COMBINATION THERAPY INCLUDING ANTIBODIES THAT BIND EGFR AND cMET.

Abstract

The invention relates to a combination of a chemotherapeutic agent and a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGER) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) for use in a method of treatment of a cancer in a subject.

Description

[0001] Title: Combination therapy including antibodies that bind EGFR and cMET. The disclosure relates to the field of antibodies. In particular it relates to the field of therapeutic antibodies, including human antibodies, for use in a combination therapy that includes a chemotherapeutic agent to treat diseases involving aberrant cells. Further, it relates to antibodies that bind EGFR and cMET, including multispecific antibodies, and their use in the binding of EGFR and cMET positive cells, particularly tumor cells. Lung cancer is the leading cause of cancer-related mortality worldwide (Siegel RL et al. Cancer statistics, 2021. CA Cancer J Clin. 2021;71(1):7–33). Approximately 85% of all cases of lung cancer are non-small cell lung cancer (NSCLC) with a very low 5-year survival rate of around 16% (Testa U et al. Lung cancers: molecular characterization, clonal heterogeneity and evolution, and cancer stem cells. Cancers (Basel). 2018;10(8):248). The epidermal growth factor receptor (EGFR), also known as ErbB-1 receptor, is a cell-surface receptor for members of the EGF-family of extracellular protein ligands. Upon activation, the receptor may undergo a transition from an inactive mostly monomeric form to an active homodimer. In addition, EGFR may pair with another member of the ErbB receptor family, such as ErbB-2, to create an activated heterodimer. EGFR dimerization stimulates intrinsic intracellular protein-tyrosine kinase activity. This activity induces several signal transduction cascades that lead to cell proliferation and differentiation. EGFR mutations are present in about 15% of Caucasian patients with NSCLC and can drive ligand-independent receptor activation which is associated with tumor invasion, metastasis, and poor prognosis (Rosell, R. et al. Screening for epidermal growth factor receptor mutations in lung cancer. N. Engl. J. Med. 2009; 36:958–967). Targeted therapy with EGFR tyrosine kinase inhibitors (EGFR-TKIs) has sparked interest as they can improve prognosis in patients with advanced NSCLC. Third-generation TKIs, such as osimertinib, olmutinib, furmonertinib, almonertinib, befotertinib and lazertinib are currently approved for clinical use (He J et al. Mechanisms and management of 3rd‑generation EGFR‑TKI resistance in advanced non‑small cell lung cancer. Int J Oncol. 2021;59(5):90). Osimertinib is currently used as a first-line standard of care therapy in patients with advanced EGFR-mutated NSCLC and for EGFR T790M-positive NSCLC after first- or second-generation EGFR-TKIs. However, despite the improved period of progression-free survival and lower rates of adverse events, the majority of patients eventually develops resistance to osimertinib, regardless of the lines of treatment. Resistance mechanisms to osimertinib or other third-generation TKIs have been categorized into EGFR-dependent and EGFR-independent resistance mechanisms which include cMET-dependent resistance, HER2 amplification, resistance via RAS-MAPK pathway activation, resistance via PI3K pathway activation, cell-cycle gene alterations and oncogenic fusions (see e.g. Leonetti et al in British Journal of Cancer (2019) 121:725–737). One mechanism of resistance to osimertinib is an on-target genetic alteration in EGFR residue C797 in exon 20 (Fu, K. et al. Therapeutic strategies for EGFR-mutated non-small cell lung cancer patients with osimertinib resistance. J Hematol Oncol. 2022; 15:173). Since EGFR C797 is the covalent binding site of osimertinib, mutations at C797 interfere with its drug-protein interaction. C797 mutations were detected in 7% or 18% of NSCLC patients at disease progression where osimertinib was used as first-, or second-line treatment, respectively (Ramalingam S.S. et al. Mechanisms of acquired resistance to first-line osimertinib: Preliminary data from the phase III FLAURA study. ESMO: NSCLC, Metastatic. 2018; 29:8, VIII740 and Chmielecki J. et al. Analysis of acquired resistance mechanisms to osimertinib in patients with EGFR-mutated advanced non-small cell lung cancer from the AURA3 trial. Nat Commun. 2023 Feb 27;14(1):1071). There is thus a need for treatment of patients that develop acquired osimertinib or other EGFR inhibitor resistance in NSCLC patients. SUMMARY OF THE INVENTION Based on the multiple mechanisms of resistance after third generation EGFR TKI, the combination of a bispecific antibody and a chemotherapeutic agent of the present disclosure, is to target tumorous cell clones that have progressed after treatment with a third generation EGFR tyrosine kinase inhibitor, such as osimertinib, and are sensitive to a bispecific antibody of the present disclosure and are chemotherapy-sensitive. An option for subjects progressing on osimertinib is to combine said bispecific antibody and said chemotherapeutic agent to address an unmet medical need. In certain aspects, the present disclosure provides a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in a method of treatment of a cancer in a subject. In certain aspects, the present disclosure provides a method of treatment of a subject having a cancer, said treatment comprising administering to the subject an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent to said subject. In certain aspects, the present disclosure provides the use of a bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind (or binds) an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent in the manufacture of a medicament for the treatment of a cancer. In certain aspects, the present disclosure provides a pharmaceutical combination comprising a chemotherapeutic agent and the bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET). In certain aspects, the present disclosure provides a pharmaceutical composition comprising a chemotherapeutic agent and instructions for the use of said chemotherapeutic agent in the treatment of cancer with instructions for use of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) in the treatment of said cancer. In certain aspects, the present disclosure provides a pharmaceutical composition comprising a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and instructions for the use of said bispecific antibody in the treatment of cancer with instructions for use of a chemotherapeutic agent in the treatment of said cancer. In certain aspects, the present disclosure provides a kit-of-parts comprising a pharmaceutical composition comprising a chemotherapeutic agent, a bispecific antibody of the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), and instructions for use of said bispecific antibody and for said chemotherapeutic agent in the treatment of cancer. In certain aspects, the present disclosure provides a method of treating cancer in a subject, comprising - identifying a subject as having an acquired, third generation EGFR tyrosine kinase inhibitor resistance, such as to osimertinib, and - administering to the subject a therapeutically effective amount of said bispecific antibody and a chemotherapeutic agent, thereby treating the cancer in the subject. In certain aspects, the present disclosure provides a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in the treatment of cancer in a subject, said treatment comprising - providing a sample from the cancer of said subject, and - determining the presence or absence of an acquired tyrosine kinase inhibitor resistance in the sample, wherein if the sample is determined to comprise the presence of said acquired tyrosine kinase inhibitor resistance, said subject is administered a therapeutically effective amount of said bispecific antibody and of said chemotherapeutic agent thereby treating the cancer in the subject. In certain aspects, the present disclosure provides a method of treating a subject having cancer, comprising - providing a sample from the cancer of said subject, and - determining the presence or absence of an acquired tyrosine kinase inhibitor resistance in the sample, wherein if the sample is determined to comprise the presence of said resistance, said subject is administered an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent, thereby treating the cancer in the subject. In certain aspects, the present disclosure provides a method of treating cancer in a subject identified as having an acquired tyrosine kinase inhibitor resistance, such as to osimertinib, comprising administering to the subject an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent, thereby treating the cancer in the subject. Said composition comprising said bispecific antibody may be contained in a holder that is separate, meaning not physically linked, from a holder that contains said a chemotherapeutic agent. In certain aspects, said bispecific antibody is intended for administration to a subject separate from any other pharmaceutical composition, including said a chemotherapeutic agent. In certain aspects, said chemotherapeutic agent to be administered is or comprises a platinum-based compound and / or a taxane. In certain aspects, said platinum-based compound comprises carboplatin and said taxane comprises paclitaxel and docetaxel. In certain aspects, said chemotherapeutic agent to be administered comprises both paclitaxel and carboplatin. In certain aspects, said chemotherapeutic agent comprises docetaxel. In certain aspects, said cancer is an advanced or a metastatic cancer. In certain aspects, said cancer is lung cancer. In certain aspects, said cancer is non-small cell lung cancer. In certain aspects, said subject or cancer has previously been treated with a third generation EGFR tyrosine kinase inhibitor, such as osimertinib (AZD9291), olmutinib (HM61713), furmonertinib, befotertinib, alflutinib (AST2818), almonertinib (HS-10296) or lazertinib (YH25448 / GNS‑1480). In certain aspects, said subject or cancer has been previously treated with osimertinib. In certain aspects, said subject or cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor, such as osimertinib (AZD9291), olmutinib (HM61713), furmonertinib, befotertinib, alflutinib (AST2818), almonertinib (HS-10296) or lazertinib (YH25448 / GNS‑1480). In certain aspects, said subject or cancer is resistant to treatment with osimertinib. In certain aspects, said subject or cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor but said subject or cancer has not been previously treated with a chemotherapeutic agent. In certain aspects, said cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor and to a chemotherapeutic agent and / or said subject has not received prior treatment with a chemotherapeutic agent. In certain aspects, the subject is a human subject. In certain aspects, said cancer or subject comprises an EGFR-dependent or EGFR- related resistance, such as an approved EGFR tyrosine kinase inhibitor resistance mutation, a tertiary EGFR tyrosine kinase inhibitor resistance mutation, a mutation that reduces binding of a third generation tyrosine kinase inhibitor to EGFR, an acquired EGFR tyrosine kinase inhibitor resistance mutation or an EGFR gene amplification. Said EGFR tyrosine kinase inhibitor is in certain aspects a third generation EGFR tyrosine kinase inhibitor, such as osimertinib. In certain aspects, said cancer or subject comprises an EGFR-dependent or EGFR- related resistance to osimertinib, such as an approved tyrosine kinase inhibitor resistance mutation, a tertiary tyrosine kinase inhibitor resistance mutation, a mutation that reduces binding of a third generation tyrosine kinase inhibitor to EGFR, an acquired tyrosine kinase inhibitor resistance mutation or an EGFR gene amplification. Said tyrosine kinase inhibitor is in certain aspects a third generation EGFR tyrosine kinase inhibitor, such as osimertinib. In certain aspects, said cancer or subject comprises a cMET-dependent or cMET- related resistance to osimertinib, such as a cMET amplification, cMET overexpression, increased signaling of the cMET pathway, a cMET gene amplification and / or increased cMET protein activity. In certain aspects, treatment of said subject having cancer comprises a diagnostic step for assessing whether said cancer is an EGFR positive and / or cMET positive cancer. In certain aspects, treatment of said subject having cancer comprises a diagnostic step for assessing the presence of an acquired tyrosine kinase inhibitor resistance, such as to osimertinib. Said diagnosis comprises assessing the presence of an EGFR- dependent or EGFR related-resistance mutation, amplification or overexpression, or a cMET-dependent or cMET-related resistance mutation, amplification or overexpression. In certain aspects, the present disclosure provides a pharmaceutical combination comprising a chemotherapeutic agent and a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET). In certain aspects, the pharmaceutical combination comprises instructions for use. The disclosure also provides a bispecific antibody as included in the treatment of the present disclosure that comprises a first variable domain that can bind an extracellular part of epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYX1X2NTNYAQKLQG and a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY wherein X1 = N or S; X2 = A or G; X3 = D or G; X4 = R, S or Y; X5 = H, L or Y; X6 = D or W and X7 = D or G with 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof at a position other than X1-X7 and wherein the second variable domain comprises a heavy chain variable region with the amino acid sequence of one of the sequences of SEQ ID NO: 1-23 (Figure 3) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects, the bispecific antibody of the present disclosure comprises or is pamvatamig (cf. WHO Drug Information, Vol. 37, No. 2, 2023 Proposed INN: List 129). The disclosure further provides a pharmaceutical combination, or a kit-of-parts, that comprises a bispecific antibody combined with a chemotherapeutic agent as disclosed herein. The pharmaceutical combination is in certain aspects not physically linked and comprises a container containing the antibody of the present disclosure and a container containing the chemotherapeutic agent. The pharmaceutical combination is in certain aspects accompanied by instructions for use. The instructions for use include clinically relevant information, such as instructions for intravenous administration, dosing amount and an interval of administration. In certain aspects, the chemotherapeutic agent such as paclitaxel, carboplatin and docetaxel, are administered according to the instructions for use as approved by relevant authorities. In certain aspects, the bispecific antibody of the present disclosure is administered with the chemotherapeutic agent of the present disclosure, such as paclitaxel and carboplatin, and the chemotherapeutic agent is administered according to the instructions for use as approved by relevant authorities. In certain aspects, the bispecific antibody of the present disclosure is administered with docetaxel and the chemotherapeutic agent is administered according to the instructions for use as approved by relevant authorities. In certain aspects, the bispecific antibody of the present disclosure is dosed at 600 mg, 1000 mg, 1500 mg or 2000 mg. In certain aspects, said bispecific antibody is provided once every two weeks. In certain aspects, said bispecific antibody is dosed at 1500 mg or 2000 mg and provided once every two weeks. In certain aspects, paclitaxel is administered in an amount of between 100 and 200 mg / m2body surface and carboplatin at AUC 3, AUC 4 or AUC 5 once every three weeks. In certain aspects, docetaxel is administered in an amount of between 40 and 75 mg / m2 body surface once every three weeks. In certain aspects, the bispecific antibody of the disclosure may be administered simultaneously, sequentially or separately with said chemotherapeutic agent of the present disclosure. In certain aspects, said chemotherapeutic agent of the present disclosure is administered prior to, simultaneously with, or after administration of said bispecific antibody. DETAILED DESCRIPTION OF THE INVENTION In certain aspects, the present disclosure provides a combination of the bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in a method of treatment of a cancer. In certain aspects, the present disclosure provides a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) for use in a method of treatment of a cancer in a subject, wherein the method further comprises administering of a chemotherapeutic agent to said subject for treatment of said cancer. In certain aspects, the present disclosure provides a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) for use in a method of treatment of a cancer in a subject, in combination with a chemotherapeutic agent. In certain aspects, the present disclosure provides a method of treatment of a subject having a cancer, comprising administering to the subject an effective amount of a combination of at least one chemotherapeutic agent and the bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET). In certain aspects, the present disclosure provides a method of treating a subject having a cancer, said treatment comprises administering to the subject a combination therapy, wherein the combination therapy comprises an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of at least one chemotherapeutic agent. In certain aspects, the present disclosure provides the use of a bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind (or binds) an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent in the manufacture of a medicament for the treatment of a cancer. In certain aspects, the present disclosure provides the use of a bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind (or binds) an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET) in the manufacture of a medicament for increasing the effect of a chemotherapeutic agent for the treatment of cancer. In certain aspects, the present disclosure provides the use of a chemotherapeutic agent in the manufacture of a medicament for increasing the effect of a bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind (or binds) an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) for the treatment of cancer. In certain aspects, the present disclosure provides a product comprising a chemotherapeutic agent and a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET). In certain aspects, the present disclosure provides a pharmaceutical composition comprising a chemotherapeutic agent and instructions for the use of said chemotherapeutic agent with a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) in the treatment of said cancer. In certain aspects, the present disclosure provides a pharmaceutical composition comprising a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and instructions for the use of said bispecific antibody with a chemotherapeutic agent in the treatment of said cancer. In certain aspects, the present disclosure provides a pharmaceutical composition for the treatment of a cancer, comprising a bispecific antibody of the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a pharmaceutical composition for the treatment of said cancer, comprising a chemotherapeutic agent. In certain aspects, the present disclosure provides a pharmaceutical composition for use in the treatment of cancer comprising a bispecific antibody of the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), wherein the pharmaceutical composition is administered in combination with a chemotherapeutic agent. In certain aspects, the present disclosure provides a pharmaceutical composition for the treatment of a cancer comprising a bispecific antibody of the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), wherein a subject to be treated in the treatment is administered a chemotherapeutic agent prior to, simultaneously with, or after administration of said bispecific antibody. In certain aspects, the present disclosure provides a pharmaceutical composition for the treatment of a cancer in a subject comprising a chemotherapeutic agent, wherein said subject to be treated in the treatment is administered a bispecific antibody of the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) prior to, simultaneously with, or after administration of said chemotherapeutic agent. In certain aspects, the present disclosure provides a kit-of-parts comprising a pharmaceutical composition comprising a chemotherapeutic agent, a bispecific antibody of the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), and instructions for use of said chemotherapeutic agent with said bispecific antibody in the treatment of said cancer. In certain aspects, the present disclosure provides a pharmaceutical composition comprising a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and instructions for the use of said bispecific antibody with a chemotherapeutic agent in the treatment of said cancer. The present disclosure thus relates to a combination of medicaments for the treatment of cancer in a subject which comprises administration to said subject of multiple, different medicaments for treating said cancer, which treatment comprises simultaneous, sequential or separate administration of said medicaments. And said medicament comprises a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto- Oncogene, Receptor Tyrosine Kinase (cMET), and said other, different medicament comprises a chemotherapeutic agent. In certain aspects, the bispecific antibody of the disclosure may be administered simultaneously, sequentially or separately with the chemotherapeutic agent of the present disclosure. Said combination of the bispecific antibody according to the present disclosure and chemotherapeutic agent thus encompasses simultaneous, sequential or separate administration. In certain aspects, when administration of said bispecific antibody and said chemotherapeutic agent is on the same day, said bispecific antibody is administered prior to said chemotherapeutic agent. In certain aspects, a chemotherapeutical agent for use in the combination treatment of the present disclosure is to be understood as consisting of one or two of said agents. In certain aspects, said chemotherapeutical agent consists of either both paclitaxel and carboplatin or of docetaxel. Hence, in certain aspects, the present disclosure provides a bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) for use in a method of treatment of a cancer, wherein the treatment further comprises administering of a chemotherapeutic agent, wherein optionally the bispecific antibody of the present disclosure is administered simultaneously, sequentially or separately with the chemotherapeutic agent of the present disclosure. In certain aspects, when administration of said bispecific antibody and said chemotherapeutic agent is on the same day, said bispecific antibody is administered prior to said chemotherapeutic agent. Hence, in certain aspects, the present disclosure provides a method of treatment of a subject having a cancer, comprising administering to the subject an effective amount of a chemotherapeutic agent and the bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), wherein optionally the bispecific antibody of the present disclosure is administered simultaneously, sequentially or separately with the chemotherapeutic agent of the present disclosure. Hence, in certain aspects, the present disclosure provides the use of a bispecific antibody according to the present disclosure that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind (or binds) an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent in the manufacture of a medicament for the treatment of a cancer, wherein optionally the bispecific antibody of the present disclosure is administered simultaneously, sequentially or separately with the chemotherapeutic agent of the present disclosure. In certain aspects, the bispecific antibody of the present disclosure is administered prior to, simultaneously with, or after administration of said a chemotherapeutic agent. In certain aspects, when administration of said bispecific antibody and said chemotherapeutic agent is on the same day, said bispecific antibody is administered prior to said chemotherapeutic agent. In certain aspects, the bispecific antibody according to the present disclosure is for use in the manufacture of a medicament for the treatment of a cancer and the chemotherapeutic agent are for use in the manufacture of a medicament for the treatment of said cancer, wherein optionally the bispecific antibody of the present disclosure is administered simultaneously, sequentially or separately with the chemotherapeutic agent. Optionally, the bispecific antibody of the present disclosure is administered prior to, simultaneously with, or after administration of said a chemotherapeutic agent. In certain aspects, when administration of said bispecific antibody and said chemotherapeutic agent is on the same day, said bispecific antibody is administered prior to said chemotherapeutic agent. EGFR is a member of a family of four receptor tyrosine kinases (RTKs), named Her- or cErbB-1, -2, -3 and -4. The EGFR has an extracellular domain (ECD) that is composed of four sub-domains, two of which are involved in ligand binding and one of which is involved in homo-dimerization and hetero-dimerization Ferguson (2008). The reference numbers used in this section refer to the numbering of the references in the list headed “cited in the specification”, which are each incorporated by reference. EGFR integrates extracellular signals from a variety of ligands to yield diverse intracellular responses (Yarden at al. 2001; and Jorissen et al. 2003). The EGFR is implicated in several human epithelial malignancies, notably cancers of the breast, bladder, non-small cell lung cancer lung, colon, ovarian head and neck and brain. Activating mutations in the gene have been found, as well as over-expression of the receptor and of its ligands, giving rise to autocrine activation loops (for review, see Robertson et al. 2000). This RTK has therefore been extensively used as target for cancer therapy. Both small-molecule inhibitors targeting the RTK and monoclonal antibodies (mAbs) directed to the extracellular ligand-binding domains have been developed and have shown hitherto several clinical successes, albeit mostly for a select group of patients. Database accession numbers for the human EGFR protein and the gene encoding it are (GenBank NM_005228.3). Other database identifiers for the gene and / or protein are HGNC: 3236; Entrez Gene: 1956; Ensembl: ENSG00000146648; OMIM: 131550 and UniProtKB: P00533. The accession numbers are primarily given to provide a further method of identification of EGFR protein as a target, the actual sequence of the EGFR protein bound by an antibody may vary, for instance because of a mutation in the encoding gene such as those occurring in some cancers or the like. Where reference herein is made to EGFR, the reference refers to human EGFR unless otherwise stated. The antigen- binding site that binds EGFR, binds EGFR and a variety of variants thereof such as those expressed on some EGFR positive tumors. The term “EGFR ligand” as used herein refers to polypeptides which bind and activate EGFR. Examples of EGFR ligands include, but are not limited to EGF, TGF-α, HB-EGF, amphiregulin, betacellulin and epiregulin (for review Olayioye MA et al. (2000)). The term includes biologically active fragments and / or variants of a naturally occurring polypeptide Cancers or subjects having cancer of the present disclosure In certain aspects, said cancer is an advanced or a metastatic cancer and said subject is afflicted with an advanced or a metastatic cancer. In certain aspects, said cancer is lung cancer. In certain aspects, said cancer of which said subject suffers is non- small cell lung cancer. The cancer or tumor may be an EGFR positive tumor, a cMET positive tumor or an EGFR and cMET positive tumor. In certain aspects, said cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor. The tumor may be resistant to treatment with an EGFR tyrosine kinase inhibitor. In certain aspects, the EGFR tyrosine kinase inhibitor is a third generation EGFR tyrosine kinase inhibitor. Examples of clinically relevant or clinically tested third generation EGFR tyrosine kinase inhibitors are osimertinib, lazertinib, alflutinib, rezivertinib, olmutinib, almonertinib, abivertinib, ASK120067, befotertinib, rociletinib, oritinib (SH-1028), nazartinib (EGF816), naquotinib (ASP8273), furmonertinib, mavelertinib (PF-0647775), olafertinib (CK-101), keynatinib or ES-072. In certain aspects, clinically relevant or clinically tested third generation EGFR tyrosine kinase inhibitors of the present disclosure are osimertinib, lazertinib, alflutinib, rezivertinib, olmutinib, almonertinib, abivertinib, ASK120067, befotertinib, oritinib (SH-1028), nazartinib (EGF816), furmonertinib, mavelertinib (PF-0647775), olafertinib (CK-101), keynatinib or ES-072. In certain aspects the third generation EGFR tyrosine kinase inhibitor is osimertinib. In certain aspects the tyrosine kinase inhibitor is lazertinib. In certain aspects the tyrosine kinase inhibitor is almonertinib. In certain aspects the tyrosine kinase inhibitor is befotertinib. In certain aspects, said cancer has previously been treated with said third generation EGFR tyrosine kinase inhibitor, such as osimertinib. In certain aspects, said cancer has been previously treated with osimertinib. In certain aspects, said cancer is resistant to treatment with osimertinib. In certain aspects, said cancer or subject has not been previously treated with a chemotherapeutic agent and / or said subject has not received prior treatment with a chemotherapeutic agent. In certain aspects, said subject or cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor but said subject or cancer has not been previously treated with a chemotherapeutic agent. In this aspect, treatment according to the present disclosure comprises second line treatment. In certain aspects, said subject or cancer is resistant to treatment with a third-generation EGFR tyrosine kinase inhibitor, such as osimertinib, but said subject has not received prior chemotherapy or said cancer has not been previously treated with a chemotherapeutic agent. In other words, said subject is chemotherapy naïve. Said aspect thus relates to a subject or population of subjects having NSCLC who are osimertinib resistant and chemotherapy naïve. In certain aspects, said subject who is resistant to treatment with the third- generation EGFR tyrosine kinase inhibitor, such as osimertinib, but chemotherapy naïve, is administered a bispecific antibody of the present disclosure and paclitaxel and carboplatin as second line treatment. Although chemotherapy can bring benefits to lung cancer patients, the median progression-free survival time has been reported to be only 5.5 months (West et al., 2019), and drug resistance is inevitable. And although many studies have explored the mechanism of platinum drug resistance, there is still no clear mechanism or targets of platinum drug resistance leaving an unmet clinical need. Hence, in certain aspects, treatment according to the present disclosure comprises third line treatment to a subject which has received prior platinum-based chemotherapy. In certain aspects, said cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor and to said chemotherapeutic agent. In this aspect, treatment according to the present disclosure comprises third line treatment. In certain aspects, said subject or cancer is resistant to treatment with a third-generation EGFR tyrosine kinase inhibitor, such as osimertinib, and resistant to chemotherapy, such as resistant to platinum-based chemotherapy. In certain aspects, said subject or cancer is resistant to treatment with a third-generation EGFR tyrosine kinase inhibitor, such as osimertinib, and chemotherapy resistant, in particular platinum-based chemotherapy. In certain aspects, said subject has non-small cell lung cancer (NSCLC) which is chemotherapy resistant and resistant to treatment with a third-generation EGFR tyrosine kinase inhibitor, such as osimertinib. Said aspect thus relates to a subject or population of subjects having NSCLC who are osimertinib and platinum resistant. In certain aspects, said subject who is resistant to treatment with the third-generation EGFR tyrosine kinase inhibitor, such as osimertinib, and said chemotherapy, is administered a bispecific antibody of the present disclosure and docetaxel as third line treatment. Aberrantly activated forms of EGFR, for instance via mutations in EGFR or EGFR gene amplification, are known to be oncogenic drivers in non-small cell lung cancer (NSCLC) and known to occur in the treatment with third generation EGFR tyrosine kinase inhibitors. The present disclosure provides a combination treatment wherein the antibody of the present disclosure is administered in combination with a chemotherapeutic agent to treat such oncogenic drivers of EGFR. In certain aspects, said EGFR tyrosine kinase inhibitor resistance comprises a resistance to a third generation EGFR tyrosine kinase inhibitor, such as osimertinib. In certain aspects, said third generation EGFR tyrosine kinase inhibitor resistance is an EGFR-dependent and / or cMET dependent resistance. In certain aspects, the cancer or subject has received prior treatment with osimertinib and has an acquired or tertiary osimertinib resistance. Said prior osimertinib treatment is in certain aspects first line therapy. In certain aspects, said first line therapy is followed by treatment with a combination of the present disclosure as a second line treatment or as third line treatment to a subject that has received prior platinum-based chemotherapy as second line treatments. Herein, the term “refractory” refers to a disease that does not respond to a treatment. A refractory disease can be resistant to a treatment before or at the beginning of the treatment, or a refractory disease can become resistant during a treatment. Herein the term “resistant” refers to a cancer or patient which is not responding to treatment when administered the prescribed dose of the therapeutic agent involved. Herein, the term “3rd generation EGFR tyrosine kinase inhibitor” (3rd generation TKI) refers to covalent irreversible EGFR inhibitors such as osimertinib and lazertinib which are selective to the EGFR activating mutations, such as deletions in exon 19 and exon 21 L858R, alone or in combination with T790M mutation and have lower inhibitory activity against wild-type EGFR. In certain aspects, the cancer or subject comprises an EGFR-dependent resistance, such as an approved tyrosine kinase inhibitor resistance mutation, a tertiary tyrosine kinase inhibitor resistance mutation, a mutation that reduces binding of a third generation tyrosine kinase inhibitor to EGFR, an acquired tyrosine kinase inhibitor resistance mutation, an EGFR gene amplification, or a cMET-dependent resistance. In certain aspects, the cancer or subject comprises an approved EGFR tyrosine kinase inhibitor resistance mutation. Herein, the term “approved tyrosine kinase inhibitor resistance mutation” means a resistance which develops after progression on an EGFR tyrosine kinase inhibitor which is presently approved for treatment of cancer. Examples of approved third-generation EGFR tyrosine kinase inhibitors are osimertinib (AZD9291), olmutinib (HM61713), furmonertinib, befotertinib, alflutinib (AST2818), almonertinib (HS-10296) or lazertinib (YH25448 / GNS‑1480). Resistance mechanisms to third-generation EGFR tyrosine kinase inhibitors are well known and have for instance been described by Minari et al (Transl. Lung Cancer Res 2016;5(6):695-708) or by Leonetti et al (British Journal of Cancer (2019) 121:725– 737). Herein, resistance to osimertinib includes EGFR-dependent resistance, EGFR- independent resistance, such as cMET-dependent resistance, HER2 amplification, resistance via RAS-MAPK pathway activation, resistance via PI3K pathway activation, cell-cycle gene alterations and oncogenic fusions. In certain aspects, the cancer or subject comprises an EGFR-dependent resistance to osimertinib selected from a tertiary tyrosine kinase inhibitor resistance, a mutation that reduces binding of a third generation tyrosine kinase inhibitor to EGFR, an acquired tyrosine kinase inhibitor resistance mutation, an EGFR amplification, In certain aspects, the cancer or subject comprises a cMET-dependent resistance to osimertinib such as a cMET amplification. In certain aspects, the cancer or subject comprises a tertiary EGFR tyrosine kinase inhibitor resistance mutation, such as L718X (e.g. L718Q), G719X (e.g. G719A), L792X (e.g. L792H), G796X (e.g. G796R, G796S, G796D), or C797X (e.g. C797S, C797G). Herein, the term “tertiary EGFR tyrosine kinase inhibitor resistance mutation” means a resistance which develops after progression on a third-generation EGFR tyrosine kinase inhibitor. In certain aspects, the cancer or subject comprises a mutation that reduces binding of a third generation EGFR tyrosine kinase inhibitor to EGFR, such as L792X (e.g. L792H , L792F, L792Y), or L718X (e.g. L718Q). In certain aspects, the cancer or subject comprises an acquired EGFR tyrosine kinase inhibitor resistance mutation to osimertinib (such as C797X, L792X, G796X, G724X, S768X, L718X or an exon 20 insertion mutation), in certain aspects a mutation which confers resistance to osimertinib or which occurred after progression on osimertinib, includes L718X (e.g. L718Q), G724X (e.g. G724S), S768X (e.g. S768I), L792X (e.g. L792H , L792F, L792Y), C797X (including C797S and C797G), or L798X (e.g. L798I). Herein, the term “ acquired EGFR tyrosine kinase inhibitor resistance mutation” means a resistance which is acquired after progression on treatment with an EGFR tyrosine kinase inhibitor, such as after progression on a third-generation EGFR tyrosine kinase inhibitor. In certain aspects, the cancer or subject comprises an EGFR gene amplification, such as an increase in EGFR mRNA or amplification of the wildtype EGFR allele, such as in combination with the presence of an EGFR-ex19del allele after progression on osimertinib. In certain aspects, the cancer or subject comprises an EGFR exon 20 mutation, in certain aspects an exon 20 insertion mutation, in certain aspects an in-frame exon 20 insertion mutation. In certain aspects, the cancer or subject comprises an EGFR mutation including an exon 20 mutation, an exon 20 insertion, or a mutation selected from L692X (e.g. L692V), E709X (e.g. E709K), L718X (e.g. L718Q, L718V), G719X (e.g. G719A), G724X (e.g. G724S), S768X (e.g. S768I), L792X (e.g. L792H, L792F, L792R, L792Y, L792V, L792P), G796X (e.g. G796S, G796D, G796R), C797X (e.g. C797S, C797G), L798X (e.g. L798I), L817Q, and L844X (e.g. L844V). In certain aspects, the cancer or subject comprises an EGFR mutation including an exon 20 mutation, an exon 20 insertion, or an osimertinib resistance mutation selected from L718X (e.g. L718Q, L718V), G719X (e.g. G719A), G724X (e.g. G724S), S768X (e.g. S768I), L792X (e.g. L792H, L792F, L792R, L792Y, L792V, L792P), G796X (e.g. G796S, G796D, G796R), C797X (e.g. C797S, C797G), and L817X (e.g. L817Q). In certain aspects, the cancer or subject comprises EGFR mutation C797X (e.g. C797S, C797G, C797N). In certain aspects, the cancer or subject comprises EGFR mutation C797S. In certain aspects, the cancer or subject comprises an EGFR mutation conferring resistance to osimertinib, such as C797X or L792X, and a further mutation including an exon 19 deletion, T790M or L858R. In certain aspects, the cancer or subject comprises a double or triple mutation selected from exon19del / L792X (e.g. exon19del / L792H, exon19del / L792F, exon19del / L792Y), exon19del / C797X (e.g. exon19del / C797S), L858X / T790X / C792X (e.g.L858R / T790M / C792H, L858R / T790M / C792F, L858R / T790M / C792Y), L858X / T790X / C797X (e.g. L858R / T790M / C797S), L858X / T790X / L718X (e.g. L858R / T790M / L718Q), exon19del / T790X / C797X (e.g. exon19del / T790M / C792H, exon19del / T790M / C792F, exon19del / T790M / C792Y), exon19del / T790X / C797X (e.g. exon19del / T790M / C797S), and exon19del / T790X / C718X (e.g. exon19del / T790M / C718Q). In certain aspects, the cancer or subject comprises an EGFR gene amplification, such as an increase in EGFR mRNA or amplification of the wildtype EGFR allele in combination with the presence of an EGFR-ex19del allele after progression on osimertinib. cMET, also called tyrosine-protein kinase MET or hepatocyte growth factor receptor (HGFR), is a protein that in humans is encoded by the MET gene. The protein possesses tyrosine kinase activity. The primary single chain precursor protein is post- translationally cleaved to produce the alpha and beta subunits, which are disulfide linked to form the mature receptor. Dysregulation of, or aberrantly activated cMET may induce tumor growth, the formation of new blood vessels (angiogenesis) that supply the tumor with nutrients, and cancer spread to other organs (metastasis). cMET is deregulated in many types of human malignancies, including cancers of kidney, liver, stomach, breast, and brain. The cMET gene is known under a number of different names such as MET Proto-Oncogene, Receptor Tyrosine Kinase; Hepatocyte Growth Factor Receptor; Tyrosine-Protein Kinase Met; Scatter Factor Receptor; Proto-Oncogene C-Met; HGF / SF Receptor; HGF Receptor; SF Receptor; EC 2.7.10.1; Met Proto-Oncogene; EC 2.7.10; DFNB97; AUTS9; RCCP2; C- Met; MET; HGFR; External Ids for cMET are HGNC: 7029; Entrez Gene: 4233; Ensembl: ENSG00000105976; OMIM: 164860 and UniProtKB: P08581. The accession numbers are primarily given to provide a further method of identification of cMET protein as a target, the actual sequence of the cMET protein bound by an antibody may vary, for instance because of a mutation in the encoding gene such as those occurring in some cancers or the like. Where reference herein is made to cMET, the reference refers to human cMET unless otherwise stated. The antigen-binding site that binds cMET, binds cMET and a variety of variants thereof such as those expressed on some cMET positive tumors. Examples of cMET aberrations or dysregulation include cMET amplification, cMET overexpression, increased signaling of the cMET pathway, cMET gene amplification and / or increased cMET protein activity. Also, cMET dysregulation may be caused by increased HGF expression. Dysregulation of c-MET is an established driver of tumor invasion, angiogenesis, and metastasis (Birchmeier et al., 2003). Three types of biological alterations of c-MET can lead to oncogenesis: amplification, mutation and fusion. These genomic alterations are found principally as either primary or secondary drivers of tumor growth and such aberrations have been reported to occur after treatment of cancer patients with EGFR tyrosine kinase inhibitors (cf. Suzawa et al., DOI: 10.1200 / PO.19.00011 JCO Precision Oncology - May 10, Vol 3, 2019). In certain aspects, the cancer or subject comprises a cMET-dependent resistance such as a cMET amplification, cMET overexpression, increased signaling of the cMET pathway, a cMET gene amplification and / or increased cMET protein activity. In certain aspects, said cancer is NSCLC and said cMET amplification is characterized by cMET / CEP7 > 5 or cfDNA ≥ 2 copies or any combination thereof. In certain aspects, the cancer or