAb-003 Light chain (LC)) 1 DIQLTQSPSS LSASVGDRVT ITCSVSSSIS SNNLHWYQQK PGKAPKPWIY 51 GTSNLASGVP SRFSGSGSGT DYTFTISSLQ PEDIATYYCQ QWSSYPYMYT 101 FGQGTKVEIK RTVAAPSVFI FPPSDEQLKS GTASVVCLLN NFYPREAKVQ 151 WKVDNALQSG NSQESVTEQD SKDSTYSLSS TLTLSKADYE KHKVYACEVT 201 HQGLSSPVTK SFNRGEC SEQ ID NO: 35 (MORAb-003 HC nt) 1 ATGGGATGGA GCTGTATCAT CCTCTTCTTG GTAGCAACAG CTACAGGTGT 51 CCACTCCGAG GTCCAACTGG TGGAGAGCGG TGGAGGTGTT GTGCAACCTG 101 GCCGGTCCCT GCGCCTGTCC TGCTCCGCAT CTGGCTTCAC CTTCAGCGGC 151 TATGGGTTGT CTTGGGTGAG ACAGGCACCT GGAAAAGGTC TTGAGTGGGT 201 TGCAATGATT AGTAGTGGTG GTAGTTATAC CTACTATGCA GACAGTGTGA 251 AGGGTAGATT TGCAATATCG CGAGACAACG CCAAGAACAC ATTGTTCCTG 301 CAAATGGACA GCCTGAGACC CGAAGACACC GGGGTCTATT TTTGTGCAAG 351 ACATGGGGAC GATCCCGCCT GGTTCGCTTA TTGGGGCCAA GGGACCCCGG 401 TCACCGTCTC CTCAGCCTCC ACCAAGGGCC CATCGGTCTT CCCCCTGGCA 451 CCCTCCTCCA AGAGCACCTC TGGGGGCACA GCGGCCCTGG GCTGCCTGGT 501 CAAGGACTAC TTCCCCGAAC CGGTGACGGT GTCGTGGAAC TCAGGCGCCC 551 TGACCAGCGG CGTGCACACC TTCCCGGCTG TCCTACAGTC CTCAGGACTC 601 TACTCCCTCA GCAGCGTGGT GACCGTGCCC TCCAGCAGCT TGGGCACCCA 651 GACCTACATC TGCAACGTGA ATCACAAGCC CAGCAACACC AAGGTGGACA 701 AGAAAGTTGA GCCCAAATCT TGTGACAAAA CTCACACATG CCCACCGTGC 751 CCAGCACCTG AACTCCTGGG GGGACCGTCA GTCTTCCTCT TCCCCCCAAA 801 ACCCAAGGAC ACCCTCATGA TCTCCCGGAC CCCTGAGGTC ACATGCGTGG 851 TGGTGGACGT GAGCCACGAA GACCCTGAGG TCAAGTTCAA CTGGTACGTG 901 GACGGCGTGG AGGTGCATAA TGCCAAGACA AAGCCGCGGG AGGAGCAGTA 951 CAACAGCACG TACCGTGTGG TCAGCGTCCT CACCGTCCTG CACCAGGACT Finngean Reference: 15648.0053-00304 1001 GGCTGAATGG CAAGGAGTAC AAGTGCAAGG TCTCCAACAA AGCCCTCCCA 1051 GCCCCCATCG AGAAAACCAT CTCCAAAGCC AAAGGGCAGC CCCGAGAACC 1101 ACAGGTGTAC ACCCTGCCCC CATCCCGGGA TGAGCTGACC AAGAACCAGG 1151 TCAGCCTGAC CTGCCTGGTC AAAGGCTTCT ATCCCAGCGA CATCGCCGTG 1201 GAGTGGGAGA GCAATGGGCA GCCGGAGAAC AACTACAAGA CCACGCCTCC 1251 CGTGCTGGAC TCCGACGGCT CCTTCTTCTT ATATTCAAAG CTCACCGTGG 1301 ACAAGAGCAG GTGGCAGCAG GGGAACGTCT TCTCATGCTC CGTGATGCAT 1351 GAGGCTCTGC ACAACCACTA CACGCAGAAG AGCCTCTCCC TGTCTCCCGG 1401 GAAATGA SEQ ID NO: 36 (MORAb-003 LC nt) 1 ATGGGATGGA GCTGTATCAT CCTCTTCTTG GTAGCAACAG CTACAGGTGT 51 CCACTCCGAC ATCCAGCTGA CCCAGAGCCC AAGCAGCCTG AGCGCCAGCG 101 TGGGTGACAG AGTGACCATC ACCTGTAGTG TCAGCTCAAG TATAAGTTCC 151 AACAACTTGC ACTGGTACCA GCAGAAGCCA GGTAAGGCTC CAAAGCCATG 201 GATCTACGGC ACATCCAACC TGGCTTCTGG TGTGCCAAGC AGATTCAGCG 251 GTAGCGGTAG CGGTACCGAC TACACCTTCA CCATCAGCAG CCTCCAGCCA 301 GAGGACATCG CCACCTACTA CTGCCAACAG TGGAGTAGTT ACCCGTACAT 351 GTACACGTTC GGCCAAGGGA CCAAGGTGGA AATCAAACGA ACTGTGGCTG 401 CACCATCTGT CTTCATCTTC CCGCCATCTG ATGAGCAGTT GAAATCTGGA 451 ACTGCCTCTG TTGTGTGCCT GCTGAATAAC TTCTATCCCA GAGAGGCCAA 501 AGTACAGTGG AAGGTGGATA ACGCCCTCCA ATCGGGTAAC TCCCAGGAGA 551 GTGTCACAGA GCAGGACAGC AAGGACAGCA CCTACAGCCT CAGCAGCACC 601 CTGACGCTGA GCAAAGCAGA CTACGAGAAA CACAAAGTCT ACGCCTGCGA 651 AGTCACCCAT CAGGGCCTGA GCTCGCCCGT CACAAAGAGC TTCAACAGGG 701 GAGAGTGTTA A SEQ ID NO: 37 (human FRA) 1 maqrmttqll lllvwvavvg eaqtriawar tellnvcmna khhkekpgpe dklheqcrpw 61 rknaccstnt sqeahkdvsy lyrfnwnhcg emapackrhf iqdtclyecs pnlgpwiqqv 121 dqswrkervl nvplckedce qwwedcrtsy tcksnwhkgw nwtsgfnkca vgaacqpfhf 181 yfptptvlcn eiwthsykvs nysrgsgrci qmwfdpaqgn pneevarfya aamsgagpwa 241 awpfllslal mllwlls Finngean Reference: 15648.0053-00304 SEQ ID NO: 38 (human FRA nucleotide) 1 cattccttgg tgccactgac cacagctctt tcttcaggga cagacatggc tcagcggatg 61 acaacacagc tgctgctcct tctagtgtgg gtggctgtag taggggaggc tcagacaagg 121 attgcatggg ccaggactga gcttctcaat gtctgcatga acgccaagca ccacaaggaa 181 aagccaggcc ccgaggacaa gttgcatgag cagtgtcgac cctggaggaa gaatgcctgc 241 tgttctacca acaccagcca ggaagcccat aaggatgttt cctacctata tagattcaac 301 tggaaccact gtggagagat ggcacctgcc tgcaaacggc atttcatcca ggacacctgc 361 ctctacgagt gctcccccaa