subject comprises a cMET-dependent resistance such as a cMET amplification. In certain aspects, said cMET amplification is determined by FISH or next-generation sequencing to establish gene copy number (GCN) or the cMET / CEP7 ratio. In certain aspects, said cMET amplification is characterized by a MET / CEP7 ratio of 2 or more, such as 3 or more, in certain aspects MET / CEP7 ratio of 4 or more, in certain aspects MET / CEP7 ratio of 5 or more and up to 15 or 20. In certain aspects, said cMET amplification is characterized by a MET / CEP7 ratio of 2 or more, up to 15 or 20. In certain aspects, said cMET amplification is characterized by a MET / CEP7 ratio of 3 or more, up to 15 or 20. In certain aspects, said cMET amplification is characterized by a MET / CEP7 ratio of 4 or more, up to 15 or 20. In certain aspects, said cMET amplification is characterized by a MET / CEP7 ratio of 5 or more, up to 15 or 20. In certain aspects, the treatment of a subject is preceded by a step of diagnosing said subject of having cancer characterized by a MET / CEP7 ratio of between 2 or 3 and 15, followed by treatment with the therapeutic agents of the present disclosure. In certain aspects, said cMET amplification is characterized by cfDNA of at least 1.8 cMET copies or more, such as between at least 1.8 and at most 2.2, or between at least 2.2 and at most 5, or at least 5 and higher. In certain aspects, the treatment of a subject is preceded by a step of diagnosing said subject of having cancer characterized by a cfDNA cMET score of at least 1.8 cMET copies or up to 5, followed by treatment with the therapeutic agents of the present disclosure. In certain aspects, said cMET amplification is characterized by a cMET GCN of between 2 and 12.7. In certain aspects, the treatment of a subject is preceded by a step of diagnosing said subject of having cancer characterized by a cMET GNC score between 2 and 12.7, followed by treatment with the therapeutic agents of the present disclosure. Therapeutic agents of the present disclosure As used herein, the term “therapeutic agent” refers to said bispecific agent of the present disclosure and a chemotherapeutic agent. In certain aspects, said agents manifest a therapeutically superior outcome to the outcome achieved by each individual constituent of the combination when used alone. In this context a therapeutically superior outcome includes one or more of the following (a) an increase in therapeutic response that is greater than either or both of the separate effects of each agent alone at the same dose as in the combination; (b) a decrease in the dose of one or more agents in the combination without a decrease in therapeutic efficacy; (c) a decrease in the incidence of adverse events while receiving a therapeutic benefit that is equal to or greater than the monotherapy of each agent at the same dose as in the combination, (d) a reduction in dose-limiting toxicities while receiving a therapeutic benefit that is greater than the monotherapy of each agent; (e) a delay or minimization of the induction of drug resistance. Methods for the safe and effective administration of chemotherapeutic agents are known to those skilled in the art. In addition, their administration is described in the standard literature. For example, the administration of many of the chemotherapeutic agents is described in the Physicians' Desk Reference (PDR), e.g., 1996 edition (Medical Economics Company, Montvale, N.J. 07645-1742, USA); the disclosure of which is incorporated herein by reference thereto. It will be apparent to those skilled in the art that the administration of the chemotherapeutic agent(s) can be varied depending on the known effects of the chemotherapeutic agent(s) on that disease. Also, in accordance with the knowledge of the skilled clinician, the therapeutic protocols (e.g., dosage amounts and times of administration) can be varied in view of the observed effects of the administered therapeutic agents on the patient, and in view of the observed responses of the disease to the administered therapeutic agents. The terms “treat,” “treating,” and “treatment,” as used herein, refer to any type of intervention or process performed on, or administering an active agent or combination of active agents to the subject with the objective of reversing, alleviating, ameliorating, inhibiting, or slowing down or preventing the progression, development, severity or recurrence of a symptom, complication, condition or biochemical indicia associated with a disease. As used herein, "effective treatment" or "positive therapeutic response" refers to a treatment producing a beneficial effect, e.g., amelioration of at least one symptom of a disease or disorder, e.g., cancer. A beneficial effect can take the form of an improvement over baseline, including an improvement over a measurement or observation made prior to initiation of therapy according to the method. For example, a beneficial effect can take the form of slowing, stabilizing, stopping or reversing the progression of a cancer in a subject at any clinical stage, as evidenced by a decrease or elimination of a clinical or diagnostic symptom of the disease, or of a marker of cancer. Effective treatment may, for example, decrease in tumor size, decrease the presence of circulating tumor cells, reduce or prevent metastases of a tumor, slow or arrest tumor growth and / or prevent or delay tumor recurrence or relapse. The term “effective amount” or "therapeutically effective amount" refers to an amount of an agent or combination of agents that provides the desired biological, therapeutic, and / or prophylactic result. That result can be reduction, amelioration, palliation, lessening, delaying, and / or alleviation of one or more of the signs, symptoms, or causes of a disease, or any other desired alteration of a biological system. In terms of tumor development, an effective amount is an amount sufficient to delay tumor development. In terms of tumor recurrence, an effective amount is an amount sufficient to prevent or delay tumor recurrence. An effective amount can be administered in one or more administrations. The effective amount of the agent or composition may: (i) reduce the number of cancer cells; (ii) reduce tumor size; (iii) inhibit, retard, slow to some extent and may stop cancer cell infiltration into peripheral organs; (iv) inhibit tumor metastasis; (v) inhibit tumor growth; (vi) prevent or delay occurrence and / or recurrence of tumor; and / or (vii) relieve to some extent one or more of the symptoms associated with the cancer. In one aspect, an “effective amount” is the amount of a bispecific antibody or chemotherapeutic agent as disclosed herein as the therapeutic agent to affect a decrease in a cancer (for example a decrease in the number of cancer cells); slowing of progression of a cancer or prevent regrowth or recurrence of the cancer. In certain aspects, said chemotherapeutic agent is or comprises a platinum-based compound and / or a taxane. In certain aspects, said chemotherapeutic agent is or comprises paclitaxel and / or carboplatin. In certain aspects, said chemotherapeutic agent is or comprises docetaxel. An antibody typically recognizes only a part of an antigen. The antigen is typically but not necessarily a protein. The recognition or binding site on an antigen, bound by an antibody is referred to as the epitope, where an epitope may be linear or conformational. Binding of an antibody to an antigen is typically specific. The ‘specificity’ of an antibody refers to its selectivity for a particular epitope, whereas ‘affinity’ refers to the strength of the interaction between the antibody’s antigen binding site and the epitope it binds. Exemplary antibodies of the disclosure binds to EGFR and cMET, in certain aspects human EGFR and human cMET. An EGFR / cMET bispecific antibody of the disclosure binds to EGFR and, under otherwise identical conditions, at least 100-fold less to the homologous receptors ErbB-2 and ErbB-4 of the same species. An EGFR / cMET bispecific antibody of the disclosure binds to cMET and, under otherwise identical conditions, at least 100-fold less to the receptors ErbB-2 and ErbB-4 of the same species. Considering that the receptors are cell surface receptors, the binding may be assessed on cells that express the receptor(s). A bispecific antibody of the present disclosure in certain aspects binds to human, cynomolgus EGFR and / or to mouse EGFR. An antibody that binds EGFR and cMET may bind other proteins as well if such other proteins contain the same epitope. Hence, the term “binding” does not exclude binding of the antibodies to another protein or protein(s) that contain the same epitope. Such binding is typically referred to as cross-reactivity. An EGFR / cMET bispecific antibody typically does not bind to other proteins than EGFR and / or cMET on the membrane of cells in a post-natal, in certain aspects adult human. An antibody according to the present disclosure is typically capable of binding EGFR with a binding affinity (i.e. equilibrium dissociation constant Kd) of at least 1x10e-6 M, as outlined in more detail below. The term “antibody” as used herein means a proteinaceous molecule in certain aspects belonging to the immunoglobulin class of proteins. An antibody typically contains two variable domains that bind an epitope on an antigen. Such domains are derived from or share sequence homology with the variable domain of an antibody. A bispecific antibody of the present disclosure in certain aspects comprises two variable domains. Antibodies for therapeutic use are in certain aspects as close to natural antibodies of the subject to be treated as possible (for instance human antibodies for human subjects). Antibody binding can be expressed in terms of specificity and affinity. The specificity determines which antigen or epitope thereof is specifically bound by the binding domain. Typically, antibodies for therapeutic applications can have affinities of up to 1x10e-10 M or higher. Antibodies such as bispecific antibodies of the present disclosure in certain aspects comprise the constant domains (Fc part) of a natural antibody. An antibody of the present disclosure is typically a bispecific full length antibody, in certain aspects of the human IgG subclass. In certain aspects, the antibodies of the present disclosure are of the human IgG1 subclass. Such antibodies of the present disclosure can have good ADCC properties, have a favorable half-life upon in vivo administration to humans and CH3 engineering technology exists that can provide for modified heavy chains that preferentially form hetero-dimers over homo-dimers upon co-expression in clonal cells. ADCC activity of an antibody can also be improved through techniques known to persons of skill in the art. An antibody of the present disclosure is in certain aspects a “full length” antibody. The term ‘full length’ according to the disclosure is defined as comprising an essentially complete antibody, which however does not necessarily have all functions of an intact antibody. For the avoidance of doubt, a full length antibody contains two heavy and two light chains. Each chain contains constant (C) and variable (V) regions, which can be broken down into domains designated CH1, CH2, CH3, VH, and CL, VL. Typically, an antibody binds to antigen via the variable domains contained in the Fab portion, and after binding can interact with molecules and cells of the immune system through the constant domains, mostly through the Fc portion. Full length antibodies according to the disclosure encompasses antibodies wherein mutations may be present that provide desired characteristics. Antibodies wherein one or several amino acid residues are deleted, without essentially altering the specificity and / or affinity characteristics of the resulting antibody are embraced within the term “full length antibody”. For instance, an IgG antibody can have 1-20 amino acid residue insertions, deletions, or substitutions or a combination thereof in the constant region. In certain aspects, an antibody of the present disclosure is a bispecific IgG antibody, such as a bispecific full length IgG1 antibody or a human IgG1. Full length IgG antibodies are preferred because of their typically favorable half-life and the desire to stay as close to fully autologous (human) molecules for reasons of immunogenicity. In certain aspects, an antibody of the disclosure is a full length IgG1, a full length IgG2, a full length IgG3 or a full length IgG4 antibody. The variable domain that can bind EGFR and that comprises the amino acid sequence of the MF3370 or variant thereof as indicated herein, in certain aspects binds to EGFR domain III (see table 4 of international patent application PCT / NL2015 / 050124; WO2015 / 130172 which is incorporated by reference herein). The variable domain in certain aspects blocks the binding of the ligand EGF to EGFR or competes with the EGF ligand for binding to EGFR. The binding of the variable domain to EGFR can be inhibited by cetuximab. The variable domain binds an epitope that is different from the epitope that is recognized by cetuximab and zalutumumab. For example, the variable domain binds to mouse EGFR whereas cetuximab and zalutumumab do not, indicating that one or more of the residues that differ between mouse and human EGFR domain III play a role in cetuximab and zalutumumab binding, but not in an antibody of the present disclosure. An advantage of a bispecific antibody of the present disclosure having human, mouse, cynomolgus EGFR cross- reactivity is that it permits the use of xenograft studies with human cancer models, which may be more predictive with respect to effectivity and toxicity as the antibody also binds to the normal mouse cells that have the receptor, while also being capable of use in cynomolgus toxicology studies. In one aspect the disclosure provides a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), wherein said first variable domain can also bind mouse EGFR, cynomolgus EGFR or both. A cMET variable domain in certain aspects comprises an amino acid sequence of the MF4356 or variant thereof as indicated herein, and in certain aspects blocks the binding of the antibody MetMab to cMET. The variable domain in certain aspects blocks the binding of the ligand HGF to cMET or competes with the ligand HGF for binding to cMET. The variable domain blocks the binding of the antibody MetMab to cMET when the binding of MetMab to cMET at half-maximum binding conditions is reduced by at least 40% and in certain aspects at least 60% in the presence of a saturating amount of said variable domain. The variable domain is in certain aspects provided in the context of a bivalent monospecific antibody. The cMET variable domain can in certain aspects bind the sema domain of cMET. The cMET variable domain of the disclosure may compete with 5D5 for binding cMET or not compete with reported anti-cMET reference antibodies, such as 5D5. See Table 3. The disclosure also provides a bispecific antibody as included in the treatment of the present disclosure that comprises a first variable domain that can bind an extracellular part of epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET), wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYX1X2NTNYAQKLQG and a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY wherein X1 = N or S; X2 = A or G; X3 = D or G; X4 = R, S or Y; X5 = H, L or Y; X6 = D or W and X7 = D or G with 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof at a position other than X1-X7 and wherein the second variable domain comprises a heavy chain variable region with the amino acid sequence of one of the sequences of SEQ ID NO: 1-23 (Figure 3) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The first variable domain in certain aspects comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and the second variable domain in certain aspects comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. In certain aspects, the antibody of the present disclosure comprises a first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYX1X2NTNYAQKLQG and a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY wherein X1 = N or S; X2 = A or G; X3 = D or G; X4 = R, S or Y; X5 = H, L or Y; X6 = D or W and X7 = D or G; with 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof at a position other than X1-X7. In certain aspects, the antibody of the present disclosure comprises a second variable domain which comprises a heavy chain variable region with the amino acid sequence of one of the sequences of SEQ ID NO: 1-23 (Figure 3) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. Bispecific antibodies are described wherein X1 = N; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = A; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = S; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; X1 = N; X2 = A; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; or X1 = S; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G. In certain aspects, X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D. In certain aspects, X3-X7 = DRHWD and X1 and X2 are NG; SG or NA. Bispecific antibodies are described wherein the heavy chain variable region of the second variable domain comprises the amino acid sequence of one of the sequences of SEQ ID NO: 1-3; 7; 8; 10; 13; 15; 16; 17; 21; 22 or 23 with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. A variable domain of the present disclosure can bind EGFR (the first variable domain) and in certain aspects comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYX1X2NTNYAQKLQG and a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY wherein X1 = N or S; X2 = A or G; X3 = D or G; X4 = R, S or Y; X5 = H, L or Y; X6 = D or W and X7 = D or G. X1-7 is in certain aspects: X1 = N; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = A; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = S; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; X1 = N; X2 = A; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; or X1 = S; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G. In certain aspects X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D. In certain aspects X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D. The first variable domain in certain aspects comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 sequence X3X4X5X6HWWLX7AFDY or a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY. The first variable domain in certain aspects comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY. The first variable domain in certain aspects comprises a heavy chain variable region with the amino acid sequence of MF3353; MF8229; MF8228; MF3370; MF8233; MF8232; MF3393; MF8227 or MF8226 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof with respect to the indicated sequence. In certain aspects the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF3353; MF8229; MF8228; MF3370; MF8233; MF8232; MF3393; MF8227 or MF8226 as depicted in figure 2. In certain aspects, the first variable domain comprises a heavy chain variable region with the CDR1, CDR2, and CDR3 amino acid sequence of MF3353; MF8229; MF8228; MF3370; MF8233; MF8232; MF3393; MF8227 or MF8226 as depicted in figure 2. The variable domain that can bind cMET (the second variable domain) in certain aspects comprises a heavy chain variable region that comprises the amino acid sequence of one of the sequences of SEQ ID NO: 1-23 (Figure 3) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The heavy chain variable region of the second variable domain in certain aspects comprises the amino acid sequence of one of the sequences of SEQ ID NO: 1-3; 7; 8; 10; 13; 15; 16; 17; 21; 22 or 23 with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The heavy chain variable region of the second variable domain in certain aspects comprises the amino acid sequence of one of the sequences of SEQ ID NO: 2; 7; 8; 10; 13 or 23 with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The heavy chain variable region of the second variable domain in certain aspects comprises the amino acid sequence of the sequence of SEQ ID NO: 13 or SEQ ID NO: 23 with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects, the second variable domain comprises a heavy chain variable region with the CDR1, CDR2, and CDR3 amino acid sequence of MF8225 (SEQ ID NO: 1), MF8243 (SEQ ID NO: 2), MF8224 (SEQ ID NO:3), MF8239 (SEQ ID NO: 4), MF8242 (SEQ ID NO: 5), MF8237 (SEQ ID NO: 6), MF8240 (SEQ ID NO: 7), MF8234 (SEQ ID NO: 8), MF8245 (SEQ ID NO: 9), MF8231 (SEQ ID NO: 10), MF8247 (SEQ ID NO: 11), MF8238 (SEQ ID NO: 12), MF8230 (SEQ ID NO: 13), MF8248 (SEQ ID NO: 14), MF8246 (SEQ ID NO: 15), MF8223 (SEQ ID NO: 16), MF8222 (SEQ ID NO: 17), MF8235 (SEQ ID NO: 18), MF8236 (SEQ ID NO: 19), MF8241 (SEQ ID NO: 20), MF8244 (SEQ ID NO: 21), MF8221 (SEQ ID NO: 22), or MF4356 (SEQ ID NO: 23). In certain aspects the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1. In certain aspects the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1. In certain aspects is provided a bispecific antibody that comprises a first variable domain that can bind an extracellular part of EGFR and a second variable domain that can bind an extracellular part of cMET wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1. In certain aspects is provided a bispecific antibody that comprises a first variable domain that can bind an extracellular part of EGFR and a second variable domain that can bind an extracellular part of cMET wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1. In certain aspects is provided a bispecific antibody that comprises a first variable domain that can bind an extracellular part of EGFR and a second variable domain that can bind an extracellular part of cMET wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYSGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1. In certain aspects is provided a bispecific antibody that comprises a first variable domain that can bind an extracellular part of EGFR and a second variable domain that can bind an extracellular part of cMET wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYSGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1. In certain aspects wherein a cMET binding variable domain is described to have a CDR2 sequence “WINTYTGDPTYAQGFTG” the CDR2 sequence can also be “WINTYTGDPTYAQGFT”. In certain aspects, the first and second variable domain of the bispecific antibody as described herein comprises the CDR1, CDR2 and CDR3 of the variable domain of light chain sequences of IgGVK1-39 / JK1 (see figure 4B), numbering such as according to IMGT. In certain aspects, the first and second variable domain of the bispecific antibody as described herein comprises a common light chain, in certain aspects the common light chain variable region of figure 4B. In certain aspects, the CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain as described herein comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1 (according to IMGT). In some of such aspects, the CDR3 comprises the amino acid sequence QQSYSTP. In some aspects of a bispecific antibody as described herein the first and second variable domain comprise a common light chain, in certain aspects a light chain variable region of figure 4B. In another certain aspect an EGFR / cMET bispecific antibody comprises a first variable domain that can bind an extracellular part of human EGFR that comprises the CDR1, CDR2 and CDR3 of the heavy chain variable region of MF3755 depicted in figure 1 and a second variable domain that can bind an extracellular part of human cMET that comprises the CDR1, CDR2 and CDR3 of the heavy chain variable region of MF4297 depicted in figure 1. The light chain variable region in said first and second variable domain is in certain aspects a common light chain variable region as described herein. The CDR1, CDR2 and CDR3 of a light chain of the first and second variable domain in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1 (according to IMGT). In certain aspects the antibody comprises a heavy chain variable region with the amino acid sequence of MF3755 as depicted in figure 1 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof with respect to the indicated sequence. In certain aspects the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF3755 as depicted in figure 1. The variable domain that can bind cMET (the second variable domain) in certain aspects comprises a heavy chain variable region that comprises the amino acid sequence of MF4297 as depicted in figure 1 with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The heavy chain variable region of the second variable domain in certain aspects comprises the amino acid sequence of MF4297 as depicted in figure 1. The term ‘bispecific’ (bs) in the context of the present disclosure means that an antibody is capable of binding two different targets or two epitopes on the same target, for example, where one variable domain of the antibody (as defined above) binds to an epitope on EGFR and a second variable domain binds to an epitope on cMET. Depending on the expression level, (sub-)cellular localization and stoichiometry of the two antigens recognized by a bispecific antibody, both Fab arms of the antibody may or may not simultaneously bind their epitope. One arm of the bispecific antibody typically contains the variable domain of one antibody and the other arm contains the variable domain of another antibody (i.e. one arm of the bispecific antibody is formed by one heavy chain paired with one light chain whereas the other arm is formed by a different heavy chain paired with a light chain). Thus, the stoichiometry of a preferred bispecific antibody of the disclosure is 1:1, EGFR:cMET binding. The heavy chain variable regions of the bispecific antibody of the present disclosure are typically different from each other, whereas the light chain variable regions are the same in certain aspects. A bispecific antibody wherein the different heavy chain variable regions are associated with the same light chain variable region is also referred to as a bispecific antibody with a common light chain variable region (cLcv). It is preferred that the light chain constant region is also the same. Such bispecific antibodies are referred to as having a common light chain (cLc). Further provided is therefore a bispecific antibody according to the present disclosure, wherein both arms comprise a common light chain. The term ‘common light chain’ according to the disclosure refers to two or more light chains in a bispecific antibody which may be identical or have some amino acid sequence differences while the binding specificity of the full length antibody is not affected. It is for instance possible within the scope of the definition of common light chains as used herein, to prepare or find light chains that are not identical but still functionally equivalent, e.g., by introducing and testing conservative amino acid changes, changes of amino acids in regions that do not or only partly contribute to binding specificity when paired with the heavy chain, and the like. The terms ‘common light chain’, ‘common LC’, ‘cLC’, ‘single light chain’ with or without the addition of the term ‘rearranged’ are all used herein interchangeably. The terms ‘common light chain variable region’, ‘common VL’, ‘common LCv’, ‘cLCv’, ‘single VL’ with or without the addition of the term ‘rearranged’ are all used herein interchangeably. In certain aspects of the present disclosure, a bispecific antibody has a common light chain (variable region) that can combine with at least two, and in certain aspects a plurality of heavy chains (variable regions) of different binding specificity to form antibodies with functional antigen binding domains (e.g., WO2009 / 157771). The common light chain (variable region) is in certain aspects a human light chain (variable region). A common light chain (variable region) in certain aspects has a germline sequence. A preferred germline sequence is a light chain variable region that has good thermodynamic stability, yield and solubility. A preferred germline light chain is O12. A common light chain in certain aspects comprises the light chain encoded by a germline human Vk gene segment, and is in certain aspects the rearranged germline human kappa light chain IgVκ1-39*01 / IGJκ1*01 (Figure 4A). The common light chain variable region is in certain aspects the variable region of the rearranged germline human kappa light chain IgVκ1- 39*01 / IGJκ1*01. A common light chain in certain aspects comprises a light chain variable region as depicted in figure 4B, or 4D with 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The common light in certain aspects further comprises a light chain constant region, in certain aspects a kappa light chain constant region. A nucleic acid that encodes the common light chain can be codon optimized for the cell system used to express the common light chain protein. The encoding nucleic acid can deviate from a germ-line nucleic acid sequence. In certain aspects, the bispecific antibody comprises a common light chain. The first and second variable domains comprise the same or substantially the same (common) light chain variable region in certain aspects. Said common light chain variable region may be one that is known to pair well with a diversity of human variable region gene segments that have undergone recombination. In certain aspects, said common light chain is a variable region encoded by a germline Vk gene segment, such as the O12 / IgVκ1-39*01 variable region gene segment. The preferred light chain variable region comprises the rearranged IgVκ1-39*01 / IGJκ1*01 or IgVκ1-39*01 / IGJκ5*01. The light chain of the cMET binding arm and the light chain of the EGFR binding arm is the same (common) light chain in certain aspects. In certain aspects, the common light chain is the rearranged kappa light chain IgVκ1-39*01 / IGJκ1*01 or IgVκ1- 39*01 / IGJκ5*01 joined to a human light chain constant region. The bispecific antibody can be a human antibody. The bispecific antibody can be a full length antibody. It may have one variable domain that can bind EGFR and one variable domain that can bind cMET. In certain aspects, the variable domain that can bind human EGFR can also beneficially bind mouse EGFR and / or cynomolgus EGFR. In certain aspects, the variable domain that binds or can bind human EGFR binds to domain III of human EGFR. The variable domain that can bind cMET may block the binding of antibody 5D5 to cMET. The variable domain that can bind cMET may block the binding of HGF to cMET. The Kd of the antibody for cMET can be at least 10 times less than the Kd of the antibody for EGFR. The amino acids at positions 405 and 409 in one CH3 domain may be the same as the amino acids at the corresponding positions in the other CH3 domain (EU- numbering). In certain aspects the light chain comprises a light chain region comprising the amino acid sequence of an O12 / IgVκ1-39*01 gene segment as depicted in figure 4A with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The phrase “O12 light chain” will be used throughout the specification as short for “a light chain comprising a light chain variable region comprising the amino acid sequence of an O12 / IgVκ1-39*01 gene segment as part of depicted figure 4A with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. IgVκ1-39 is short for Immunoglobulin Variable Kappa 1-39 Gene. The gene is also known as Immunoglobulin Kappa Variable 1-39; IgGKV139; IgGKV1-39; O12a or O12. External Ids for the gene are HGNC: 5740; Entrez Gene: 28930; Ensembl: ENSG00000242371. A preferred amino acid sequence for IgVκ1-39 is given in figure 4E. This lists the sequence of the V-region. The V-region can be combined with one of five J-regions. Figure 4B and 4D describe two preferred sequences for IgVκ1-39 in combination with a J-region. The joined sequences are indicated as IgGKV1-39 / jk1 and IgGKV1-39 / jk5; alternative names are IgVκ1- 39*01 / IgGJκ1*01 or IgVκ1-39*01 / IgGJκ5*01 (nomenclature according to the IMGT database worldwide web at imgt.org). It is preferred that the O12 / IgVκ1-39*01 comprising light chain variable region is a germline sequence. It is further preferred that the IgGJκ1*01 or / IgGJκ5*01 comprising light chain variable region is a germline sequence. In certain aspects, the IgGKV1-39 / jk1 or IgGKV1-39 / jk5 light chain variable regions are germline sequences. In certain aspects the light chain variable region comprises a germline O12 / IgVκ1-39*01. In certain aspects the light chain variable region comprises the kappa light chain IgVκ1-39*01 / IgGJκ1*01 or IgVκ1-39*01 / IgGJκ5*01. In certain aspects a IgVκ1-39*01 / IgGJκ1*01. The light chain variable region in certain aspects comprises a germline kappa light chain IgVκ1-39*01 / IgGJκ1*01 or germline kappa light chain IgVκ1-39*01 / IgGJκ5*01, in certain aspects a germline IgVκ1-39*01 / IgGJκ1*01. Mature B-cells that produce an antibody with an O12 light chain often produce a light chain that has undergone one or more mutations with respect to the germline sequence, i.e. the normal sequence in non-lymphoid cells of the organism. The process that is responsible for these mutations is often referred to as somatic (hyper)mutation. The resulting light chain is referred to as an affinity matured light chain. Such light chains, when derived from an O12 germline sequence are O12-derived light chains. In this specification, the phrase “common light chain” will include “common light chain derived light chains and the phrase “O12 light chains” will include O12-derived light chains. The mutations that are introduced by somatic hypermutation can also be introduced artificially in the lab. In the lab also other mutations can be introduced without affecting the properties of the light chain in kind, not necessarily in amount. A light chain is at least an O12 light chain if it comprises a sequence as depicted in figure 4A, figure 4B; figure 4D or figure 4E with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects the O12 light chain is a light chain comprising a sequence as depicted in figure 4A; 4b; 4d or 4e with 0-9, 0-8, 0-7, 0-6, 0-5, 0-4 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects the O12 light chain is a light chain comprising a sequence as depicted in figure 4A, figure 4B; figure 4D or figure 4E with 0-5, in certain aspects 0-4, in certain aspects 0-3 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects the O12 light chain is a light chain comprising a sequence as depicted in figure 4A, figure 4B; figure 4D or figure 4E with 0-2, in certain aspects 0-1, in certain aspects 0 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects the O12 light chain is a light chain comprising a sequence as depicted in figure 4A or figure 4B with the mentioned amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects the light chain comprises the sequence of figure 4A. In certain aspects the light chain variable region comprises the sequence of figure 4B. The mentioned 1, 2, 3, 4 or 5 amino acid substitutions are in certain aspects conservative amino acid substitutions and may be present in the CDR regions of the heavy and / or light chain; the insertions, deletions, substitutions or combination thereof are in certain aspects not in the CDR3 region of the VL chain, in certain aspects not in the CDR1, CDR2 or CDR3 region or FR4 region of the VL chain. For instance, conservative amino acid substitutions may be applied. Examples of conservative amino acid substitution include the substitution of one hydrophobic residue such as isoleucine, valine, leucine or methionine for another hydrophobic residue, and the substitution of one polar residue for another polar residue, such as the substitution of arginine for lysine, glutamic acid for aspartic acid, or glutamine for asparagine. In certain aspects, any heavy or light chain CDR1, CDR2 or CDR3 sequence comprises at most 1 or at most 2 conservative amino acid substitutions with respect to the indicated sequence. The common light chain can have a lambda light chain and this is therefore also provided in the context of the disclosure, however a kappa light chain is preferred. The constant part of a common light chain of the disclosure can be a constant region of a kappa or a lambda light chain. It is in certain aspects a constant region of a kappa light chain, in certain aspects said common light chain is a germline light chain, in certain aspects a rearranged germline human kappa light chain comprising the IgVKl-39 gene segment, in certain aspects the rearranged germline human kappa light chain IgVKl- 39*01 / IgGJKl*01 (Figure 4). The terms rearranged germline human kappa light chain IgGVκ1-39*01 / IgGJκ1*01, IgGKV1-39 / IgGKJ1, huVκ1-39 light chain or in short huVκ1- 39, or simply 1-39 are used interchangeably throughout the application. A cell that produces a common light chain can produce for instance rearranged germline human kappa light chain IgVκ1-39*01 / IGJκ1*01 and a light chain comprising the variable region of the mentioned light chain fused to a lambda constant region. In certain aspects the light chain variable region comprises the amino acid sequence DIQMT QSPSS LSASV GDRVT ITCRA SQSIS SYLNW YQQKP GKAPK LLIYA ASSLQ SGVPS RFSGS GSGTD FTLTI SSLQP EDFAT YYCQQ SYSTP PTFGQ GTKVE IK or DIQMT QSPSS LSASV GDRVT ITCRA SQSIS SYLNW YQQKP GKAPK LLIYA ASSLQ SGVPS RFSGS GSGTD FTLTI SSLQP EDFAT YYCQQ SYSTP PITFG QGTRL EIK with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. In certain aspects the light chain variable region comprises 0-9, 0-8, 0-7, 0-6, 0-5, 0-4, in certain aspects 0-3, in certain aspects 0-2, in certain aspects 0-1 and in certain aspects 0 amino acid insertions, deletions, substitutions, additions with respect to the indicated amino acid sequence, or a combination thereof. A combination of an insertion, deletion, addition or substitution is a combination as claimed if aligned sequences do not differ at more than 5 positions. In certain aspects the light chain variable region comprises the amino acid sequence DIQMT QSPSS LSASV GDRVT ITCRA SQSIS SYLNW YQQKP GKAPK LLIYA ASSLQ SGVPS RFSGS GSGTD FTLTI SSLQP EDFAT YYCQQ SYSTP PTFGQ GTKVE IK or DIQMT QSPSS LSASV GDRVT ITCRA SQSIS SYLNW YQQKP GKAPK LLIYA ASSLQ SGVPS RFSGS GSGTD FTLTI SSLQP EDFAT YYCQQ SYSTP PITFG QGTRL EIK. In certain aspects the light chain variable region comprises the amino acid sequence DIQMT QSPSS LSASV GDRVT ITCRA SQSIS SYLNW YQQKP GKAPK LLIYA ASSLQ SGVPS RFSGS GSGTD FTLTI SSLQP EDFAT YYCQQ SYSTP PTFGQ GTKVE IK. In certain aspects, the light chain variable region comprises the amino acid sequence DIQMT QSPSS LSASV GDRVT ITCRA SQSIS SYLNW YQQKP GKAPK LLIYA ASSLQ SGVPS RFSGS GSGTD FTLTI SSLQP EDFAT YYCQQ SYSTP PITFG QGTRL EIK. The amino acid insertions, deletions, substitutions, additions or combination thereof are in certain aspects not in the CDR3 region of the light chain variable region, in certain aspects not in the CDR1 or CDR2 region of the light chain variable region. In certain aspects the light chain variable region does not comprise a deletion, addition or insertion with respect to the sequence indicated. In this aspect the heavy chain variable region can have 0-5 amino acid substitutions with respect to the indicated amino acid sequence. An amino acid substitution is in certain aspects a conservative amino acid substitution. The CDR1, CDR2 and CDR3 of a light chain of an antibody of the disclosure in certain aspects comprises respectively the amino acid sequence CDR1 - QSISSY, CDR2 – AAS, CDR3 – QQSYSTPPT, i.e. the CDRs of IgGVK1-39 / JK1 (according to IMGT). In certain aspects, bispecific antibodies as described herein have one heavy chain variable region / light chain variable region (VH / VL) combination that binds an extracellular part of EGFR and a second VH / VL combination that binds an extracellular of cMET. In certain aspects the VL in said first VH / VL combination is similar to the VL in said second VH / VL combination. In a particular aspect, the VLs in the first and second VH / VL combinations are identical. In certain aspects, the bispecific antibody is a full length antibody which has one heavy / light (H / L) chain combination that binds an extracellular part of EGFR and one H / L chain combination that binds an extracellular part of cMET. In certain aspects the light chain in said first H / L chain combination is similar to the light chain in said second H / L chain combination. In a particular aspect, the light chains in the first and second H / L chain combinations are identical. Several methods have been published to produce a host cell whose expression favors the production of the bispecific antibody or vice versa, the monospecific antibodies. In the present disclosure it is preferred that the cellular expression of the antibody molecules is favored toward the production of the bispecific antibody over the production of the respective monospecific antibodies. Such is typically achieved by modifying the constant region of the heavy chains such that they favor heterodimerization (i.e. dimerization with the heavy chain of the other heavy / light chain combination) over homodimerization. In certain aspects the bispecific antibody of the present disclosure comprises two different immunoglobulin heavy chains with compatible heterodimerization domains. Various compatible heterodimerization domains have been described in the art. The compatible heterodimerization domains are in certain aspects compatible immunoglobulin heavy chain CH3 heterodimerization domains. When wildtype CH3 domains are used, co-expression of two different heavy chains (A and B) and a common light chain will result in three different antibody species, AA, AB and BB. AA and BB are designations for the two mono-specific, bivalent antibodies, and AB is a designation for the bispecific antibody. To increase the percentage of the desired bispecific product (AB) CH3 engineering can be employed, or in other words, one can use heavy chains with compatible hetero-dimerization domains, as defined hereunder. The art describes various ways in which such hetero-dimerization of heavy chains can be achieved. One way is to generate 'knob into hole' bispecific antibodies. The term ‘compatible hetero-dimerization domains’ as used herein refers to protein domains that are engineered such that engineered domain A’ will preferentially form heterodimers with engineered domain B’ and vice versa, homo-dimerization between A’- A’ and B’-B’ is diminished. In granted patents US 9,248,181, US 9,358,286 and PCT / NL2013 / 050294 (published as WO2013 / 157954; incorporated herein by reference) methods and means are disclosed for producing bispecific antibodies using compatible heterodimerization domains. These means and methods can also be favorably employed in the present disclosure. Specifically, a bispecific antibody of the present disclosure in certain aspects comprises mutations to produce substantial expression of bispecific full length IgG molecules in host cells. Preferred mutations are the amino acid substitutions L351K and T366K in the first CH3 domain (the ‘KK-variant’ heavy chain) and the amino acid substitutions L351D and L368E in the second domain (the ‘DE-variant’ heavy chain), or vice versa. US 9,248,181 and US 9,358,286 patents as well as the WO2013 / 157954 PCT application (which are incorporated by reference herein) demonstrate that the DE- variant and KK-variant preferentially pair to form heterodimers (so-called ‘DEKK’ bispecific molecules). Homodimerization of DE-variant heavy chains (DEDE homodimers) are disfavored due to repulsion between the charged residues in the CH3- CH3 interface between identical heavy chains. Bispecific antibodies can be generated by (transient) transfection of plasmids encoding a light chain and two different heavy chains that are CH3 engineered to ensure efficient hetero-dimerization and formation of the bispecific antibodies. The production of these chains in a single cell leads to the favored formation of bispecific antibodies over the formation of monospecific antibodies. Preferred mutations to produce essentially only bispecific full length IgG1 molecules are amino acid substitutions at positions 351 and 366, e.g. L351K and T366K (numbering according to EU numbering) in the first CH3 domain (the 'KK-variant' heavy chain) and amino acid substitutions at positions 351 and 368, e.g. L351D and L368E in the second CH3 domain (the 'DE- variant' heavy chain), or vice versa (see for instance figures 5E and 5F). In one aspect the heavy chain / light chain combination that comprises the variable domain that binds EGFR, comprises a DE variant of the heavy chain. In this aspect the heavy chain / light chain combination that comprises the variable domain that can bind to cMET comprises a KK variant of the heavy chain. The KK variant of the heavy chain that binds cMET do not produce homodimers thereby rendering the observed effect of HGF induced cMET activation inhibition by the bispecific antibody very precise. It avoids activation of cMET sometimes observed with bivalent cMET antibodies (agonism). The Fc region mediates effector functions of an antibody, such as complement- dependent cytotoxicity (CDC), antibody-dependent cellular cytotoxicity (ADCC) and antibody-dependent cell phagocytosis (ADCP). Depending on the therapeutic antibody or Fc fusion protein application, it may be desired to either reduce or increase the effector function. Reduced effector function can be desired when an immune response is to be activated, enhanced or stimulated as in some of the aspects of the present disclosure. Antibodies with reduced effector functions can be used to target cell-surface molecules of immune cells, among others. In certain aspects, the antibody of the present disclosure promotes antibody-dependent cellular phagocytosis (ADCP). In certain aspects, the antibody of the present disclosure promotes antibody-dependent cellular cytotoxicity (ADCC). One advantage of the present disclosure is that in certain aspects, bispecific antibodies of the present disclosure show more potent ADCC activity than amivantamab, especially for cells or a cancer comprising a cMET aberration. Antibodies with reduced effector functions are in certain aspects IgG antibodies comprising a modified CH2 / lower hinge region, for instance to reduce Fc-receptor interaction or to reduce C1q binding. In some aspects the antibody of the disclosure is an IgG antibody with a mutant CH2 and / or lower hinge domain such that interaction of the bispecific IgG antibody to a Fc-gamma receptor is reduced. An antibody comprising a mutant CH2 region is in certain aspects an IgG1 antibody. Such a mutant IgG1 CH2 and / or lower hinge domain in certain aspects comprise an amino substitution at position 235 and / or 236 (EU-numbering), in certain aspects an L235G and / or G236R substitution (Figure 5D). In certain aspects, a bispecific antibody of the disclosure exhibits ADCC activity, in certain aspects the antibody has improved ADCC activity. In such aspect the antibody can have altered ADCC activity by means of one or more CH2 variations relative to a fully human CH2 domain. Further provided is therefore a bispecific antibody according to the disclosure, which is afucosylated. In certain aspects, the antibody of the present disclosure comprises two afucosylated CH2 domains. In certain aspects, the antibody of the present disclosure comprises a total of two CH2 domains, both of which are afucosylated. In certain aspects, the antibody of the present disclosure comprises two CH2 domains, both of which are afucosylated. In certain aspects, a bispecific antibody of the disclosure exhibits ADCP activity, in certain aspects the antibody has improved ADCP activity. In certain aspects, both the EGFR and cMET binding arms, or both heavy chains that comprise the EGFR and cMET binding arms, contribute to ADCP. In certain aspects, the bispecific antibody of the present disclosure has or exhibits ADCP activity towards NSCLC cells. In certain aspects, the bispecific antibody of the present disclosure induces ADCP of NSCLC cells. An antibody of the present disclosure in certain aspects has effector function. A bispecific antibody as disclosed herein in certain aspects comprises antibody-dependent cell-mediated cytotoxicity (ADCC). The antibody can be engineered to enhance the ADCC activity (for review, see Cancer Sci. 2009 Sep;100(9):1566-72. Engineered therapeutic antibodies with improved effector functions. Kubota T, Niwa R, Satoh M, Akinaga S, Shitara K, Hanai N). Several in vitro methods exist for determining the efficacy of antibodies or effector cells in eliciting ADCC. Among these are chromium-51 [Cr51] release assays, europium [Eu] release assays, and sulfur-35 [S35] release assays. Usually, a labeled target cell line expressing a certain surface-exposed antigen is incubated with antibody specific for that antigen. After washing, effector cells expressing Fc receptor CD16 are co-incubated with the antibody-labeled target cells. Target cell lysis is subsequently measured by release of intracellular label by a scintillation counter or spectrophotometry. In one aspect a bispecific antibody of the present disclosure exhibits ADCC activity. In such aspect the bispecific antibody can have improved ADCC activity. In such aspect the antibody can have altered ADCC activity by means of one or more CH2 mutations as described elsewhere herein and by techniques known to in the art. One technique for enhancing ADCC of an antibody is afucosylation. (See for instance Junttila, T. T., K. Parsons, et al. (2010). Further provided is therefore a bispecific antibody according to the disclosure, which is afucosylated. In certain aspects, the antibody of the present disclosure comprises two afucosylated CH2 domains. In certain aspects, the antibody of the present disclosure comprises a total of two CH2 domains, both of which are afucosylated. In certain aspects, the antibody of the present disclosure is a full-length antibody, such as of the IgG-type, having two CH2 domains, both of which are afucosylated. Alternatively, or additionally, multiple other strategies can be used to achieve ADCC enhancement, for instance including glycoengineering (Kyowa Hakko / Biowa, GlycArt (Roche) and Eureka Therapeutics) and mutagenesis, all of which seek to improve Fc binding to low-affinity activating FcγRIIIa, and / or to reduce binding to the low affinity inhibitory FcγRIIb. A bispecific antibody of the present disclosure is in certain aspects afucosylated in order to enhance ADCC activity. A bispecific antibody of the present disclosure herein in certain aspects comprises a reduced amount of fucosylation of the N-linked carbohydrate structure in the Fc region, when compared to the same antibody produced in a normal CHO cell. A variant of an antibody or bispecific antibody as described herein comprises a functional part, derivative and / or analogue of the antibody or bispecific antibody. The variant maintains the binding specificity of the (bispecific) antibody. The functional part, derivative and / or analogue maintains the binding specificity of the (bispecific) antibody. Binding specificity is defined by capacity to bind an extracellular part of a first membrane protein and a second membrane protein as described herein. A bispecific antibody of the present disclosure is in certain aspects used in humans. A preferred antibody of the disclosure is a humanized or in certain aspects human antibody. The constant region of a bispecific antibody of the present disclosure is in certain aspects a human constant region. The constant region may contain one or more, in certain aspects not more than 10, in certain aspects not more than 5 amino-acid differences with the constant region of a naturally occurring human antibody. It is preferred that the constant part is entirely derived from a naturally occurring human antibody. Various antibodies produced herein are derived from a human antibody variable domain library. As such these variable domains are human. The unique CDR regions may be derived from humans, be synthetic or derived from another organism. The variable region is considered a humanized variable region when it has an amino acid sequence that is identical to an amino acid sequence of the variable region of a naturally occurring human antibody, but for the CDR regions. In such aspects, the VH of a variable domain of an antibody that binds EGFR or cMET of the present disclosure may contain one or more, in certain aspects not more than 10, in certain aspects not more than 5 amino-acid differences with the variable region of a naturally occurring human antibody, not counting possible differences in the amino acid sequence of the CDR regions. The light chain variable region of an EGFR binding domain and / or a cMET binding domain in an antibody of the disclosure may contain one or more, in certain aspects not more than 10, in certain aspects not more than 5 amino-acid differences with the variable region of a naturally occurring human antibody, not counting possible differences in the amino acid sequence of the CDR regions. The light chain in an antibody of the present disclosure may contain one or more, in certain aspects not more than 10, in certain aspects not more than 5 amino-acid differences with the variable region of a naturally occurring human antibody, not counting possible differences in the amino acid sequence of the CDR regions. Such mutations also occur in nature in the context of somatic hypermutation. Antibodies may be derived from various animal species, at least with regard to the heavy chain variable region. It is common practice to humanize such e.g. murine heavy chain variable regions. There are various ways in which this can be achieved among which there are CDR-grafting into a human heavy chain variable region with a 3D- structure that matches the 3-D structure of the murine heavy chain variable region; deimmunization of the murine heavy chain variable region, in certain aspects done by removing known or suspected T- or B- cell epitopes from the murine heavy chain variable region. The removal is typically by substituting one or more of the amino acids in the epitope for another (typically conservative) amino acid, such that the sequence of the epitope is modified such that it is no longer a T- or B-cell epitope. Deimmunized murine heavy chain variable regions are less immunogenic in humans than the original murine heavy chain variable region. In certain aspects a variable region or domain of the present disclosure is further humanized, such as for instance veneered. By using veneering techniques, exterior residues which are readily encountered by the immune system are selectively replaced with human residues to provide a hybrid molecule that comprises either a weakly immunogenic or substantially non-immunogenic veneered surface. An animal as used in the present disclosure is in certain aspects a mammal, in certain aspects a primate, in certain aspects a human. A bispecific antibody according to the present disclosure in certain aspects comprises a constant region of a human antibody. According to differences in their heavy chain constant domains, antibodies are grouped into five classes, or isotypes: IgG, IgA, IgM, IgD, and IgE. These classes or isotypes comprise at least one of said heavy chains that is named with a corresponding Greek letter. A certain aspect comprises an antibody wherein said constant region is selected from the group of IgG, IgA, IgM, IgD, and IgE constant regions, in certain aspects said constant region comprises an IgG constant region, i.e. selected from the group consisting of IgG1, IgG2, IgG3 and IgG4. In certain aspects, said constant region is an IgG1 or IgG4 constant region, in certain aspects a mutated IgG1 constant region. Some variation in the constant region of IgG1 occurs in nature and / or is allowed without changing the immunological properties of the resulting antibody. Variation can also be introduced artificially to install certain preferred features on the antibody or parts thereof. Such features are for instance described herein in the context of CH2 and CH3. Typically between about 1-10 amino acid insertions, deletions, substitutions or a combination thereof are allowed in the constant region. A VH chain of Figure 1, 2 or 3 in certain aspects has at most 15, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 amino acid insertions, deletions, substitutions or a combination thereof with respect to the VH chain depicted in Figures 1, 2 or 3, in certain aspects has 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof with respect to the VH chain depicted in Figures 1, 2 or 3, in certain aspects 0, 1, 2, 3 or 4 insertions, deletions, substitutions or a combination thereof, in certain aspects 0, 1, 2 or 3 insertions, deletions, substitutions or a combination thereof, more in certain aspects 0; 1 or 2 insertions, deletions, substitutions or a combination thereof, and in certain aspects 0 or 1 insertion, deletion, substitution or a combination thereof with respect to the VH chain depicted in Figures 1, 2 or 3. The one or two amino acid insertions, deletions, substitutions or a combination thereof are in certain aspects not in the CDR1, CDR2 and / or CDR3 region of the VH chain. They are also in certain aspects not present in the FR4 region. An amino acid substitution is in certain aspects a conservative amino acid substitution. Rational methods have evolved toward minimizing the content of non-human residues in the human context. Various methods are available to successfully graft the antigen-binding property of an antibody onto another antibody. The binding properties of antibodies may rest predominantly in the exact sequence of the CDR3 region, often supported by the sequence of the CDR1 and CDR2 regions in the variable domain combined with the appropriate structure of the variable domain as a whole. CDR sequences can be defined using different methods, including, but not limited to, according to the Kabat numbering scheme (Kabat et al., J. Biol. Chem.252:6609-6616 (1977); and / or Kabat et al., U.S. Dept. of Health and Human Services, “Sequences of proteins of immunological interest” (1991)), the Chothia numbering scheme (Chothia et al., J. Mol. Biol.196:901-917 (1987); Chothia et al., Nature 342: 877-883, 1989; and / or Al- Lazikani B. et al., J. Mol. Biol., 273: 927-948 (1997)), the numbering system of Honegger and Plukthun (Honegger and Plückthun, J. Mol. Biol., 309:657-670 (2001)), the numbering system of MacCallum (MacCallum et al., J. Mol. Biol.262:732-745 (1996); and / or Abhinandan and Martin, Mol. Immunol., 45: 3832-3839 (2008)), the numbering system of Lefranc (Lefranc M.P. et al., Dev. Comp. Immunol., 27: 55-77 (2003); and / or Honegger and Plückthun, J. Mol. Biol., 309:657-670 (2001)), or according to IMGT (discussed in Giudicelli et al., Nucleic Acids Res. 25: 206-211 (1997)). Each of these numbering schemes base their definition of CDRs on a predicted contribution of amino acid residues in the heavy or light chain variable region to antigen binding. Hence, each method to identify CDRs can be used to identify the CDRs of the binding domains of the present disclosure. In certain aspects, the heavy chain CDRs of a binding domain of the present disclosure is according to Kabat, Chothia, or IMGT. In certain aspects, the heavy chain CDRs of a binding domain of the present disclosure is according to Kabat. In certain aspects, the heavy chain CDRs of a binding domain of the present disclosure is according to Chothia. In certain aspects, the heavy chain CDRs of a binding domain of the present disclosure is according to IMGT. In certain aspects, the light chain CDRs of a binding domain of the present disclosure is according to Kabat. In certain aspects, the light chain CDRs of a binding domain of the present disclosure is according to Chothia. In certain aspects, the light chain CDRs of a binding domain of the present disclosure is according to IMGT. The amino acid sequence of a heavy chain CDR region as depicted herein is determined with the Kabat definition. Various methods are presently available to graft CDR regions onto a suitable variable domain of another antibody. Some of these methods are reviewed in J.C. Almagro1 and J. Fransson (2008) Frontiers in Bioscience 13, 1619-1633, which is included by reference herein. The disclosure therefore further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first antigen-binding site that binds EGFR and a second antigen-binding site that binds cMET, wherein the variable domain comprising the EGFR binding site comprises a VH CDR3 sequence as depicted for MF3370 in Figure 1, and wherein the variable domain comprising the cMET binding site comprises a VH CDR3 region as depicted for MF4356 in Figure 1. The VH variable region comprising the EGFR binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF3370 in Figure 1. The VH variable region comprising the cMET binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF4356 in Figure 1. CDR grafting may also be used to produce a VH chain with the CDR regions of a VH of Figure 1, but having a different framework. The different framework may be of another human VH, or of a different mammal. The disclosure therefore further provides a humanized or in certain aspects human bispecific antibody comprising a first antigen-binding site that binds EGFR and a second antigen- binding site that binds cMET, wherein the variable domain comprising the EGFR binding site comprises a VH CDR3 sequence as depicted for MF8233 in Figure 2, and wherein the variable domain comprising the cMET binding site comprises a VH CDR3 region as depicted for MF8230 in Figure 3. The VH variable region comprising the EGFR binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8233 in Figure 2. The VH variable region comprising the cMET binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8230 in Figure 3. CDR grafting may also be used to produce a VH chain with the CDR regions of a VH of Figure 2 or Figure 3, but having a different framework. The different framework may be of another human VH, or of a different mammal. The disclosure therefore further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first antigen-binding site that binds EGFR and a second antigen-binding site that binds cMET, wherein the variable domain comprising the EGFR binding site comprises a VH CDR3 sequence as depicted for MF3370 in Figure 1, and wherein the variable domain comprising the cMET binding site comprises a VH CDR3 region as depicted for MF8230 in Figure 3. The VH variable region comprising the EGFR binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF3370 in Figure 1. The VH variable region comprising the cMET binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8230 in Figure 3. CDR grafting may also be used to produce a VH chain with the CDR regions of a VH of Figure 2 or Figure 3, but having a different framework. The different framework may be of another human VH, or of a different mammal. The disclosure therefore further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first antigen-binding site that binds EGFR and a second antigen-binding site that binds cMET, wherein the variable domain comprising the EGFR binding site comprises a VH CDR3 sequence as depicted for MF8233 in Figure 2, and wherein the variable domain comprising the cMET binding site comprises a VH CDR3 region as depicted for MF4356 in Figure 3. The VH variable region comprising the EGFR binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8233 in Figure 2. The VH variable region comprising the cMET binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF4356 in Figure 3. CDR grafting may also be used to produce a VH chain with the CDR regions of a VH of Figure 2 or Figure 3, but having a different framework. The different framework may be of another human VH, or of a different mammal. The disclosure therefore further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first antigen-binding site that binds EGFR and a second antigen-binding site that binds cMET, wherein the variable domain comprising the EGFR binding site comprises a VH CDR3 sequence as depicted for MF8232 in Figure 2, and wherein the variable domain comprising the cMET binding site comprises a VH CDR3 region as depicted for MF8230 in Figure 3. The VH variable region comprising the EGFR binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8232 in Figure 2. The VH variable region comprising the cMET binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8230 in Figure 3. CDR grafting may also be used to produce a VH chain with the CDR regions of a VH of Figure 2 or Figure 3, but having a different framework. The different framework may be of another human VH, or of a different mammal. The disclosure therefore further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first antigen-binding site that binds EGFR and a second antigen-binding site that binds cMET, wherein the variable domain comprising the EGFR binding site comprises a VH CDR3 sequence as depicted for MF8232 in Figure 2, and wherein the variable domain comprising the cMET binding site comprises a VH CDR3 region as depicted for MF4356 in Figure 3. The VH variable region comprising the EGFR binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF8232 in Figure 2. The VH variable region comprising the cMET binding site in certain aspects comprises the sequence of the CDR1 region, CDR2 region and the CDR3 region of a VH chain as depicted for MF4356 in Figure 3. CDR grafting may also be used to produce a VH chain with the CDR regions of a VH of Figure 2 or Figure 3, but having a different framework. The different framework may be of another human VH, or of a different mammal. Methods for generating sequence variants are well known in the art. One can take a random approach in generating sequence variants or a targeted approach, where one can for instance aim at introducing variations that are likely to increase or decrease binding affinity. Routine methods for affinity maturing antibody binding domains are widely known in the art, see for instance Tabasinezhad M. et al., 2019. One can also aim at introducing variations that mitigate developability risks with a view on producing a binding domain, or moiety comprising such binding domain, at large scale. Variations may be introduced that are likely not to cause a loss in binding specificity and / or affect binding affinity. Whether amino acid residues within the CDRs and / or framework regions can be substituted, for instance with a conservative amino acid residue, and without, or substantially without, loss in binding specificity and / or affinity, can be determined by methods well known in the art. Experimental examples include, but are not limited to, for instance, alanine scanning (Cunningham BC, 1989), and deep mutational scanning (Araya CL.2011). Computational methods have also been developed that can predict the effect of amino acid variation, such as for instance described in Sruthi CK (2020), Choi Y. et al. (2012) and Munro D (2020). Further provided herein are any variant anti-human EGFR and c-MET binding domains produced by the above described method; binding moieties, such as antibodies, comprising any of said variant binding domains; a pharmaceutical composition comprising any of said variant anti-human EGFR and c-MET binding domains or binding moieties; nucleic acids encoding any of said variant binding domains; vectors and cells comprising said nucleic acids; and use of said variant binding domains or pharmaceutical composition for the treatment of cancer. The disclosure further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first variable domain that binds EGFR and a second variable domain that binds cMET wherein the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF3370 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof and wherein the second variable domain comprises a heavy chain variable region that comprises the amino acid sequence of MF4356 depicted in figure 3 (SEQ ID NO: 23) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The disclosure further provides a humanized or in certain aspects human bispecific antibody comprising a first variable domain that binds EGFR and a second variable domain that binds cMET wherein the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF8233 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof and wherein the second variable domain comprises a heavy chain variable region that comprises the amino acid sequence of MF8230 depicted in figure 3 (SEQ ID NO: 13) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The disclosure further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first variable domain that binds EGFR and a second variable domain that binds cMET wherein the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF3370 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof and wherein the second variable domain comprises a heavy chain variable region that comprises the amino acid sequence of MF8230 depicted in figure 3 (SEQ ID NO: 13) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The disclosure further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first variable domain that binds EGFR and a second variable domain that binds cMET wherein the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF8233 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof and wherein the second variable domain comprises a heavy chain variable region that comprises the amino acid sequence of MF4356 depicted in figure 3 (SEQ ID NO: 23) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The disclosure further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first variable domain that binds EGFR and a second variable domain that binds cMET wherein the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF8232 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof and wherein the second variable domain comprises a heavy chain variable region that comprises the amino acid sequence of MF4356 depicted in figure 3 (SEQ ID NO: 23) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The disclosure further provides a humanized or in certain aspects human bispecific antibody as included in the treatment of the present disclosure comprising a first variable domain that binds EGFR and a second variable domain that binds cMET wherein the first variable domain comprises a heavy chain variable region with the amino acid sequence of MF8232 as depicted in figure 2 having at most 10, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects having 0, 1, 2, 3, 4 or 5 amino acid insertions, deletions, substitutions or a combination thereof and wherein the second variable domain comprises a heavy chain variable region that comprises the amino acid sequence of MF8230 depicted in figure 3 (SEQ ID NO: 13) with 0-10, in certain aspects 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. The mentioned at most 15, in certain aspects 0, 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10 and in certain aspects 0, 1, 2, 3, 4 or 5 amino acid substitutions are in certain aspects conservative amino acid substitutions, the insertions, deletions, substitutions or a combination thereof are in certain aspects not in the CDR3 region of the VH chain, in certain aspects not in the CDR1, CDR2 or CDR3 region of the VH chain and in certain aspects not in the FR4 region. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF3370 and a second variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF4356. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8233 and a second variable domain which comprisesthe CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8230. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8232 and a second variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF4356. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8233 and a second variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF4356. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF3370 and a second variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8230. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8232 and a second variable domain which comprises the CDR1, CDR2 and CDR3 sequences of the heavy chain variable region of MF8230. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYSGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYSGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF3370 and a second variable domain which comprises the heavy chain variable region of MF4356. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF8233 and a second variable domain which comprises the CDR1, CDR2 and CDR3 sequences of theheavy chain variable region of MF8230.In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF8233 and a second variable domain which comprises the heavy chain variable region of MF8230. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF8232 and a second variable domain which comprises the heavy chain variable region of MF4356. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF8233 and a second variable domain which comprises the heavy chain variable region of MF4356. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF3370 and a second variable domain which comprises the heavy chain variable region of MF8230. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises the heavy chain variable region of MF8232 and a second variable domain which comprises the heavy chain variable region of MF8230. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP, and the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT, which bispecific antibody is dosed at a flat dose of 1500 mg once every two weeks and wherein said chemotherapeutic agent is paclitaxel and carboplatin, wherein paclitaxel is dosed at 175 mg / m2, once every three weeks and carboplatin is dosed at AUC5, once every three weeks to subjects that are resistant to previous treatment with osimertinib. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP, and the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT, which bispecific antibody is dosed at a flat dose of 2000 mg once every two weeks and wherein said chemotherapeutic agent is paclitaxel and carboplatin, wherein paclitaxel is dosed at 175 mg / m2, once every three weeks and carboplatin is dosed at AUC5, once every three weeks to subjects that are resistant to previous treatment with osimertinib. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin, which bispecific antibody is dosed at a flat dose of 1500 mg once every two weeks and wherein said chemotherapeutic agent is paclitaxel and carboplatin, wherein paclitaxel is dosed at 175 mg / m2, once every three weeks and carboplatin is dosed at AUC5, once every three weeks to subjects that are resistant to previous treatment with osimertinib. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin, which bispecific antibody is dosed at a flat dose of 2000 mg once every two weeks and wherein said chemotherapeutic agent is paclitaxel and carboplatin, wherein paclitaxel is dosed at 175 mg / m2, once every three weeks and carboplatin is dosed at AUC5, once every three weeks to subjects that are resistant to previous treatment with osimertinib. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP, and the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT, which bispecific antibody is dosed at a flat dose of 1500 mg once every two weeks and wherein said chemotherapeutic agent is or comprises docetaxel which is dosed at 75 mg / m2once every three weeks to subjects that are resistant to previous treatment with osimertinib and resistant to platinum-based chemotherapy. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP, and the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT, which bispecific antibody is dosed at a flat dose of 2000 mg once every two weeks and wherein said chemotherapeutic agent is or comprises docetaxel which is dosed at 75 mg / m2once every three weeks to subjects that are resistant to previous treatment with osimertinib and resistant to platinum-based chemotherapy. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin, which bispecific antibody is dosed at a flat dose of 1500 mg once every two weeks and wherein said chemotherapeutic agent is or comprises docetaxel which is dosed at 75 mg / m2once every three weeks to subjects that are resistant to previous treatment with osimertinib and resistant to platinum-based chemotherapy. In certain aspects, said bispecific antibody of the present disclosure comprises a first variable domain which comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, a second variable domain which comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin, which bispecific antibody is dosed at a flat dose of 2000 mg once every two weeks and wherein said chemotherapeutic agent is or comprises docetaxel which is dosed at 75 mg / m2once every three weeks to subjects that are resistant to previous treatment with osimertinib and resistant to platinum-based chemotherapy The disclosure further provides a pharmaceutical composition comprising a combination of an antibody according to the present disclosure and said chemotherapeutic agent. The pharmaceutical composition in certain aspects comprises a in certain aspects pharmaceutically acceptable excipient or carrier. An antibody can comprise a label, in certain aspects a label for in vivo imaging. Such a label is typically not necessary for therapeutic applications. In for instance a diagnostic setting, a label can be helpful. For instance in visualizing target cells in the body. Various labels are suited and many are well known in the art. In certain aspects the label is a radioactive label for detection. In another certain aspect, the label is an infrared label. In certain aspects the infrared label is suited for in vivo imaging. Various infrared labels are available to the person skilled in the art. Preferred infrared labels are for instance, IRDye 800; IRDye 680RD; IRDye 680LT; IRDye 750; IRDye 700DX; IRDye 800RS IRDye 650; IRDye 700 phosphoramidite; IRDye 800 phosphoramidite (LI- COR USA; 4647 Superior Street; Lincoln, Nebraska). The disclosure further provides a method for the treatment of a subject that has a tumor or is at risk of having said tumor comprising administering to the subject in need thereof an antibody and a chemotherapeutic agent or a pharmaceutical composition of the present disclosure. The tumor is in certain aspects an EGFR, cMET or EGFR / cMET positive tumor. Before start of said treatment, the method in certain aspects further comprises determining whether said subject has such an EGFR, cMET or EGFR / cMET positive tumor. The disclosure further provides an antibody or pharmaceutical composition of the disclosure for use in the treatment of a subject that has or is at risk of having an EGFR, cMET or EGFR / cMET positive tumor. In certain aspects, the bispecific antibody of the present disclosure comprises or is pamvatamig (cf. WHO Drug Information, Vol. 37, No. 2, 2023 Proposed INN: List 129). Dosage regimen and administration of therapeutic agents of the present disclosure In certain aspects, said treatment comprises administering to said subject an effective amount of said bispecific antibody and an effective amount of said chemotherapeutic agent. The amount of therapeutic agent to be administered to a patient is typically in the therapeutic window, meaning that a sufficient quantity is used for obtaining a therapeutic effect, while the amount does not exceed a threshold value leading to an unacceptable extent of side-effects. The lower the amount of antibody needed for obtaining a desired therapeutic effect, the larger the therapeutic window will typically be. An antibody according to the present disclosure exerting sufficient therapeutic effects at low dosage is, therefore, preferred. The dosage can be in range of the dosing regimen of cetuximab. In certain aspects, the dose is 600 mg, 1000 mg, 1500 mg, or 2000 mg. Dosing may be once every week or once every two weeks. In certain aspects, the bispecific antibody binding EGFR and cMET is provided to a subject at a dosage of 600, 1000, 1500 or 2000 mg, in particular using a flat dose regimen. A flat dose regimen offers several advantages over body-surface or weight dosing as it reduces preparation time and reduces potential dose calculation mistakes. In certain aspects, the bispecific antibody is administered once every week (Q1W), once every 2 weeks (Q2W) or once every 3 weeks (Q3W). In certain aspects, the bispecific antibody is administered once every two weeks. In the art, such a dosing scheme is noted as Q2W. In certain aspects, the flat dose regimen disclosed herein is suitable for use in adults and / or in subjects weighing at least 35kg. As is understood by the skilled person, the dosage can be administered over time. As is understood by the skilled person, the term “flat dose” or “flat dose regimen” means that the subject undergoes a dosing regimen wherein on each day the subject is scheduled to receive the bispecific antibody or chemotherapeutic agent with substantially the same predetermined amount thereof which amount is irrespective of the subjects’ body weight. Also, the subject is also provided a dose of a chemotherapeutic agent. Thus, in certain aspects, said bispecific antibody of the present disclosure is dosed or administered at 600 mg, in particular using a flat dose of 600 mg. In certain aspects, said bispecific antibody is administered in an amount of 600 mg once every week. In certain aspects, said bispecific antibody is administered in an amount of 600 mg once every two weeks. In certain aspects, said bispecific antibody is administered in a flat dose of 600 mg once every two weeks. In certain aspects, the bispecific antibody comprises or is pamvatamig. Thus, in certain aspects, said bispecific antibody of the present disclosure is dosed or administered at 1000 mg, in particular using a flat dose of 1000 mg. In certain aspects, said bispecific antibody is administered in an amount of 1000 mg once every week. In certain aspects, said bispecific antibody is administered in an amount of 1000 mg once every two weeks. In certain aspects, said bispecific antibody is administered in a flat dose of 1000 mg once every two weeks. In certain aspects, the bispecific antibody comprises or is pamvatamig. Thus, in certain aspects, said bispecific antibody of the present disclosure is dosed or administered at 1500 mg, in particular using a flat dose of 1500 mg. In certain aspects, said bispecific antibody is administered an amount of 1500 mg once every two weeks. In certain aspects, said bispecific antibody is administered in a flat dose of 1500 mg once every two weeks. In certain aspects, the bispecific antibody comprises or is pamvatamig. Thus, in certain aspects, said bispecific antibody of the present disclosure is dosed or administered at 2000 mg, in particular using a flat dose of 2000 mg. In certain aspects, said bispecific antibody is administered in an amount of 2000 mg once every two weeks. In certain aspects, said bispecific antibody is administered in a flat dose of 2000 mg once every two weeks. In certain aspects, the bispecific antibody comprises or is pamvatamig. In certain aspects, paclitaxel is administered in an amount of between 50 and 200 mg / m2 body surface q3w and carboplatin is administered at AUC 3, AUC 4 or AUC 5 q3w. In certain aspects, paclitaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. In certain aspects, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks. In certain aspects, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks. In certain aspects, paclitaxel is administered in an amount of 175 mg / m2 body surface once every three weeks. In certain aspects, paclitaxel is administered in an amount of 200 mg / m2 body surface once every three weeks. In certain aspects, carboplatin is administered at AUC 3 once every three weeks once every three weeks. In certain aspects, carboplatin is administered at AUC 4 once every three weeks once every three weeks. In certain aspects, carboplatin is administered at AUC 5 once every three weeks once every three weeks. In certain aspects, docetaxel is administered in an amount of between 20 and 100 mg / m2 body surface once every three weeks. In certain aspects, docetaxel is administered in an amount of 40 mg / m2 body surface once every three weeks. In certain aspects, docetaxel is administered in an amount of 55 mg / m2 body surface once every three weeks. In certain aspects, docetaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. In certain aspects, docetaxel is administered in an amount of 100 mg / m2 body surface once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 2000 mg once every weeks, paclitaxel is administered in an amount of 175 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 5 once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 1500 mg once every weeks, paclitaxel is administered in an amount of 175 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 5 once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 1500 mg once every weeks, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 4 once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 1000 mg once every weeks, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 4 once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 1000 mg once every weeks, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 3 once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 600 mg once every weeks, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 3 once every three weeks. In certain aspects, said bispecific antibody is administered in an amount of 2000 mg once every two weeks and docetaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. In certain aspects, said In certain aspects, said bispecific antibody is administered in an amount of 1500 mg once every two weeks and docetaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. In certain aspects, said In certain aspects, said bispecific antibody is administered in an amount of 1500 mg once every two weeks and docetaxel is administered in an amount of 55 mg / m2 body surface once every three weeks. In certain aspects, said In certain aspects, said bispecific antibody is administered in an amount of 1000 mg once every two weeks and docetaxel is administered in an amount of 55 mg / m2 body surface once every three weeks. In certain aspects, said In certain aspects, said bispecific antibody is administered in an amount of 1000 mg once every two weeks and docetaxel is administered in an amount of 40 mg / m2 body surface once every three weeks. In certain aspects, said In certain aspects, said bispecific antibody is administered in an amount of 600 mg once every two weeks and docetaxel is administered in an amount of 40 mg / m2 body surface once every three weeks. In certain aspects, said subject does not have impaired or reduced creatine clearance capacity levels. In certain aspects, said subject has a creatine clearance capacity level of at least 60 mg / ml. In certain aspects, said subject has a creatine clearance capacity level of from at least 60 mg / ml to non-impaired clearance levels. In certain aspects, wherein said subject has a creatine clearance capacity level of between 41 and 59 mg / ml, carboplatin is administered