cttggggccc tggatccagc aggtggatca gagctggcgc 421 aaagagcggg tactgaacgt gcccctgtgc aaagaggact gtgagcaatg gtgggaagat 481 tgtcgcacct cctacacctg caagagcaac tggcacaagg gctggaactg gacttcaggg 541 tttaacaagt gcgcagtggg agctgcctgc caacctttcc atttctactt ccccacaccc 601 actgttctgt gcaatgaaat ctggactcac tcctacaagg tcagcaacta cagccgaggg 661 agtggccgct gcatccagat gtggttcgac ccagcccagg gcaaccccaa tgaggaggtg 721 gcgaggttct atgctgcagc catgagtggg gctgggccct gggcagcctg gcctttcctg 781 cttagcctgg ccctaatgct gctgtggctg ctcagctgac ctccttttac cttctgatac 841 ctggaaatcc ctgccctgtt cagccccaca gctcccaact atttggttcc tgctccatgg 901 tcgggcctct gacagccact ttgaataaac cagacaccgc acatgtgtct tgagaattat 961 ttggaaaaaa aaaaaaaaaa aa Table 14. Biomarker Sequences Finngean Reference: 15648.0053-00304 Finngean Reference: 15648.0053-00304 Finngean Reference: 15648.0053-00304 Finngean Reference: 15648.0053-00304 Finngean Reference: 15648.0053-00304 Finngean Reference: 15648.0053-00304

Claims

Finngean Reference: 15648.0053-00304 CLAIMS: 1. A method of treating a folate receptor alpha (FRA)-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to a subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen- binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8, (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) administering a further dose of the antibody-drug conjugate if a change in the level is detected. 2. A method of reducing risk of interstitial lung disease (ILD) in a subject being treated for an FRA-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to the subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen- binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), Finngean Reference: 15648.0053-00304 and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8. (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) administering a further dose of the antibody-drug conjugate if a change in the level is detected. 3. The method of claim 1 or claim 2, wherein the level of surfactant protein D (SP-D) in a sample taken from the subject after administration is increased relative to the level of SP-D in the baseline sample. 4. The method of claim 3, wherein the level of SP-D is increased at least 100% relative to the level of SP-D in the baseline sample. 5. The method of claim 1 or claim 2, wherein the level of kallikrein related peptidase 7 (KLK-7) in a sample taken from the subject after administration is reduced relative to the level of KLK-7 in the baseline sample. 6. The method of claim 5, wherein the level of KLK-7 is reduced at least 30% relative to the level of KLK-7 in the baseline sample. 7. The method of claim 1 or claim 2, wherein the level of monocyte chemoattractant protein-1 (MCP-1) in a sample taken from the subject after administration is reduced relative to the level of MCP-1 in the baseline sample. 8. The method of claim 7, wherein the level of MCP-1 is reduced at least 15% relative to the level of MCP-1 in the baseline sample. Finngean Reference: 15648.0053-00304 9. The method of claim 1 or claim 2, wherein the level of angiopoietin 2 (ANG-2) in a sample taken from the subject after administration is reduced relative to the level of ANG-2 in the baseline sample. 10. The method of claim 9, wherein the level of ANG-2 is reduced at least 30% relative to the level of ANG-2 in the baseline sample. 11. The method of claim 1 or claim 2, wherein the level of kallikrein related peptidase 5 (KLK-5) in a sample taken from the subject after administration is reduced relative to the level of KLK-5 in the baseline sample. 12. The method of claim 11, wherein the level of KLK-5 is reduced at least 40% relative to the level of KLK-5 in the baseline sample. 