at 250 mg / m2 body surface once every three weeks. In certain aspects, wherein said subject has a creatine clearance capacity level of between 16 and 40 mg / ml, carboplatin is administered at 200 mg / m2 body surface once every three weeks. In certain aspects, said subject does not suffer from febrile neutropenia, has an absolute neutrophil count of more than 500 cells per mm3and / or does not exhibit a non- hematological Grade 3 or 4 adverse event. In certain aspects, wherein said subject suffers from febrile neutropenia, has an absolute neutrophil count of less than 500 cells per mm3and / or exhibits a non- hematological Grade 3 or 4 adverse event, docetaxel is administered in an amount of 55 mg / m2 body surface once every three weeks. In certain aspects, said subject has a platelets count per milliliter of ≥ 50 and has an absolute neutrophil cell count per microliter of ≥ 0.5. In certain aspects, wherein said subject has a platelets count per milliliter of ≥50 and has an absolute neutrophil cell count per microliter of <0.5, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject has a platelets count per milliliter of <50 without bleeding, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject has a platelets count per milliliter of <50 with Grade 2 or higher bleeding, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 3 once every three weeks. In certain aspects, wherein said subject has an absolute neutrophil cell count per microliter of <1.0 and a fever of at least 38.5ºC or higher (or 101ºF or higher), paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, said subject does not experience the following adverse events (AEs); nausea or vomiting Grade 3 or 4, diarrhea Grade 3 or 4, mucositis Grade 3 or 4, neurotoxicity Grade 2, 3 or 4, transaminase elevation Grade 3 or 4, or another non- hematological toxicity Grade 3 or 4. In certain aspects, wherein said subject experiences nausea or vomiting Grade 3 or 4, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject experiences diarrhea Grade 3 or 4, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject experiences mucositis Grade 3 or 4, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject experiences neurotoxicity Grade 2, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 5 once every three weeks. In certain aspects, wherein said subject experiences neurotoxicity Grade 3 or 4, carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject has transaminase elevation Grade 3, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. In certain aspects, wherein said subject experiences a hematological toxicity Grade 3 or 4, not being transaminase elevation, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 4 once every three weeks. A bispecific antibody according to the disclosure in certain aspects induces less skin toxicity as compared to cetuximab under otherwise similar conditions. A bispecific antibody according to the disclosure in certain aspects produces less proinflammatory chemokines, in certain aspects of CXCL14 as compared to cetuximab under otherwise similar conditions. A bispecific antibody according to the disclosure in certain aspects induces less impairment of antimicrobial RNAses, in certain aspects Rnase 7, as compared to cetuximab under otherwise similar conditions. The present disclosure describes among others antibodies that target the EGFR and cMET receptors and result in potent proliferation inhibition of cancer cell lines in vitro and tumor growth inhibition in vivo. A bispecific antibody of the disclosure can combine low toxicity profiles with high efficacy. An antibody of the disclosure can be useful in various types and lines of EGFR-targeted therapies. An antibody of the disclosure can have an increased therapeutic window when compared to an antibody that binds the same antigen(s) with both arms. A bispecific antibody of the disclosure can exhibit better growth inhibitory effects in vitro, in vivo or a combination thereof when compared to the cetuximab antibody. In certain aspects, prior to every paclitaxel / carboplatin administration, said subject has a neutrophil cell count of at least 1500 cells / mm3and platelet count of at least 100,000 cells / mm3; absence of Grade 3 or 4 toxicities; absence of Interstitial Lung Disease (ILD), including pneumonitis; In certain aspects, prior to every docetaxel administration, said subject has a neutrophil cell count of at least 1500 cells / mm3and platelet count of at least 100,000 cells / mm3; absence of Grade 3 or 4 toxicities; a bilirubin level not higher than ULN; AST and / or ALT not higher than 1.5 x ULN concomitant with alkaline phosphatase higher than 2.5 x ULN; absence of corneal ulceration; and absence of ILD, including pneumonitis. Quantitative or qualitative determination of EGFR and / or cMET To establish whether a tumor is positive for EGFR the skilled person can for instance determine the EGFR amplification and / or immuno-histochemistry staining. At least 10% of the tumor cells in a biopsy should be positive. The biopsy can also contain 20%, 30% 40% 50% 60% 70% or more positive cells. To establish whether a tumor is positive for cMET the skilled person can for instance determine the cMET amplification and / or staining in immunohistochemistry. At least 10% of the tumor cells in a biopsy should be positive. The biopsy can also contain 20%, 30% 40% 50% 60% 70% or more positive cells. As used herein, a cancer expresses EGFR if the cancer comprises cells that express EGFR. A cell which expresses EGFR comprises detectable levels of RNA that codes for EGFR. In certain aspects, EGFR expression is determined by ISH. In certain aspects, EGFR amplification is defined as an EGFR number of 8 or more, in particular defined as 8 copies or more above ploidy based on solid tissue amplification. In certain aspects, subjects having a cancer are characterized by an EGFR ctDNA score of at least 2.14, at least 2.5, or at least 4 or higher (e.g. up to 20 or more). In certain aspects, EGFR copy number is established by next-generation sequencing on a formalin-fixed paraffin embedded (FFPE) tissue sample. In certain aspects, EGFR copy number is established using next-generation sequencing (NGS). In certain aspects, said NGS is performed on a solid tissue sample or a liquid sample, such as blood or plasma. In certain aspects, said copy number assessment may be based on blood-derived cfDNA. As an example, determining of EGFR copy number can be performed as mentioned by Kato et al. (2019). Herein, the term “ctDNA” (circulating tumor DNA) is used interchangeably with “cfDNA” (cell-free tumor DNA). In certain aspects, EGFR copy number is established using FISH. In certain aspects, said cancer is characterized by an EGFR / CEP7 ratio of at least 2.0 or higher. Establishing the EGFR / CEP7 ratio is standard in the art but may for instance be established using a commercially available kit, or be performed as described by Maron, et al., (2018). The EGFR FISH test is designed to detect amplification of the EGFR locus (positioned at chromosome 7p11.2). In such a methodology, FISH is performed on sections of formalin-fixed, paraffin-embedded tumor tissue. Slides are prepared per standard protocols and 100 interphase cells are scored. Another example is the EGFR FISH molecular test (7p11) / SE 7 (D7Z1) - XL for BOND (catalog number: KBI-XL011). In each such test, cutoff for amplification is set at ≥2.0 ratio of EGFR:CEP7. In certain aspects, EGFR protein expression is detected by IHC. In certain aspects, EGFR expression is determined by IHC using a commercially available EGFR detection kit, such as the EGFR pharmDx™ kit for a Dako autostainer (Agilent), using the manufacturer’s recommendations or the commercially available IHC EGFR detection kit based on EGFR clone 113 which binds the EGFR extracellular domain (Leica, https: / / shop.leicabiosystems.com / us / ihc-ish / ihc-primary-antibodies / pid-epidermal- growth-factor-receptor). Alternatively, EGFR expression is determined using the NovocastraTM Liquid Mouse Monoclonal Antibody Epidermal Growth Factor Receptor which is based on clone EGFR.113 (Product Code: NCL-L-EGFR, Epidermal Growth Factor Receptor - IHC Primary Antibodies by leicabiosystems.com). In certain aspects, subjects having cancer characterized by an EGFR gene amplification which comprises an EGFR / CEP7 ratio of at least 2.0 or higher or an EGFR number of 8 or more are selected for treatment. In certain aspects, the treatment of a subject is preceded by a step of diagnosing said subject of having cancer characterized by an EGFR gene amplification which comprises an EGFR / CEP7 ratio of at least 2.0 or higher or an EGFR number of 8 or more. In certain aspects, cMET overexpression is detected by IHC. In certain aspects, cMET expression is determined by IHC using a commercially available cMET detection kit, such as the Ventana Medical Systems' (Ventana) CONFIRM anti-Total c-MET (SP44) Rabbit Monoclonal Primary Antibody or the Rabbit Recombinant Monoclonal Met (c-Met) antibody - C-terminal (Product Code AB227637, Abcam) which is suitable for IHC-P, Flow Cyt (Intra) and reacts with human samples (Abcam), using the manufacturer’s recommendations. Said antibody is directed against a membranous and / or cytoplasmic epitope present in human normal epithelial or tumor cells. This antibody may be used to aid in the identification of normal and neoplastic c-MET expressing cells. The antibody is intended for qualitative staining in sections of formalin fixed, paraffin embedded tissue and can for instance be visualized using ultraView Universal DAB Detection Kit (Ventana) and the BenchMark ULTRA (Roche), the BenchMark XT / LT (Roche) IHC instrument or the like. In certain aspects, cMET overexpression is characterized by a IHC score of 2+ or 3+. In certain aspects, the treatment of a subject is preceded by a step of diagnosing said subject of having cancer characterized by a cMET IHC score of 2+ or 3+, followed by treatment with the therapeutic agents of the present disclosure. The cancer or tumor may be an EGFR, cMET or EGFR / cMET positive cancer. In one aspect, the disclosure provides treatment of a positive cancer that is an EGFR, cMET or EGFR / cMET positive cancer that is lung cancer, in certain aspects non-small cell lung cancer. The subject is in certain aspects a human subject. The subject is in certain aspects a subject eligible for antibody therapy using an EGFR specific antibody such as cetuximab. In certain aspects the disclosure may in certain aspects treat a subject that comprises a tumor, in certain aspects an EGFR / cMET positive cancer, in certain aspects a tumor / cancer with an EGFR TKI resistant phenotype, an EGFR monoclonal antibody resistant phenotype or a combination thereof. The tumor may be an EGFR positive tumor, a cMET positive tumor or an EGFR and cMET positive tumor. The tumor may be a lung cancer including non-small cell lung cancer. The tumor may be resistant to treatment with an EGFR tyrosine kinase inhibitor. In certain aspects, the EGFR tyrosine kinase inhibitor is a third generation EGFR tyrosine kinase inhibitor, in certain aspects osimertinib or an analogue thereof. Examples of clinically relevant third generation EGFR tyrosine kinase inhibitors are osimertinib, lazertinib, alflutinib, rezivertinib, olmutinib, almonertinib, abivertinib, ASK120067, befotertinib, rociletinib, oritinib (SH-1028), nazartinib (EGF816), naquotinib (ASP8273), furmonertinib, mavelertinib (PF-0647775), olafertinib (CK-101), keynatinib or ES-072. In certain aspects the third generation EGFR tyrosine kinase inhibitor is osimertinib. In certain aspects the tyrosine kinase inhibitor is lazertinib. In certain aspects the tyrosine kinase inhibitor is almonertinib. In certain aspects the tyrosine kinase inhibitor is befotertinib. In certain aspects, at the start of treatment, at least one, more than one or all of the following inclusion factors IF1-IF7 are applicable to subjects for treatment. In certain aspects, the subject comprises or complies with all of inclusion factors IF1-IF7: IF1. Having an age of equal to or higher than 18 years at signature of informed consent. IF2. Having a histologically or cytologically confirmed solid tumor with evidence of metastatic or locally advanced unresected disease that is incurable. Subjects have progressed on or are intolerant to osimertinib treatment. IF2.1. For subjects who have progressed on or are intolerant to prior first-line osimertinib treatment but are chemotherapy naïve: Subjects have progressed on or are intolerant to therapies that are known to provide clinical benefit. Subjects have either NSCLC harboring activating EGFR mutations including tyrosine kinase inhibitor (TKI) sensitizing mutations, and / or approved TKI-resistance mutations, or any activating c- MET mutation / amplification. IF2.2. For subjects who have failed prior first-line osimertinib treatment and are second-line platinum resistant (i.e. subject has progressed on or after a previous platinum chemotherapy). IF3. Having availability of FFPE embedded after progression at the latest therapy, archival or a fresh tumor tissue sample. IF4. Having measurable disease as defined by RECIST version 1.1 by radiologic methods (patients with non-measurable but evaluable disease can be included in the dose escalation part). IF5. Having an Eastern Cooperative Oncology Group (ECOG) performance status of 0 or 1. IF6. Having a life expectancy ≥ 12 weeks. IF7. Having adequate organ function, as established by at least one or all of: IF7.1 Absolute neutrophil count (ANC) ≥1.5 X 109 / L. IF7.2 Hemoglobin ≥9 g / dL. IF7.3 Platelets ≥100 x 109 / L. IF7.4 Corrected total serum calcium within normal ranges. IF7.5 Serum magnesium within normal ranges (or corrected with supplements). IF7.6 Serum potassium within normal ranges. IF7.7 Alanine aminotransferase (ALT) and aspartate aminotransferase (AST) equal to or less than 2.5 x the upper limit of normal (ULN) and total bilirubin equal to or less than 1.5 x ULN, with the proviso that in cases of a liver involvement or malignancy, ALT / AST is equal to or less than 5 x ULN and total bilirubin is equal to or less than 2 x ULN. IF7.8 For patients with Gilbert’s syndrome, conjugated bilirubin has a value within normal limits. IF7.9 Serum creatinine equal to or less than 1.5 x ULN or creatinine clearance equal to or higher than 50 mL / min calculated according to the Cockcroft and Gault formula or the MDRD formula for patients aged over 65 years. IF7.10 For subjects receiving paclitaxel / carboplatin, creatinine clearance is in certain aspects ≥60 mL / min. IF7.11 Serum albumin >3.3 g / dL IF7.12 International Normalized Ratio (INR) or Prothrombin Time (PT) ≤1.5 x ULN, with the proviso the subject is not receiving anticoagulant therapy IF7.13 Activated Partial Thromboplastin Time (aPTT) or Partial Thromboplastin Time (PTT) ≤1.5 x ULN, with the proviso the subject is not receiving anticoagulant therapy. In certain aspects, all values for organ function measurements according to IF7 have an upper limit observed with healthy subjects. In certain aspects, the subject for treatment comprises one or more factors selected from the group consisting of IF1-IF13. In certain aspects, the subject for treatment comprises factors IF2, IF4, IF5 and IF7. In certain aspects, the subject for treatment comprises all of the factors IF1-IF7. In certain aspects, at the start of treatment, at least one, more than one or all of the following exclusion factors EF1-EF17 are applicable to subjects for treatment: EF1. Having central nervous system metastases that: EF1.1: are untreated or symptomatic, whereas subjects having untreated, asymptomatic lesions can be included if considered stable; EF1.2 require radiation or surgery; EF1.3 require continued steroid therapy (> 10 mg prednisone or equivalent) to control symptoms within 14 days of administration prior to administration of the first dose. Subjects with other central nervous system metastasis are allowed. EF2. Having known leptomeningeal involvement. EF3. Participation in another clinical study or treatment with any investigational drug within 4 weeks prior to administration of the first dose. EF4. Administration of systemic anticancer therapy or immunotherapy within 4 weeks or 5 half-lives, whichever is shorter, of the first dose of study drug. For cytotoxic agents that have major delayed toxicity (e.g., mitomycin C, nitrosoureas), a washout period of 6 weeks is required. EF5. Having undergone major surgery or radiotherapy within 3 weeks of administration of the first dose. Subjects who received prior radiotherapy to equal or more than 25% of bone marrow at any time are not eligible. Subjects who received radiotherapy on lung at any time are not eligible. EF6. Having persistent Grade > 1 clinically significant toxicity, related to prior antineoplastic therapies (except for alopecia); with the proviso that stable sensory neuropathy with a grade equal to 2 or lower of NCI-CTCAE v5.0 and hypothyroidism with a grade equal to 2 or lower which is stable on hormone replacement is not excluded. EF7. Having a history of hypersensitivity reaction or any toxicity attributed to human proteins or any of the excipients that warranted permanent cessation of these agents. EF8. Having a history of clinically significant cardiovascular disease including, but not limited to: EF8.1 Having prolonged QT interval >470 msec, (for women) and >450 msec (for men), obtained from 3 electrocardiograms (ECGs), or clinically significant cardiac arrythmia, conduction or morphology of resting ECG (i.e., complete left bundle branch block, third degree heart block and second degree heart block), or electrophysiologic disease (i.e., placement of implantable cardioverter defibrillator or atrial fibrillation with uncontrolled rate) or any factors that increase the risk of QTc prolongation or risk of arrhythmic events such as electrolyte abnormalities. Subjects with cardiac pacemakers who are clinically stable are eligible. EF8.2 Having heart failure, congenital long QT syndrome, family history of long QT syndrome, or unexplained sudden death under 40 years of age in first-degree relatives or any concomitant medication known to prolong the QT interval and cause Torsades de Pointes. EF8.3 Having uncontrolled (persistent) arterial hypertension: systolic blood pressure >180 mm Hg and / or diastolic blood pressure >100 mm Hg. EF8.4 Having congestive heart failure (CHF) defined as New York Heart Association (NYHA) class III-IV or hospitalization for CHF within 6 months of the first dose of study drug. EF9. Having a history of interstitial lung disease (ILD) or pneumonitis, or any evidence of clinically active ILD or pneumonitis. EF10. Having a previous or concurrent malignancy, excluding non-basal cell carcinomas of skin or carcinoma in situ of the uterine cervix, unless the tumor was treated with curative or palliative intent and the previous or concurrent malignancy condition does not affect the assessment of safety and efficacy of the study drug. EF11. Having current serious illness or medical conditions including, but not limited to uncontrolled active infection, clinically significant pulmonary, metabolic or psychiatric disorders. EF12. Having active Hepatitis B infection (HBsAg positive) without receiving antiviral treatment. Subjects with active hepatitis B (HbsAg positive) must receive antiviral treatment with lamivudine, tenofovir, entecavir, or other antiviral agents, starting at least 7 days or more before administration of the first dose. Subjects with antecedents of Hepatitis B (anti-HBc positive, HbsAg and HBV-DNA negative) are eligible. EF13. Having a positive test for Hepatitis C ribonucleic acid (HCV RNA); Subjects in whom HCV infection resolved spontaneously (positive HCV antibodies without detectable HCV-RNA) or those who achieved a sustained virological response after antiviral treatment and show absence of detectable HCV RNA equal to or more than 6 months (with the use of IFN-free regimens) or equal to or more than 12 months (with the use of IFN-based regimens) after cessation of antiviral treatment are eligible. EF14. Having a known history of HIV (HIV 1 / 2 antibodies). Patients with HIV with undetectable viral load are allowed. HIV testing is not required unless mandated by local health authority or regulations. EF15. In case of sexually active male and female patients of childbearing potential agree to use one of the following methods of birth control during the entire duration of the study and for 6 months after final administration of PB19478: • combined (estrogen and progestogen containing) hormonal contraception associated with inhibition of ovulation (oral, intravaginal, transdermal) • progestogen-only hormonal contraception associated with inhibition of ovulation (oral, injectable, implantable) • intrauterine device (IUD) • intrauterine hormone-releasing system (IUS) • bilateral tubal occlusion • vasectomized partner • sexual abstinence EF16. Being pregnant or breast-feeding. EF17. Having peripheral neuropathy Grade 2 or higher. In certain aspects, the subject for treatment complies with one or more factors selected from the group consisting of EF1-EF17. In certain aspects, the subject for treatment complies with all of the factors EF1-EF17. Herein, the ECOG Performance Status Scale with indicated grade and performance status is as follows: Grade 0: Fully active, able to carry on all pre-disease performance without restriction. Grade 1: Restricted in physically strenuous activity but ambulatory and able to carry out work of a light or sedentary nature, e.g., light house work, office work. Grade 2: Ambulatory and capable of all selfcare but unable to carry out any work activities; up and about more than 50% of waking hours. Grade 3: Capable of only limited selfcare; confined to bed or chair more than 50% of waking hours. Grade 4: Completely disabled; cannot carry on any selfcare; totally confined to bed or chair. Grade 5: Dead. Herein, calculation of renal clearance is according to Cockcroft & Gault formula for subjects aged <65 years: Male=1.25 x weight (kg) x (140-age) / serum creatinine (µmol / L). Female=1.04 x weight (kg) x (140-age) / serum creatinine (µmol / L). Herein, calculation of MDRD (Modification of Diet in Renal Disease) is according to the following formula: Patients aged >65 years. For a male subject older than 65 years of age, calculation is as follows: Male=186 x (serum creatinine (µmol / L) x 0,0113)-1,154x age- 0,203. For dark skinned subjects, the outcome is multiplied by 1.21. For female subjects, the outcome is multiplied by 0.742. For calculation of carboplatin dosing, AUC x clearance of creatinine is used as follows. Clearance is first calculated as mentioned above according to Cockcroft and Gault followed by multiplying by 3, 4 or 5, depending on whether AUC 3 AUC 4 or AUC 5 is desirable. A reference herein to a patent document or other matter which is cited is not to be taken as an admission that that document or matter was known or that the information it contains was part of the common general knowledge as at the priority date of any of the claims. Where herein ranges are given as between number 1 and number 2, the range includes the number 1 and number 2. For instance a range of between 2-5 includes the number 2 and 5. As used herein, the term ‘cancer’ applies to the same as the term ‘tumor’, such that treatment of a tumor also applies to treatment of cancer. The conjunctive term “and / or” between multiple recited elements is understood as encompassing both individual and combined options. For instance, where two elements are conjoined by “and / or,” a first option refers to the applicability of the first element without the second. A second option refers to the applicability of the second element without the first. A third option refers to the applicability of the first and second elements together. Any one of these options is understood to fall within the meaning, and therefore satisfy the requirement of the term “and / or” as used herein. Concurrent applicability of more than one of the options is also understood to fall within the meaning, and therefore satisfy the requirement of the term “and / or.” For the purpose of clarity and a concise description, features are described herein as part of the same or separate embodiments, however, it will be appreciated that the scope of the disclosure may include embodiments having combinations of all or some of the features described. BRIEF DESCRIPTION OF THE DRAWINGS Figure 1. Amino acid sequence of the heavy chain variable regions of variable domains referred to in this application. Figure 2. MF3370 and variants thereof. The CDR1, CDR2 and CDR3 sequences in MF8226 are underlined from left to right. The CDRs in the other sequences are at the corresponding positions (according to Kabat). Figure 3. MF4356 and variants thereof. The CDR1, CDR2 and CDR3 sequences in MF4356 are underlined from left to right. The CDRs in the other sequences are at the corresponding positions (according to Kabat). Figure 4. Common light chain used in mono- and bispecific IgG. Figure 4A: Common light chain amino acid sequence. Figure 4B: Common light chain variable domain DNA sequence and translation (IgGVK1-39 / jk1). Figure 4C: Common light chain constant region DNA sequence and translation. Figure 4D: IgGVK1-39 / jk5 common light chain variable domain translation. Figure 4E: V-region IgGKV1-39A. Figure 5. IgG heavy chains for the generation of bispecific molecules. Figure 5A: CH1 region. Figure 5B: hinge region. Figure 5C: CH2 region. Figure 5D: CH2 containing L235G and G236R silencing substitutions. Figure 5E: CH3 domain containing substitutions L351K and T366K (KK). Figure 5F; CH3 domain containing substitutions L351D and L368E (DE). Clauses 1. A bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in a method of treatment of a cancer in a subject. 2. A method of treating a subject having a cancer, said treatment comprising administering to the subject an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent to said subject. 3. The use or method of any one of the preceding clauses, wherein said chemotherapeutic agent is or comprises a platinum-based compound and / or a taxane. 4. The use or method of any one of the preceding clauses, wherein said chemotherapeutic agent is or comprises paclitaxel and / or carboplatin. 5. The use or method of any one of the preceding clauses, wherein said chemotherapeutic agent is or comprises docetaxel. 6. The use or method of any one of the preceding clauses, wherein said cancer is an advanced or a metastatic cancer. 7. The use or method of any one of the preceding clauses, wherein said cancer is lung cancer, in particular non-small cell lung cancer. 8 The use or method of any one of the preceding clauses, wherein said cancer or said subject is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor, such as osimertinib. 9. The use or method of clause 8, wherein said cancer or said subject has not been previously treated with a chemotherapeutic agent. 10. The use or method of clause 8, wherein said cancer or said subject is furthermore resistant to treatment with a platinum-based chemotherapy. 11 The use or method of any one of the preceding clauses, wherein said subject or said cancer has been previously treated with a third generation EGFR tyrosine kinase inhibitor, such as osimertinib. 12. The use or method of clause 11, wherein said subject or said cancer has not been previously treated with a chemotherapeutic agent. 13. The use or method of clause 11, wherein said subject or said cancer has been previously treated with a platinum-based chemotherapy. 14. The use or method according to any one of clauses 8-13, wherein said third- generation EGFR tyrosine kinase inhibitor comprises or is osimertinib, lazertinib, alflutinib, rezivertinib, olmutinib, almonertinib, abivertinib, ASK120067, befotertinib, rociletinib, oritinib (SH-1028), nazartinib (EGF816), naquotinib (ASP8273), furmonertinib, mavelertinib (PF-0647775), olafertinib (CK-101), keynatinib or ES-072. 15. The use or method according to any one of clauses 8-14, wherein said third- generation EGFR tyrosine kinase inhibitor comprises or is osimertinib, furmonertinib, almonertinib, befotertinib or lazertinib. 16. The use or method according to any one of clauses 8-14, wherein said third- generation EGFR tyrosine kinase inhibitor comprises or is osimertinib. 17. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 600 mg once every two weeks. 18. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1000 mg once every two weeks. 19. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1500 mg once every two weeks. 20. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 2000 mg once every two weeks. 21. The use or method of any one of the preceding clauses, wherein paclitaxel is administered in an amount of between 50 and 200 mg / m2 body surface once every three weeks and carboplatin is administered at AUC 3, AUC 4 or AUC 5 once every three weeks. 22. The use or method of any one of the preceding clauses, wherein paclitaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. 23. The use or method of any one of the preceding clauses, wherein paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks. 24. The use or method of any one of the preceding clauses, wherein paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks. 25. The use or method of any one of the preceding clauses, wherein paclitaxel is administered in an amount of 175 mg / m2 body surface once every three weeks. 26. The use or method of any one of the preceding clauses, wherein paclitaxel is administered in an amount of 200 mg / m2 body surface once every three weeks. 27. The use or method of any one of the preceding clauses, wherein carboplatin is administered at AUC 3 once every three weeks. 28. The use or method of any one of the preceding clauses, wherein carboplatin is administered at AUC 4 once every three weeks. 29. The use or method of any one of the preceding clauses, wherein carboplatin is administered at AUC 5 once every three weeks. 30. The use or method of any one of the preceding clauses, wherein docetaxel is administered in an amount of between 20 and 100 mg / m2 body surface once every three weeks. 31. The use or method of any one of the preceding clauses, wherein docetaxel is administered in an amount of 40 mg / m2 body surface once every three weeks. 32. The use or method of any one of the preceding clauses, wherein docetaxel is administered in an amount of 55 mg / m2 body surface once every three weeks. 33. The use or method of any one of the preceding clauses, wherein docetaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. 34. The use or method of any one of the preceding clauses, wherein docetaxel is administered in an amount of 100 mg / m2 body surface once every three weeks. 35. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 2000 mg once every weeks, paclitaxel is administered in an amount of 175 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 5 once every three weeks. 36. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1500 mg once every weeks, paclitaxel is administered in an amount of 175 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 5 once every three weeks. 37. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1500 mg once every weeks, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 4 once every three weeks. 38. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1000 mg once every weeks, paclitaxel is administered in an amount of 150 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 4 once every three weeks. 39. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1000 mg once every weeks, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 3 once every three weeks. 40. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 600 mg once every weeks, paclitaxel is administered in an amount of 100 mg / m2 body surface once every three weeks, carboplatin is administered at AUC 3 once every three weeks. 41. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 2000 mg once every two weeks and docetaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. 42. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered in an amount of 1500 mg once every two weeks and docetaxel is administered in an amount of 75 mg / m2 body surface once every three weeks. 43. The use or method of any one of the preceding clauses, wherein said bispecific antibody is administered prior to said a chemotherapeutic agent when administration of said antibody and chemotherapeutic agents occurs on the same day. 44. The use or method of any one of the preceding clauses, wherein said cancer is an EGFR positive and / or cMET positive cancer. 45. The use or method of any one of the preceding clauses, wherein said cancer or subject comprises an EGFR-dependent resistance and / or cMET-dependent resistance to osimertinib. 46. The use or method of any one of the preceding clauses, wherein said cancer or subject comprises an EGFR-dependent resistance to osimertinib, such as an approved EGFR tyrosine kinase inhibitor resistance mutation, a tertiary EGFR tyrosine kinase inhibitor resistance mutation, a mutation that reduces binding of a third generation EGFR tyrosine kinase inhibitor to EGFR, an acquired EGFR tyrosine kinase inhibitor resistance mutation or an EGFR gene amplification. 47. The use or method of any one of the preceding clauses, wherein said cancer or subject comprises a cMET-dependent resistance to osimertinib, such as a cMET amplification, cMET overexpression, increased signaling of the cMET pathway, a cMET gene amplification and / or increased cMET protein activity. 48. The use or method of any one of the preceding clauses, wherein said cancer or subject comprises an osimertinib resistance selected from a HER2 amplification, resistance via RAS-MAPK pathway activation, resistance via PI3K pathway activation, cell-cycle gene alterations and an oncogenic fusion. 49. The use or method of any one of the preceding clauses, wherein the cancer or subject comprises a cMET amplification characterized by cMET / CEP7 > 5 or cfDNA ≥ 2 copies or any combination thereof. 50. The use or method of any one of the preceding clauses, wherein the cancer or subject comprises a cMET amplification characterized by a MET / CEP7 of between ≥ 3 and 20, such as MET / CEP7 ≥ 4, MET / CEP7 ≥ 5, up to 15 or up to 20, or a cMET amplification characterized by cfDNA of between ≥ 1.8 cMET and up to 5 copies, or between at least 1.8 and at most 2.2, or between at least 2.2 and at most 5, or at least 5 and higher. 51. The use or method of any one of the preceding clauses, wherein the cancer or subject comprises an EGFR exon 20 mutation, in certain aspects an exon 20 insertion mutation, in certain aspects an in-frame exon 20 insertion mutation. 52. The use or method of any one of the preceding clauses, wherein said subject or cancer comprises an EGFR mutation including an exon 20 mutation, an exon 20 insertion, or a mutation selected from L692X (e.g. L692V), E709X (e.g. E709K), L718X (e.g. L718Q, L718V), G719X (e.g. G719A), G724X (e.g. G724S), S768X (e.g. S768I), L792X (e.g. L792H, L792F, L792R, L792Y, L792V, L792P), G796X (e.g. G796S, G796D, G796R), C797X (e.g. C797S, C797G), L798X (e.g. L798I), L817Q, and L844X (e.g. L844V). 52. The use or method of any one of the preceding clauses, wherein said subject or cancer comprises an EGFR mutation including an exon 20 mutation, an exon 20 insertion, or an osimertinib resistance mutation selected from L718X (e.g. L718Q, L718V), G719X (e.g. G719A), G724X (e.g. G724S), S768X (e.g. S768I), L792X (e.g. L792H, L792F, L792R, L792Y, L792V, L792P), G796X (e.g. G796S, G796D, G796R), C797X (e.g. C797S, C797G), and L817X (e.g. L817Q). 53. The use or method of any one of the preceding clauses, wherein said subject or cancer comprises EGFR mutation C797X (e.g. C797S, C797G, C797N). 54. The use or method of any one of the preceding clauses, wherein said subject or cancer comprises EGFR mutation C797S. 55. The use or method of any one of the preceding clauses, wherein said subject or cancer comprises an EGFR mutation conferring resistance to osimertinib, such as C797X or L792X, and a further mutation including an exon 19 deletion, T790M or L858R. 56. The use or method of any one of the preceding clauses, wherein said subject or cancer comprises a double or triple mutation selected from exon19del / L792X (e.g. exon19del / L792H, exon19del / L792F, exon19del / L792Y), exon19del / C797X (e.g. exon19del / C797S), L858X / T790X / C792X (e.g.L858R / T790M / C792H, L858R / T790M / C792F, L858R / T790M / C792Y), L858X / T790X / C797X (e.g. L858R / T790M / C797S), L858X / T790X / L718X (e.g. L858R / T790M / L718Q), exon19del / T790X / C797X (e.g. exon19del / T790M / C792H, exon19del / T790M / C792F, exon19del / T790M / C792Y), exon19del / T790X / C797X (e.g. exon19del / T790M / C797S), exon19del / T790X / C718X (e.g. exon19del / T790M / C718Q). 57. The use or method according to any one of the preceding clauses, wherein the treatment comprises administering said bispecific antibody and said chemotherapeutic agent to a subject in need thereof, wherein said bispecific antibody is administered simultaneously, sequentially or separately with said chemotherapeutic agent. 58. The use or method according to any one of the preceding clauses, wherein the treatment comprises administering said bispecific antibody and said chemotherapeutic agent to a subject in need thereof, wherein said bispecific antibody is administered prior to, simultaneously with, or after said chemotherapeutic agent. 59. The use or method according to any one of the preceding clauses, when if administration of said bispecific antibody and said chemotherapeutic agent is on the same day, said bispecific antibody is administered prior to said chemotherapeutic agent. 60. The use or method according to any one of the preceding clauses, wherein the subject is a human subject. 61. A product comprising a chemotherapeutic agent and a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET). 62. A pharmaceutical composition comprising a chemotherapeutic agent and instructions for the use of said chemotherapeutic agent with a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) in the treatment of cancer. 63. A pharmaceutical composition comprising a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and instructions for the use of said bispecific antibody with a chemotherapeutic agent in the treatment of cancer. 64. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the antibody is a human antibody. 65. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the antibody is ADCC enhanced. 66. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the antibody is an IgG1 format antibody having an anti- EGFR, anti-cMET stoichiometry of 1:1. 67. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the antibody has one variable domain that can bind EGFR and one variable domain that can bind cMET. 68. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the variable domain that can bind human EGFR can also bind cynomolgus and mouse EGFR. 69. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the variable domain that can bind human EGFR binds to domain III of human EGFR. 70. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the variable domain that can bind cMET blocks the binding of antibody 5D5 to cMET. 71. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the variable domain that can bind cMET blocks the binding of HGF to cMET. 72. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the amino acids at positions 405 and 409 in one CH3 domain are the same as the amino acids at the corresponding positions in the other CH3 domain (EU-numbering). 73. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYX1X2NTNYAQKLQG and a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY, wherein X1 = N or S; X2 = A or G; X3 = D or G; X4 = R, S or Y; X5 = H, L or Y; X6 = D or W and X7 = D or G; with 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof at a position other than X1- X7 and wherein the second variable domain comprises a heavy chain variable region with the amino acid sequence of one of the sequences of SEQ ID NO: 1-23 with 0-10 preferably 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. 74. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein X1 = N; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = A; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = S; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; X1 = N; X2 = A; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; or X1 = S; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G 75. The use, method, product or pharmaceutical composition according to any one of the preceding clauses wherein X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D. 76. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D. 77. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the heavy chain variable region of the second variable domain comprises the amino acid sequence of one of the sequences of SEQ ID NO: 1-3; 7; 8; 10; 13; 15; 16; 17; 21; 22 or 23 with 0-10 preferably 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. 78. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the heavy chain variable region of the second variable domain comprises the amino acid sequence of one of the sequences of SEQ ID NO: 2; 7; 8; 10; 13 or 23 with 0-10 preferably 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof. 79. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. 80. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. 81. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYSGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP. 82. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP. 83. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. 84. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYSGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP. 85. The use, method, product or pharmaceutical composition according to any one of the preceding clauses, wherein the first and second variable domain comprise a common light chain, including the light chain variable domain of figure 4B. 86. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the first and second variable domain comprise a light chain with a CDR1, CDR2 and CDR3 amino acid sequence, such as QSISSY, AAS, and QQSYSTP, respectively (according to IMGT). 87. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP or a CDR3 comprising the sequence ETYYYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin. 88. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin. 89. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the antibody comprises or is pamvatamig. 90. The use, method or pharmaceutical combination according to any one of the preceding clauses, wherein the antibody inhibits HGF induced growth of an HGF- growth responsive cell. 91. The use, method or pharmaceutical combination according to any one of the preceding clauses, which antibody inhibits EGF induced growth of an EGF-growth responsive cell. 92. A method of treating cancer in a subject, comprising - identifying a subject as having an EGFR tyrosine kinase inhibitor resistance, such as to osimertinib, and - administering to the subject a therapeutically effective amount of said bispecific antibody and a chemotherapeutic agent, thereby treating the cancer in the subject. 93. The method according to clause 92, wherein the antibody comprises or is pamvatamig. 94. A bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in the treatment of cancer in a subject, comprising - providing a sample from the cancer of said subject, and - determining the presence or absence of an EGFR tyrosine kinase inhibitor resistance in the sample, wherein if the sample is determined to comprise the presence of said EGFR tyrosine kinase inhibitor resistance, said subject is administered a therapeutically effective amount of said bispecific antibody and of said chemotherapeutic agent, thereby treating the cancer in the subject. 95. The use according to clause 94, wherein the antibody comprises or is pamvatamig. 96. A method of treating a subject from having cancer, comprising - providing a sample from the cancer of said subject, and - determining the presence or absence of an EGFR tyrosine kinase inhibitor resistance in the sample, wherein if the sample is determined to comprise the presence of said resistance, said subject is administered an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent, thereby treating the cancer in the subject. 97. A method of treating cancer in a subject identified as having an EGFR tyrosine kinase inhibitor resistance, such as to osimertinib, comprising administering to the subject an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent, thereby treating the cancer in the subject. 98. The method according to clause 96 or 97, wherein the antibody comprises or is pamvatamig. EXAMPLES As used herein “MFXXXX” wherein X is independently a numeral 0-9, refers to a Fab comprising a variable domain wherein the VH has the amino acid sequence identified by the 4 digits. Unless otherwise indicated the light chain variable region of the variable domain typically has a sequence of Figure 4A, typically 4B. “MFXXXX VH” refers to the amino acid sequence of the VH identified by the 4 digits. The MF further comprises a constant region of a light chain and a constant region of a heavy chain that normally interacts with a constant region of a light chain. PG refers to a monospecific antibody comprising identical heavy and light chains. PB refers to a bispecific antibody with two different heavy chains. The VH variable regions of the heavy chains differ and typically also the CH3 region, wherein one of the heavy chains has a KK mutation of its CH3 domain and the other has the complementing DE mutation of its CH3 domain (see for reference PCT / NL2013 / 050294 (published as WO2013 / 157954). Reference is made to PCTNL / 2018 / 050537 (published as WO2019 / 031965) for details on production of antibodies of the present disclosure. Bispecific antibodies binding EGFR and cMET suitable for use in the appended examples and for use in the methods of the disclosure include those of Tables 3, 4, 5 and 6. In particular, bispecific antibody PB19478 or pamvatamig is suitably used in the appended examples. Each bispecific antibody comprises two VH as specified by the MF numbers capable of binding EGFR and cMET respectively, further comprises an Fc tail with a KK / DE CH3 heterodimerization domain as indicated in Figure 5e and Figure 5f, respectively, a CH2 domain as indicated by Figure 5d, a hinge domain as indicated by Figure 5b, a CH1 domain as indicated by Figure 5a and a common light chain as indicated by Figures 4a-e. For example, a bispecific antibody indicated by MF8233 x MF8230 has the above general sequences and a variable domain with a VH with the sequence of MF8233 and a variable domain with a VH with the sequence of MF8230 and is preferably used in the appended examples. Example 1 Generation of bivalent monoclonal antibodies and antibody characterization VH genes of unique antibodies, as judged by VH gene sequence and some sequence variants thereof, were cloned in the backbone IgG1 vector. Suspension adapted 293F Freestyle cells were cultivated in T125 flasks at a shaker plateau until a density of 3.0 x 106cells / ml. Cells were seeded at a density of 0.3-0.5 x 106viable cells / ml in each well of a 24-deep well plate. The cells were transiently transfected with the individual sterile DNA: PEl mixture and further cultivated. Seven days after transfection, supernatant was harvested and filtrated through 0.22 µM (Sartorius) and purified on protein A beads using batch purification followed by a buffer exchange to PBS. Cross block assay cMET antibodies cMET specific phages were tested for competition with cMET reference antibodies in ELISA. Therefore 2.5µg / ml of cMET-Fc fusion protein was coated overnight to MAXISORPTM ELISA plates at 4°C. Wells of the ELISA plates were blocked with PBS (pH 7.2) containing 2% ELK for 1 H at RT while shaking (700rpm). Next reference or negative control IgG was added at a concentration of 5 µg / ml and allowed to bind for 15 min at RT at700rpm. Next, 5µl of PEG precipitated phage was added and allowed to bind for 1H at RT at 700rpm. Bound phages were detected with HRP labelled anti-M13 antibody for 1H at RT at 700rpm. As a control the procedure was performed simultaneously with an antibody specific for the coated antigens and a negative control phage. Bound secondary antibody was visualized by TMB / H2O2 staining and staining was quantified by means of OD450nm measurement. Table 3 demonstrates that MF4040 and MF4356 show competition with the 5D5 reference antibody. MF4297 competes with 13.3.2 and C8H241 to a lesser extent. The positive control phages all show complete competition with the corresponding IgG, whereas the no antibody control, does not influence the competition assay. Generation of bispecific antibodies Bispecific antibodies were generated by transient co-transfection of two plasmids encoding IgG with different VH domains, using a proprietary CH3 engineering technology to ensure efficient heterodimerisation and formation of bispecific antibodies. The common light chain is also co-transfected in the same cell, either on the same plasmid or on another plasmid. In our co-pending applications (e.g. WO2013 / 157954 and WO2013 / 157953; incorporated herein by reference) we have disclosed methods and means for producing bispecific antibodies from a single cell, whereby means are provided that favor the formation of bispecific antibodies over the formation of monospecific antibodies. These methods can also be favorably employed in the present disclosure. Specifically, preferred mutations to produce essentially only bispecific full length IgG molecules are amino acid substitutions at positions 351 and 366, e.g. L351K and T366K (numbering according to EU numbering) in the first CH3 domain (the 'KK-variant' heavy chain) and amino acid substitutions at positions 351 and 368, e.g. L351D and 10 L368E in the second CH3 domain (the 'DE-variant' heavy chain), or vice versa. It was previously demonstrated in our co-pending applications that the negatively charged DE-variant heavy chain and positively charged KK- variant heavy chain preferentially pair to form heterodimers (so-called 'DEKK' bispecific molecules). Homodimerization of DE-variant heavy chains (DE-DE homodimers) or KK-variant heavy chains (KK-KK homodimers) are disfavored due to strong repulsion between the charged residues in the CH3-CH3 interface between identical heavy chains. Table 4 shows which cMET and EGFR Fab arms were cloned in the appropriate KK and DE vectors. After production, bispecific IgG were purified by protein-A batch purification and the buffer was exchanged to PBS. Successful productions resulted in an IgG1 full length antibody, with a minimal concentration of 0.1 mg / ml, which were assigned a unique code (PBnnnnn; where nnnnn represents a randomly generated number) to identify the specific combination of 2 different target binding Fab fragments. Successfully produced bispecific IgG were tested for binding to their respective targets in ELISA. Reference is made herein to PCTNL / 2018 / 050537 (published as WO2019 / 031965) for more details on production of bispecific antibodies. Example 2 Screening of c-MET x EGFR bispecific antibodies in an EGF / HGF and HGF and EGF proliferation assay The potency of a panel of cMET x EGFR bispecific antibodies was tested in N87 cells using an HGF / EGF, HGF and EGF assays. The N87 cell line, official name NCI- N87, is a gastric carcinoma cell line derived from a metastatic site and has high EGFR expression levels and intermediate cMET expression levels (Zhang et al, 2010). Antibodies were tested in an 8 steps semi-log titration ranging from 10 µg / ml to 3.16 ng / ml. Each antibody was tested in duplicate. The anti-RSV-G antibody PG2708 was used as negative control. The reference antibody 2994 Fab was used as positive control for the HGF assay and the reference antibody cetuximab was used as positive control for the EGF assay. An equimolar 1:1 cetuximab / 5D5 Fab was used as positive control for the EGF, HGF and EGF / HGF assays. Wells with either one, or a combination of ligand, as well as medium control were included to determine the assay window. Antibodies were diluted in chemically defined starvation medium (CDS: RPMI1640 medium, containing 80U penicillin and 80µg of streptomycin per ml, 0.05% (w / v) BSA and 10µg / ml holo-transferrin) and 50µl of diluted antibody was added to the wells of a 96 wells black well clear bottom plate (Costar). Ligand was added (50µl per well of a stock solution containing 400ng / ml HGF and 4ng / ml of EGF, and a EGF / HGF concentration of 4 ng / ml EGF / 400 ng / ml HGF diluted in CDS: R&D systems, cat. nr. 396-HB and 236-EG). N87 cells were trypsinised, harvested and counted and 8000 cells in 100µl of CDS were added to each well of the plate. To avoid edge effects, plates were left for an hour at RT before being put in a container inside a 37°C cell culture incubator for three days. On the fourth day, Alamar blue (Invitrogen, # DAL1100) was added (20µl per well) and the fluorescence was measured after 6 hours of incubation (at 37°C) with Alamar blue using 560nm excitation and 590nm readout on a Biotek Synergy 2 Multi-mode microplate reader. Fluorescence values were normalised to uninhibited growth (no antibody, but both ligands added). Table 5 lists the results of the various experiments. In the N87 HGF / EGF assay, fourteen different cMETxEGFR bispecifics with potency comparable to the reference monospecific antibodies (equimolar mix of cetuximab and 5D5 Fab) were identified: PB7679, PB7686, PB8218, PB8244, PB8292, PB8316, PB8340, PB8364, PB8388, PB8511, PB8535, PB8583, PB8607 and PB8640. In the N87 EGF assay, eleven different cMETxEGFR bispecifics with potency comparable to monospecific cetuximab were identified: PB7679, PB8244, PB8292, PB8340, PB8364, PB8388, PB8511, PB8535, PB8583, PB8607 and PB8640. They all contain the EGFR Fab arm MF3755. In the HGF N87 assay nine bispecifics were identified that showed a higher potency compared to the monospecific 5D5 Fab reference antibody: PB8218, PB8388, PB8511, PB8532, PB8535, PB8545, PB8583, PB8639 and PB8640. They contain six different cMET Fab arms MF4040, MF4297, MF4301, MF4356, MF4491 and MF4506. ADCC activity The ADCC activity of the 24 cMetxEGFR bispecifics was tested to the tumor cell lines N87 (EGFR-high, cMET-low) and MKN-45 (EGFR-low, cMET-amplified). The ADCC assay was performed using the Promega ADCC Bioassay kit in 384-well plate format. Antibodies were tested in duplicate at 9 different concentrations in semi-log serial dilutions ranging from 10 µg / ml to 1 ng / ml. The reference cetuximab antibody was included as a positive control for the assay and PG2708 was used as negative control antibody. Antibodies or assay medium control (no IgG) were incubated for 6 hours of induction at 37°C with ADCC effector cells, and target cells (N87 or MKN-45). Luciferase activity was quantified using Bio-Glo luciferase reagent. An example of the ADCC assay is shown in Figure 15 of WO2019 / 031965. None of the cMETxEGFR bispecifics showed a significant ADCC activity in both cell lines. The positive control reference cetuximab antibody showed a dose-dependent ADCC activity to both cell lines. Five bispecifics composed of EGFR and cMet arms which did show high efficacy in the N87 HGF / EGF assay and showed high sequence diversity (Table 6) were selected for further analysis. Two from the five bispecifics contain MF4356, which competes with 5D5 for binding to cMET (Table 3). Table 6 summarizes the characteristics of the selected candidates. Example 3 Figure 2 depicts various sequences for alternative variable regions of the heavy chain of an EGFR binding variable domain as disclosed herein. Figure 3 depicts various sequences for alternative variable regions of the heavy chain of a cMET binding variable domain as disclosed herein. The heavy chain variable regions were used to create a number of different cMET x EGFR bispecific antibodies. The light chain in these antibodies has the sequence as depicted in figure 4B. Bispecific antibodies were produced as described in example 1. The antibodies were also produced as an ADCC enhanced version. ADCC enhanced versions were produced by including in the co- transfection of the antibody constructs, a DNA encoding a reductase enzyme that removes a fucose residue from the Fc region of IgG1. See table 7 for a list of bispecific antibodies used and their PB coding. Example 4 The heavy chain variable region (VH) of the cMET variable domain of PB8532 comprises the amino acid of MF4356 as depicted for instance in figure 3. The VH of the cMET variable domain of PB19748 comprises the amino acid sequence of MF8230 (see figure 3). The VH of the EGFR variable domain of PB8532 comprises the amino acid of MF3370 as depicted for instance in figure 2. The VH of the EGFR variable domain of PB19748 comprises the amino acid sequence of MF8233 of figure 2. The light chain in PB8532 and PB19748 is the same and is depicted in figure 4B. The cMET antibody LY2875358 antibody is among other described in Kim and Kim 2017. Example 5 This example describes a clinical trial protocol which may be suitably followed using any bispecific antibody mentioned herein but is tailored towards using PB19478 (specifically pamvatamig). Phase I Dose escalation In the dose escalation phase 1 part, PB19478 will be administered with increasing doses from 100 to 3000 mg to patients with NSCLC harboring an activating EGFR mutation (e.g. an approved TKI-resistance mutations) or c-MET amplification (MET / CEP7 >5 or cfDNA ≥2 copies). Allometric scaling of a preclinical PK model was used to predict bispecific antibody PB19478 exposure in humans. The PB19478 starting dose is 100 mg (flat dose, intravenously) once every 2 weeks (q2w), with 4-week cycles (28 days). Dose levels of 100 to 3000mg are initially planned to be investigated. Intermediate q2w dose levels, or alternative schedules (q1w, q3w) may be tested, until MTD is reached, based on the preliminary analysis in agreement with the investigators to better characterize safety, efficacy, PK, and / or pharmacodynamic activity. Using an RP2D of bispecific antibody PB19478 at an administration of 1500 mg, additional two cohorts will be opened to investigate the safety and tolerability of PB19478 in combination with paclitaxel (175 mg / m2) / carboplatin (AUC 5) or docetaxel (75 mg / m2) with at least 2 cycles of follow-up (each cycle having 28 days). The planned PB19478 dose levels for these combinations of treatment are 1500 mg and 2000 mg, and any intermediate dose levels in between may be explored to determine the maximum tested and safe dose in the combination treatment. Patients experiencing DLTs will not be replaced in the dose-escalation for the combination treatment. To confirm the safety of the maximum tested and safe dose, approximately 6 patients will be treated at the selected dose level for at least 2 cycles in each combination cohort. Dose expansion For dose expansion, two cohorts are investigated. Cohort 1, which comprises a second line NSCLC, osimertinib resistant, chemotherapy naïve population, is investigated using a combination of bispecific antibody PB19478 with paclitaxel / carboplatin. Cohort 2, which comprises a third line NSCLC, osimertinib resistant, platinum resistant population, is investigated using a combination of bispecific antibody PB19478 with docetaxel. For dose expansion cohort 1 with paclitaxel / carboplatin: ^Following the safety assessment from the dose escalation phase, if the maximumtested and safe dose for the PB19478 combination treatment is determined to be 1500 mg, a single arm cohort with up to 40 patients will be opened. ^If the maximum tested and safe dose for the PB19478 combination treatment ishigher than 1500 mg, the cohort will be opened to randomize patients in a 1:1 ratio to receive paclitaxel / carboplatin in combination with MCLA-129 at either 1500 mg or the maximum tested and safe dose for the purpose of dose optimization, with up to 40 patients in each randomized arm to characterize the efficacy and safety profile. For dose expansion cohort 2 with docetaxel: ^Following the determination of the maximum tested and safe dose for thePB19478 combination treatment in the dose-escalation phase, a single arm cohort will open for enrollment of approximately 30 patients treated with PB19478 at the maximum tested and safe dose in combination with docetaxel. Patients will be continuously monitored for DLT and other safety signals. Antitumor activity of PB19478 in any combination with said chemotherapeutic agents will be evaluated in terms of ORR, and an evaluation of other efficacy parameters, safety, tolerability, PK, immunogenicity, and biomarkers will be performed. STUDY POPULATION Inclusion criteria Patients must fulfill all of the following requirements to enter the study: 1. Signed informed consent before initiation of any study procedures. 2. Age ≥ 18 years at signature of informed consent. 3. Histologically or cytologically confirmed solid tumors with evidence of metastatic or locally advanced unresected disease that is incurable. 1. Expansion Part Cohort 1: NSCLC 2L, osimertinib resistant, chemotherapy naïve population or Cohort 2: NSCLC 3L, osimertinib resistant, platinum resistant (participant must have progressed on or after a previous platinum chemotherapy) population. 4. Availability of tissue sample formalin-fixed paraffin-embedded (FFPE), embedded after progression at the latest therapy. 5. Measurable disease as defined by RECIST version 1.1 by radiologic methods (patients with non-measurable but evaluable disease can be included in the dose escalation part). 6. Eastern Cooperative Oncology Group (ECOG) performance status of 0 or 1. 7. Life expectancy ≥ 12 weeks, as per Investigator judgment 8. Adequate organ function, as per Investigator judgment • Absolute neutrophil count (ANC) ≥1.5 X 109 / L • Hemoglobin ≥9 g / dL • Platelets ≥100 x 109 / L • Corrected total serum calcium within normal ranges • Serum potassium within normal ranges • Serum magnesium within normal ranges (or corrected with supplements) • Alanine aminotransferase (ALT), aspartate aminotransferase (AST) ≤2.5 x upper limit of normal (ULN) and total bilirubin ≤1.5 x ULN (patients with Gilbert’s syndrome are eligible if conjugated bilirubin value is within normal limits); in cases of liver involvement, ALT / AST ≤5 x ULN and total bilirubin ≤2 x ULN will be allowed • Serum creatinine ≤1.5 x ULN or creatinine clearance ≥50 mL / min calculated according to the Cockcroft and Gault formula or MDRD formula for patients aged >65 years (creatinine clearance ≥60 mL / min if the patient is receiving paclitaxel / carboplatin). • Serum albumin >3.3 g / dL • International Normalized Ratio (INR) or Prothrombin Time (PT) ≤1.5 x ULN unless the subject is receiving anticoagulant therapy • Activated Partial Thromboplastin Time (aPTT) or Partial Thromboplastin Time (PTT) ≤1.5 x ULN unless the subject is receiving anticoagulant therapy. Exclusion Criteria The presence of any of the following criteria excludes a patient from participating in the study: 1. Central nervous system metastases that: • are untreated or symptomatic (patients with untreated, asymptomatic lesions can be included if in the investigator judgment considered clinically and radiologically stable) (expansion phase only) • require radiation or surgery (expansion phase only) • require continued steroid therapy (>10 mg prednisone or equivalent) to control symptoms within 14 days of study entry (dose expansion phase only). Patients with other central nervous system metastasis are allowed. 2. Known leptomeningeal involvement (dose expansion phase only). 3. Participation in another clinical study or treatment with any investigational drug within 4 weeks prior to study entry. 4. [Previous criterion deleted; numbering kept] 5. Systemic anticancer therapy or immunotherapy within 4 weeks or 5 half-lives (whichever is shorter) of the first dose of study drug. For cytotoxic agents that have major delayed toxicity (e.g., mitomycin C, nitrosoureas), a washout period of 6 weeks is required. Note: For agents with long half-lives, enrollment before the fifth half-life requires Sponsor approval. Cohort E patients can continue to receive osimertinib, as last treatment. 6. Major surgery or radiotherapy within 3 weeks of the first dose of study drug. Patients who received prior radiotherapy to ≥25% of bone marrow at any time are not eligible. Patients who received radiotherapy on lung at any time are not eligible. 7. Persistent Grade >1 clinically significant toxicities, in the Investigator judgment, related to prior antineoplastic therapies (except for alopecia); stable sensory neuropathy Grade ≤2 NCI-CTCAE v5.0 and hypothyroidism Grade ≤2 which is stable on hormone replacement are allowed. 8. History of hypersensitivity reaction or any toxicity attributed to human proteins or any of the excipients that warranted permanent cessation of these agents. 9. History of clinically significant cardiovascular disease including, but not limited to in particular: • Prolonged QT interval >470 msec, (for women) and >450 msec (for men), obtained from 3 electrocardiograms (ECGs), or clinically significant cardiac arrythmia, conduction or morphology of resting ECG (ie., complete left bundle branch block, third degree heart block and second degree heart block), or electrophysiologic disease (i.e., placement of implantable cardioverter defibrillator or atrial fibrillation with uncontrolled rate) or any factors that increase the risk of QTc prolongation or risk of arrhythmic events such as electrolyte abnormalities. Patients with cardiac pacemakers who are clinically stable are eligible. • Heart failure, congenital long QT syndrome, family history of long QT syndrome, or unexplained sudden death under 40 years of age in first-degree relatives or any concomitant medication known to prolong the QT interval and cause Torsades de Pointes. • Uncontrolled (persistent) arterial hypertension: systolic blood pressure >180 mm Hg and / or diastolic blood pressure >100 mm Hg. • Congestive heart failure (CHF) defined as New York Heart Association (NYHA) class III-IV or hospitalization for CHF within 6 months of the first dose of study drug. 10. Past medical history of ILD or pneumonitis, or any evidence of clinically active ILD or pneumonitis. 11. Previous or concurrent malignancy, excluding non-basal cell carcinomas of skin or carcinoma in situ of the uterine cervix, unless the tumor was treated with curative or palliative intent and in the opinion of the Investigator, with Sponsor agreement, the previous or concurrent malignancy condition does not affect the assessment of safety and efficacy of the study drug (dose expansion phase only). 12. Current serious illness or medical conditions including, but not limited to uncontrolled active infection, clinically significant pulmonary, metabolic or psychiatric disorders. 13. Active Hepatitis B infection (HBsAg positive) without receiving antiviral treatment. Note: Patients with active hepatitis B (HbsAg positive) must receive antiviral treatment with lamivudine, tenofovir, entecavir, or other antiviral agents, starting at least ≥7 days before the initiation of the study treatment. Patients with antecedents of Hepatitis B (anti-HBc positive, HbsAg and HBV-DNA negative) are eligible. 14. Positive test for Hepatitis C ribonucleic acid (HCV RNA); Note: Patients in whom HCV infection resolved spontaneously (positive HCV antibodies without detectable HCV-RNA) or those who achieved a sustained virological response after antiviral treatment and show absence of detectable HCV RNA ≥6 months (with the use of IFN- free regimens) or ≥12 months (with the use of IFN-based regimens) after cessation of antiviral treatment are eligible. 15. Known history of HIV (HIV 1 / 2 antibodies). Patients with HIV with undetectable viral load are allowed. In patients with HIV, viral RNA load and CD4+ cell count should be monitored per local standard of care (e.g., every 3 months).HIV testing is not required unless mandated by local health authority or regulations. 16. Sexually active male and female patients of childbearing potential must agree to use one of the following highly effective methods of birth control* during the entire duration of the study and for 6 months after final administration of MCLA-129: • Combined (estrogen and progestogen containing) hormonal contraception associated with inhibition of ovulation (oral, intravaginal, transdermal) • Progestogen-only hormonal contraception associated with inhibition of ovulation (oral, injectable, implantable) • Intrauterine device (IUD) • Intrauterine hormone-releasing system (IUS) • Bilateral tubal occlusion • Vasectomized partner1• Sexual abstinence2*NOTE: Double barrier methods are not considered to be highly effective birth control methods. Sterility in female patients must be confirmed in the patient’s medical records and is defined as any of the following: surgical hysterectomy with bilateral oophorectomy, bilateral tubular ligation, natural menopause with last menses >1 year ago; radiation induced oophorectomy with last menses >1 year ago; chemotherapy- induced menopause with a 1-year interval since last menses.1A vasectomized partner is only a highly effective birth control method provided that partner is the sole sexual partner of the woman of childbearing potential and that the vasectomized partner has received medical assessment of the surgical success.2Sexual abstinence is considered a highly effective method only if defined as refraining from heterosexual intercourse during the entire period of risk associated with the study treatment. The reliability of sexual abstinence needs to be evaluated in relation to the clinical study and the preferred and usual lifestyle of the patient. 17. Pregnant or breast-feeding women are excluded from this study. 18. Peripheral neuropathy ≥Grade 2. INVESTIGATIONAL THERAPY AND REGIMEN PB19478 will be administered as an IV infusion, once every 2 weeks (q2w), with a starting dose of 100 mg (flat dose), with 4-week cycles. Dose levels are planned between 100 and 3000 (flat dose), including dosing at 600, 1000, 1500 and 2000 mg (flat dose). The administered dose, dose increments, and frequency of dosing for each patient (including the expansion cohorts) is subject to change based on patient safety, PK and pharmacodynamic data, and upon recommendation of the Sponsor. The Sponsor may recommend the use of an alternate weekly dosing schedule. Additional dose levels, or schedules may be tested, until MTD is reached, based on the preliminary analysis in agreement with the investigators. Paclitaxel 175 mg / m2 will be administered as an IV infusion over 10 minutes, followed by carboplatin AUC5 as an IV infusion over 60 minutes every 3 weeks. Premedication can be given according to local prescribing information. Docetaxel 75 mg / m2 will be administered as an IV infusion over 60 minutes every 3 weeks. Premedication can be given according to local prescribing information. Table 1: Study treatment for cohort 1 and 2 with PB19478 in combination with chemotherapy Screening Cycle 1Cycle 2 Cycle 3 Cycle 4 Cycle 5 Cycle 6 Cycle 7 Cycle 8 Cycle 9 etc etc etc ≤28 days before Day Day Day Day Day Day Day Day Day Day Day Day STUDY TREATMENT treatment 1 8 15 22 1 8 15 22 1 8 15 22 PB19478 (intravenous)1X X X X X X Administration of X X X X paclitaxel / carboplatin (Cohort 1)2Administration of docetaxel X X X X (Cohort 2)31PB19478 will be administered as an IV infusion, once every 2 weeks, on Day 1 and Day 15 of each cycle.2Paclitaxel 175 mg / m2will be administered as an IV infusion over 10 minutes, followed by carboplatin AUC5 as an IV infusion over 60 minutes every 3 weeks. On days that PB19478 is given in combination with chemotherapy (e.g. Day 1, cycle 1, cycle 4, cycle 7 with continued incremental steps of 3 weeks), PB19478 will be given before the chemotherapy. The infusion of the chemotherapeutic agents can start after PB19478 infusion and the respective premedication. CONCOMITANT MEDICATIONS Permitted ^ Paracetamol / acetaminophen, antihistamines and systemic corticosteroids are permitted in the event of an IRR, hypersensitivity or allergic reactions, according to standard local clinical practice. ^ All medication necessary for the wellbeing of the patient and which is not expected to interfere with evaluation of the study drug may be given at the Investigator’s discretion.^Supportive treatment of symptoms and adverse events (AEs) or standard treatment of concomitant conditions. ^ Concurrent radiation treatment during this study for symptom control (excluding lung radiation, see Prohibited concomitant medications). Prohibited ^ Concomitant chronic oral corticosteroids (>10 mg / day prednisone equivalent), or other immunosuppressive medication. ^ Any investigational drug, other anticancer therapy or immunotherapy during the study or within 4 weeks or 5 half-lives, whichever is shorter, prior to the first dose of study treatment. ^ For cytotoxic agents that have major delayed toxicity (e.g., mitomycin C, nitrosoureas), a washout period of 6 weeks is required. ^ Initiation of herbal remedies for cancer treatment. Herbal remedies initiated prior to study entry and continuing during the study are permitted and must be reported in the eCRF. ^ Major surgery or radiotherapy within 3 weeks prior to the first dose of study treatment. ^ Prior radiotherapy to lung or ≥25% of bone marrow. ^ Any medication taken by patients known to lead to a decrease in magnesium or potassium levels should be used with caution due to the potential safety risks associated with PB19478.^Drugs known to prolong the QTc interval with known risk of Torsades de Pointes. ^ For the combination cohorts with docetaxel coadministration with strong CYP3A4 inhibitor should be avoided as this may increase the exposure to docetaxel. Dose Modification Guidelines The following general dose modification guidelines apply to combination of bispecific antibody PB19478 with the chemotherapeutic agents as indicated. Recommended dose modifications for study drug and combination chemotherapeutics as indicated. If a patient in combination cohorts with chemotherapy has dose reduction of either study drug or combination drug, all drugs in the combination treatment should be reduced following the below table. Dose Level 0 Dose Level -1 Dose Level -2 PB19478 1500 mg 1000 mg 600 mgPB19478 2000 mg 1500 mg 1000 mgPaclitaxel 175 mg / m2 150 mg / m2 100 mg / m2Carboplatin AUC 5 AUC 4 AUC 3Docetaxel 75 mg / m2 55 mg / m2 40 mg / m2For patients with renally-impaired function treated with carboplatin, it is suggested to reduce the dose in case of reduced creatinine clearance in accordance with the creatine clearance levels of the below table. Creatinine clearance Carboplatin dose41-59 mL / min 250 mg / m216-40 mL / min 200 mg / m2All adverse events (AEs), whether or not considered related to the study drug, are graded using the NCI CTCAE v5.0 (see Common Terminology Criteria for Adverse Events (CTCAE) Version 5.0 Published: November 27, 2017. U.S. department of health and human services, National Institutes of Health, National Cancer Institute). AE grades reflect their severity, with Grade 1 meaning “mild”, Grade 2 meaning “moderate”, Grade 3 meaning “severe”, Grade 4 meaning “life-threatening” and Grade 5 meaning “fatal”. The worst grade is documented. The term “severity” is used to describe the intensity of an AE; the event itself, however, may be of relatively minor clinical significance (e.g., ‘severe’ headache). Severity is not the same as “serious”. Seriousness of AEs is based on the outcome / action of an AE and associated with events that pose a threat to a patient’s life or functioning. For AEs that cannot be graded according to the NCI CTCAE v5.0, intensity of the AE will be evaluated using the following criteria: ● Mild: The patient is aware of the sign or symptom, but finds it easily tolerated. The event is of little concern to the patient and of little clinical significance. The event is not expected to have any effects on the patient’s overall health or wellbeing. ● Moderate: The patient has discomfort enough to cause interference with or change in usual activities. The event is of some concern to the patient’s health or wellbeing and may require medical intervention and / or close follow-up. ● Severe: The AE interferes considerably with the patient’s usual activities. The event is of definite concern to the patient and / or poses substantial risk to the patient’s health or wellbeing. The event is likely to require medical intervention and / or close follow-up and may be incapacitating or life-threatening. Hospitalization and treatment may be required. Example 6 A 59 year old female patient with no significant medical history was diagnosed with NSCLC in 2018 and received loboectomy. Subsequently the cancer metastasized in 2019 to bone and lymph nodes. Before treatment was initiated with pamvatamig, the patient received prior treatment with afatinib and osimertinib. Treatment with osimertinib was suspended due to toxicity (G2 enteritis, G2 mucositis, G2 Dermatitis). The patient progressed on osimertinib for about 3 years but treatment was continued until June 2024. The patient showed stable disease (SD) upon treatment with osimertinib along with skin toxicity and neutropenia. The patient was tested positive for an EGFR del19 mutation and treated with pamvatamig at 1000 mg in combination with paclitaxel / carboplatin. The patient received 4 cycles of the combination treatment, and showed stable disease (SD) reaching a 26% reduction, as measured by CT scan. Treatment was stopped after the patient developed leptomeningeal carcinomatosis. Example 7 A 78 year old female patient with no significant medical history was diagnosed with NSCLC with metastases to bone, brain, liver and lymph node. Treatment was initiated with osimertinib and stopped after 13 months treatment due to disease progression. Subsequently, the patient was treated with carboplatin / pemetrexed which lasted for after about 7 months. Treatment with a combination of osimertinib and carboplatin / pemetrexed showed Partial Response (PR) as best response, but treatment was stopped due to disease progression. The patient was subsequently determined to carry EGFR mutation L858R and to have cMet amplification, and started on pamvatamig 1000 mg combined with docetaxel . The patient achieved a Partial response (PR) with the study drug with -32% tumor reduction as observed at the first scan. The patient received 4 cycles of treatment and 3 infusions of chemotherapy. cMET amplification status was determined by performing MET FISH using MET IQFISH Probe along with CEP7 (CE-IVD, Dako Omnis, Dako / Agilent). The number of invasive tumor cells were found to be 25. Average number of MET signals per nucleus were 19.2. Average number of CEP7 chromosome probes per nucleus were 7.2. Example 8 A 59 year old female patient with no significant medical history was diagnosed with NSCLC in May 2022 with metastases to bone, lymph node and pleura. The patient was first treated with osimertinib and achieved partial response (PR) as best response. The treatment was stopped after about 26 months due to disease progression. The mutational status in the patient was determined to be EGFR del19 and the patient was subsequently treated with pamvatamig 1500 mg together with carboplatin / paclitaxel. The patient received 4 cycles in total with 3 infusion of chemotherapy. The patient achieved a Partial Response (PR) under the study drugs and also showed a Complete Response on the target lesions. CITED ART Abhinandan and Martin, Mol. Immunol., 45: 3832-3839 (2008). Ahmed, M et al. Lack of in Vivo Antibody Dependent Cellular Cytotoxicity with Antibody containing gold particles / Bioconjugate chemistry (2015): 26812-816. DOI:10.1021 / acs.bioconjchem.5b00139. Al-Lazikani B. et al., J. Mol. Biol., 273: 927-948 (1997). Araya CL, Fowler DM. Trends Biotechnol.2011;29(9):435-42. Birchmeier, C, Birchmeier, W, Gherardi, E, et al. (2003). Met, metastasis, motility and more. Nat Rev Mol Cell Biol 4(12): 915-25. Castoldi, R., et al. "A novel bispecific EGFR / Met antibody blocks tumor-promoting phenotypic effects induced by resistance to EGFR inhibition and has potent antitumor activity." Oncogene 32.50 (2013): 5593-5601. Chmielecki J. et al. Analysis of acquired resistance mechanisms to osimertinib in patients with EGFR-mutated advanced non-small cell lung cancer from the AURA3 trial. Nat Commun. 2023 Feb 27;14(1):1071). Choi Y. et al. PLoS One. 2012;7(10):e46688. Chothia et al., J. Mol. Biol.196:901-917 (1987). Chothia et al., Nature 342: 877-883, 1989. Cunningham BC, Wells JA. Science. 1989;244(4908):1081-5). Eisenhauer et al., New response evaluation criteria in solid tumours: Revised RECIST guideline (version 1.1). European Journal of Cancer 45 (2009) 228-247) Ferguson KM. Structure-based view of epidermal growth factor receptor regulation. Annu Rev Biophys 2008;37: 353–73. Fu, K. et al. Therapeutic strategies for EGFR-mutated non-small cell lung cancer patients with osimertinib resistance. J Hematol Oncol.2022; 15:173. Giudicelli et al., Nucleic Acids Res.25: 206-211 (1997). He J. et al. Mechanisms and management of 3rd‑generation EGFR‑TKI resistance in advanced non‑small cell lung cancer. Int J Oncol. 2021;59(5):90. Honegger and Plückthun, J. Mol. Biol., 309:657-670 (2001). Jorissen RN., Exp Cell Res. Mar 10;284(1):31-53 (2003). Junttila, T. T., K. Parsons, et al. (2010). "Superior In vivo Efficacy of Afucosylated Trastuzumab in the Treatment of HER2-Amplified Breast Cancer." Cancer Research 70(11): 4481-4489). Kabat et al., J. Biol. Chem.252:6609-6616 (1977). Kabat et al., U.S. Dept. of Health and Human Services, “Sequences of proteins of immunological interest” (1991) Kim, George P., and Axel Grothey. "Targeting colorectal cancer with human anti-EGFR monoclonal antibodies: focus on panitumumab." Biologics 2.2 (2008): 223-228. Kim, Ki-Hyun and Kim, Hyori. Progress of antibody-based inhibitors of the HGF-cMET axis in cancer therapy. Experimental & Molecular medicine (2017), e307; doi:10.1038 / emm.2017.17). Kato et al. 2019 (Revisiting Epidermal Growth Factor Receptor (EGFR) Amplification as a Target for Anti-EGFR Therapy: Analysis of Cell-Free Circulating Tumor DNA in Patients With Advanced Malignancies. JCO Precis Oncol 3: PO.18.00180). Lefranc M.P. et al., Dev. Comp. Immunol., 27: 55-77 (2003). Leonetti et al in British Journal of Cancer (2019) 121:725–737. MacCallum et al., J. Mol. Biol.262:732-745 (1996). Maron, et al., 2018 (Targeted Therapies for Targeted Populations: Anti-EGFR Treatment for EGFR-Amplified Gastroesophageal Adenocarcinoma. Cancer Discov 8:696–713). Minari et al., Transl. Lung Cancer Res 2016;5(6):695-708. Moores, Sheri L., et al. "A novel bispecific antibody targeting EGFR and cMet is effective against EGFR inhibitor–resistant lung tumors." Cancer research 76.13 (2016): 3942-3953. Munro D, Singh M. Bioinformatics. 2020;36(22-23):5322–9. Oken MM, Creech RH, Tormey DC, Horton J, Davis TE, McFadden ET, Carbone PP. Toxicity and response criteria of the Eastern Cooperative Oncology Group. Am J Clin Oncol.1982 Dec;5(6):649-655. PMID: 7165009. Olayioye MA et al.; EMBO J (2000) Vol 19: pp 3159-3167). Ramalingam S.S. et al. Mechanisms of acquired resistance to first-line osimertinib: Preliminary data from the phase III FLAURA study. ESMO: NSCLC, Metastatic. 2018; 29:8, VIII740. Robertson SC, Tynan J, Donoghue DJ. RTK mutations and human syndromes: when good receptors turn bad. Trends Genet 2000;16:368. Rosell, R. et al. Screening for epidermal growth factor receptor mutations in lung cancer. N. Engl. J. Med. 2009; 36:958–967. Siegel RL et al. Cancer statistics, 2021. CA Cancer J Clin.2021;71(1):7–33. Sruthi CK, Prakash M. PLoS One.2020;15(1):e0227621. Suzawa et al., DOI: 10.1200 / PO.19.00011 JCO Precision Oncology - May 10, Vol 3, 2019. Tabasinezhad M. et al. Immunol Lett. 2019;212:106-113. Testa U et al. Lung cancers: molecular characterization, clonal heterogeneity and evolution, and cancer stem cells. Cancers (Basel). 2018;10(8):248. West H., McCleod M., Hussein M., Morabito A., Rittmeyer A., Conter H. J., et al. (2019). Atezolizumab in combination with carboplatin plus nab-paclitaxel chemotherapy compared with chemotherapy alone as first-line treatment for metastatic non- squamous non-small-cell lung cancer: A multicentre, randomised, open-label, phase 3 trial. Lancet. Oncol.20 (7), 924–937. 10.1016 / S1470-2045(19)30167-6. Yarden Y. The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities. Eur J Cancer 2001;37 (Suppl 4):S3–S8. Zhang, X., Zhu, W., Zhang, J., Huo, S., Zhou, L., Gu, Z., Zhang, M. MicroRNA-650 targets ING4 to promote gastric cancer tumorigenicity. Biochem. Biophys. Res. Commun.395: 275-280, 2010. Name INN name Epitope MOA5D5 MetMAb Sema Domain HGF block13.3.2 224G11 HGF block, C8-H241 LY-2875358internalization R13 13-METTable 2. Reference antibodies with reported specificities against cMET extracellular domains. Competition of phages with reference antibodies MF tested no IgG 13.3.2 5D5 R13 224G11 C8H241 R284040 1.915 1.818 0.066 1.608 1.907 1.979 1.7874297 1.769 0.072 1.499 1.332 1.955 1.031 1.8854356 2.380 2.541 0.088 2.231 2.170 1.806 1.82513.3.2 2.172 0.311 1.934 1.988 2.221 1.893 2.1295D5 1.868 1.773 0.164 1.660 2.025 2.054 2.035R13 1.693 1.590 1.549 0.090 1.878 0.078 1.794Table 3. Competition of cMet reference antibodies with cMET cLC antibodies. Shown are OD450 values. OD450 values indicate the existence or lack of competition with the stated antibody. MF4506 was not tested. PBs MF's PBs EGFR cMET PB7678 MF4280 EGYYETTTYYYNLFDS MF4298 KLEPTGYYYYYMDV PB7679 MF3755 ERFLEWLHFDY MF4487 KTSRYSGYHYYMDV PB7686 MF3755 ERFLEWLHFDY MF4507 AHYDILTG PB8021 MF3755 ERFLEWLHFDY MF3462 GKSHYSWDAFDY PB8218 MF3752 DRNWGWDFDY MF4040 GTYYYGSGSFSTRVFDAFDV PB8244 MF3755 ERFLEWLHFDY MF4044 QSRRYSGYASYFDY PB8292 MF3755 ERFLEWLHFDY MF4130 QRRAYSGYNWYFDL PB8301 MF4280 EGYYETTTYYYNLFDS MF4130 QRRAYSGYNWYFDL PB8316 MF3755 ERFLEWLHFDY MF4293 RNDFWSGYLFDY PB8339 MF3752 DRNWGWDFDY MF4294 KTTVGYYYYYMDV PB8340 MF3755 ERFLEWLHFDY MF4294 KTTVGYYYYYMDV PB8364 MF3755 ERFLEWLHFDY MF4296 GPELGYYYYYMDI PB8388 MF3755 ERFLEWLHFDY MF4297 ASSMITFGGVIVSWFDP PB8511 MF3755 ERFLEWLHFDY MF4301 RVNRYSGYATYFDL PB8532 MF3370 DRHWHWWLDAFDY MF4356 ETYYYDRGGYPFDP PB8535 MF3755 ERFLEWLHFDY MF4356 ETYYYDRGGYPFDP PB8545 MF4281 GDLFITGTLDY MF4356 ETYYYDRGGYPFDP PB8582 MF3752 DRNWGWDFDY MF4491 RTSRYSGYHYYLDV PB8583 MF3755 ERFLEWLHFDY MF4491 RTSRYSGYHYYLDV PB8607 MF3755 ERFLEWLHFDY MF4505 LLYDLFDL PB8639 MF3752 DRNWGWDFDY MF4506 SIDMATITDAFDI PB8640 MF3755 ERFLEWLHFDY MF4506 SIDMATITDAFDI PB8687 MF3752 DRNWGWDFDY MF4508 GTTGNPYYFYYYMDV PB8688 MF3755 ERFLEWLHFDY MF4508 GTTGNPYYFYYYMDV Table 4. List of the 24 cMETxEGFR bispecifics antibodies selected after dose dependent titration experiments in a N87 HGF / EGF proliferation assay. The MF number of the EGFR and cMET arms in each individual PB as well as the their HCDR3 sequence are indicated.