13. The method of claim 1 or claim 2, wherein the level of matrix metalloproteinase 12 (MMP12) in a sample taken from the subject after administration is reduced relative to the level of MMP12 in the baseline sample. 14. The method of claim 13, wherein the level of MMP12 is reduced at least 40% relative to the level of MMP12 in the baseline sample. 15. The method of claim 1 or claim 2, wherein the level of ferritin (FRTN) in a sample taken from the subject after administration is reduced relative to the level of FRTN in the baseline sample. 16. The method of claim 15, wherein the level of FRTN is reduced at least 40% relative to the level of FRTN in the baseline sample. 17. The method of claim 1 or claim 2, wherein the level of insulin like growth factor binding protein 2 (IGFBP-2) in a sample taken from the subject after administration is reduced relative to the level of IGFBP-2 in the baseline sample. 18. The method of claim 17, wherein the level of IGFBP-2 is reduced at least 30% relative to the level of IGFBP-2 in the baseline sample. 19. A method of treating a folate receptor alpha (FRA)-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, Finngean Reference: 15648.0053-00304 (b) administering to a subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen- binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8, (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) administering a further dose of the antibody-drug conjugate if a change in the level is not detected, wherein the biomarker is one or more of IGFBP-1, FLT3L, and VEGF-D. 20. The method of claim 19, wherein the biomarker of tumor response is insulin like growth factor binding protein 1 (IGFBP-1). 21. The method of claim 19, wherein the biomarker of tumor response is fms related receptor tyrosine kinase 3 ligand (FLT3LG). 22. The method of claim 19, wherein the biomarker of tumor response is vascular endothelial growth factor D (VEGF-D). 23. A method of treating a folate receptor alpha (FRA)-expressing cancer, comprising (a) measuring the level of one or more biomarkers of tumor response in a baseline biological sample from a subject, (b) administering to a subject in need thereof a dose of an antibody-drug conjugate of Formula (I): Ab-(L-D)p (I) Finngean Reference: 15648.0053-00304 wherein (i) Ab is an internalizing anti-folate receptor alpha antibody or internalizing antigen- binding fragment thereof comprising three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 1 (HCDR1), SEQ ID NO: 2 (HCDR2), and SEQ ID NO: 3 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 4 (LCDR1), SEQ ID NO: 5 (LCDR2), and SEQ ID NO: 6 (LCDR3), as defined by the Kabat numbering system; or three heavy chain complementarity determining regions (HCDRs) comprising amino acid sequences of SEQ ID NO: 7 (HCDR1), SEQ ID NO: 8 (HCDR2), and SEQ ID NO: 9 (HCDR3); and three light chain complementarity determining regions (LCDRs) comprising amino acid sequences of SEQ ID NO: 10 (LCDR1), SEQ ID NO: 11 (LCDR2), and SEQ ID NO: 12 (LCDR3), as defined by the IMGT numbering system; (ii) D is eribulin; (iii) L is a cleavable linker comprising Mal-(PEG)2-Val-Cit-pAB; and (iv) p is an integer from 1 to 8, (c) measuring the level of one or more biomarkers of tumor response in a sample taken from the subject to determine a change relative to the level in the baseline sample, and (d) determining the efficacy of the antibody-drug conjugate based on a level change in the one or more biomarkers of tumor response, wherein the biomarker of tumor response is one or more of those in claims 1-22. 24. The method of any one of claims 1 to 23, wherein the antibody or antigen-binding fragment comprises a heavy chain comprising an amino acid sequence of SEQ ID NO: 15, and a light chain comprising an amino acid sequence of SEQ ID NO: 16. 