[0002] PBs MF's N87 proliferation assays PBs HGF / EGFR cMET HGF EGF EGF PB7678 MF4280 MF4298 + + + PB7679 MF3755 MF4487 ++ - ++ PB7686 MF3755 MF4507 ++ + + PB8021 MF3755 MF3462 + + + PB8218 MF3752 MF4040 ++ +++ + PB8244 MF3755 MF4044 ++ + ++ PB8292 MF3755 MF4130 ++ + ++ PB8301 MF4280 MF4130 + ++ + PB8316 MF3755 MF4293 ++ + + PB8339 MF3752 MF4294 + + + PB8340 MF3755 MF4294 ++ + ++ PB8364 MF3755 MF4296 ++ + ++ PB8388 MF3755 MF4297 ++ +++ ++ PB8511 MF3755 MF4301 ++ +++ ++ PB8532 MF3370 MF4356 + +++ + PB8535 MF3755 MF4356 ++ +++ ++ PB8545 MF4281 MF4356 + +++ + PB8582 MF3752 MF4491 + - + PB8583 MF3755 MF4491 ++ +++ ++ PB8607 MF3755 MF4505 ++ - ++ PB8639 MF3752 MF4506 + +++ + PB8640 MF3755 MF4506 ++ +++ ++ PB8687 MF3752 MF4508 + ++ + PB8688 MF3755 MF4508 + - + Table 5. Summary of the antibody titration experiments done using N87 HGF / EGF, HGF and EGF proliferation assays with the 24 cMETxEGFR bispecific antibodies. Bispecifics are indicated as PBXXXX and the different Fab arms with MGXXXX. The activity of the bispecifics in the individual assays is indicated as: - no effect; + inhibition of proliferation lower than positive control; ++ = inhibition of proliferation comparable to positive control antibody 5D5 Fab; +++ = Inhibition of proliferation higher than positive control antibody 5D5 Fab.

[0003] BispecificEGFR arm EGFRcMET Cross antibody blocking arm reference compared antibody to cetux blocking (based on IC50) PB8535 MF3755 100% MF4356 5D5PB8640 MF3755 100% MF4506 NDPB8388 MF3755 100% MF4297 13.3.2PB8218 MF3752 80% MF4040 5D5PB8532 MF3370 80% MF4356 5D5Table 6. Composition of the most potent EGFRxcMET bispecific antibodies and their competition with reference antibodies. Bispecific antibody cMET arm EGFR arm ADCC enhanced Cetuximab - - - PB8532p05 MF4356 MF3370 No PB19474p01 MF4356 MF8232 Yes PB19475p01 MF4356 MF8233 Yes PB19476p01 MF8230 MF3370 Yes PB19477p01 MF8230 MF8232 Yes PB19478p01 MF8230 MF8233 Yes PB8532p06 MF4356 MF3370 Yes PB8532p04 MF4356 MF3370 No HER-3 arm EGFR arm PB4522p34 MF3178 MF4280 Yes PB4522p25 MF3178 MF4280 No TT arm TT arm PG1337p218 MF1337 MF1337 No Table 7. Composition of bispecific antibodies. The pXX number indicates the number of the production run and can be used to identify whether the antibody was produced in an ADCC version or not.