25. The method of any one of claims 1 to 24, wherein the antibody-drug conjugate is MORAb- 202. 26. The method of any one of claims 1 to 25, wherein p is from 3 to 5. 27. The method of any one of claims 1 to 26, wherein the dose is 8 mg to 44 mg per m2 of the subject’s BSA. 28. The method of any one of claims 1 to 26, wherein the dose is 0.3 mg/kg to 1.2 mg/kg of the subject’s bodyweight. 29. The method of any one of claims 1 to 28, wherein the antibody-drug conjugate is administered once every three weeks. Finngean Reference: 15648.0053-00304 30. The method of any one of claims 1 to 28, wherein the antibody-drug conjugate is administered once every two weeks. 31. The method of any one of claims 1 to 28, wherein the antibody-drug conjugate is administered once per week. 32. The method of any one of claims 1 to 31, further comprising administering a corticosteroid. 33. The method of any one of claims 1 to 32, wherein the antibody-drug conjugate is administered intravenously. 34. The method of any one of claims 1 to 33, wherein the FRA-expressing cancer is selected from: gastric cancer, ovarian cancer, serous ovarian cancer, serous high-grade ovarian cancer, clear cell ovarian cancer, platinum resistant ovarian cancer, lung cancer, non-small cell lung cancer, metastatic non-small cell lung cancer, lung carcinoid, colorectal cancer, breast cancer, triple negative breast cancer, hormone receptor (HR)-positive and HER2-low breast cancer, endometrial cancer, serous endometrial carcinoma, peritoneal cancer, primary peritoneal cancer, fallopian tube cancer, pancreatic cancer, kidney cancer, renal cell cancer, cervical cancer, esophageal cancer, osteosarcoma, chorid plexus carcinoma ependymoma, epedymoblastoma, medulloblastoma, Wilms tumor, acute myeloid leukemia, and head and neck cancer. 35. The method of claim 34, wherein the FRA-expressing cancer is ovarian cancer. 36. The method of claim 35, wherein the ovarian cancer is platinum resistant ovarian cancer (PROC). 37. The method of any one of claims 34 to 36, wherein the FRA-expressing cancer is a refractory cancer. 38. The method of claim 37, wherein the refractory cancer is non-responsive to a targeted treatment. 39. The method of claim 38, wherein the targeted treatment is a targeted treatment against any one of the following genes or variants thereof: EGFR, ALK, BRAF, RET, MET, NTRK, and ROS1. Finngean Reference: 15648.0053-00304 40. The method of claim 37, wherein the refractory cancer is non-responsive to a platinum-based treatment and an immunotherapy-based treatment, wherein the treatments are administered concurrently or sequentially. 41. The method of claim 40, wherein the platinum-based treatment is a platinum-doublet chemotherapy, and wherein the immunotherapy-based treatment is a PD-1 inhibitor or a PD-L1 inhibitor. 42. The method of any one of claims 1 to 41, wherein the subject at the start of treatment does not have one or more of: interstitial lung disease (ILD) and/or pneumonitis, a history of ILD and/or pneumonitis, a lung-specific clinically significant illness, pleural effusion, pericardial effusion, prior pneumonectomy, a history of chest radiotherapy within the past 2 years, autoimmune disorder with pulmonary involvement, connective tissue disorder with pulmonary involvement, or inflammatory disorder with pulmonary involvement. 43. The method of any one of claims 1 to 41, wherein the subject does not have one or more of: a history of more than three prior therapies for the FRA-expressing cancer, a high neutrophil-to- lymphocyte ratio, or a serum albumin level at the start of treatment of less than 3 g/dL.
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