Claims

Claims 1. A bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in a method of treatment of a cancer in a subject.

2. A method of treating a subject having a cancer, said treatment comprising administering to the subject an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and comprising an effective amount of a chemotherapeutic agent to said subject.

3. The use or method of any one of the preceding claims, wherein said chemotherapeutic agent is or comprises a platinum-based compound and / or a taxane.

4. The use or method of any one of the preceding claims, wherein said chemotherapeutic agent is or comprises paclitaxel and / or carboplatin.

5. The use or method of any one of the preceding claims, wherein said chemotherapeutic agent is or comprises docetaxel.

6. The use or method of any one of the preceding claims, wherein said cancer is an advanced or a metastatic cancer.

7. The use or method of any one of the preceding claims, wherein said cancer is lung cancer, in particular non-small cell lung cancer. 8 The use or method of any one of the preceding claims, wherein said cancer is resistant to treatment with a third generation EGFR tyrosine kinase inhibitor, such as osimertinib.

9. The use or method of claim 8, wherein said cancer has not been previously treated with a chemotherapeutic agent.

10. The use or method of claim 8, wherein said cancer is resistant to treatment with a platinum-based chemotherapy 11. The use or method according to any one of claims 8-10, wherein said third- generation EGFR tyrosine kinase inhibitor comprises or is osimertinib, lazertinib, alflutinib, rezivertinib, olmutinib, almonertinib, abivertinib, ASK120067, befotertinib, rociletinib, oritinib (SH-1028), nazartinib (EGF816), naquotinib (ASP8273), furmonertinib, mavelertinib (PF-0647775), olafertinib (CK-101), keynatinib or ES-072.

12. The use or method according to any one of claims 8-11, wherein said third- generation EGFR tyrosine kinase inhibitor comprises or is osimertinib.

13. The use or method of any one of the preceding claims, wherein said bispecific antibody is administered in an amount of 1500 mg or 2000 mg once every two weeks.

14. The use or method of any one of the preceding claims, wherein paclitaxel is administered in an amount of between 100 and 200 mg / m2body surface and carboplatin at AUC 3, AUC 4 or AUC 5 once every three weeks.

15. The use or method of any one of the preceding claims, wherein docetaxel is administered in an amount of between 40 and 75 mg / m2body surface once every two weeks.

16. The use or method of any one of the preceding claims, wherein said cancer is an EGFR positive and / or cMET positive cancer.

17. The use or method of any one of the preceding claims, wherein said cancer comprises an EGFR-dependent resistance and / or cMET-dependent resistance.

18. The use or method according to any one of the preceding claims, wherein said cancer comprises an acquired tyrosine kinase inhibitor resistance mutation such as a mutation which confers resistance to a third generation TKI, such as osimertinib.

19. The use or method according to any one of the preceding claims, wherein the treatment comprises administering said bispecific antibody and said chemotherapeutic agent to a subject in need thereof, wherein said bispecific antibody is administered simultaneously, sequentially or separately with said chemotherapeutic agent.

20. The use or method according to any one of the preceding claims, wherein the subject is a human subject.

21. A product comprising a chemotherapeutic agent and a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET).

22. A pharmaceutical composition comprising a chemotherapeutic agent and instructions for the use of said chemotherapeutic agent with a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) in the treatment of cancer.

23. A pharmaceutical composition comprising a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growthfactor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and instructions for the use of said bispecific antibody with a chemotherapeutic agent in the treatment of cancer.

24. The use, method, product or pharmaceutical composition according to any one of the preceding claims, wherein the antibody is a human antibody.

25. The use, method, product or pharmaceutical composition according to any one of the preceding claims, wherein the antibody is ADCC enhanced.

26. The use, method, product or pharmaceutical composition according to any one of the preceding claims, wherein the antibody is an IgG1 format antibody having an anti- EGFR, anti-cMET stoichiometry of 1:

1.

27. The use, method, product or pharmaceutical composition according to any one of the preceding claims, wherein the antibody has one variable domain that can bind EGFR and one variable domain that can bind cMET.

28. The use, method, product or pharmaceutical composition according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYX1X2NTNYAQKLQG and a CDR3 comprising the sequence X3X4X5X6HWWLX7AFDY, wherein X1 = N or S; X2 = A or G; X3 = D or G; X4 = R, S or Y; X5 = H, L or Y; X6 = D or W and X7 = D or G; with 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof at a position other than X1- X7 and wherein the second variable domain comprises a heavy chain variable region with the amino acid sequence of one of the sequences of SEQ ID NO: 1-23 with 0-10 preferably 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof.

29. The use, method, product or pharmaceutical composition according to claim 28, wherein X1 = N; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = A; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = S; X2 = G; X3 = D; X4 = S; X5 = Y; X6 = W and X7 = G; X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; X1 = N; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; X1 = N; X2 = A; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G; or X1 = S; X2 = G; X3 = G; X4 = Y; X5 = L; X6 = D and X7 = G 30. The use, method or pharmaceutical combination according to claim 28 or 29, wherein X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = N; X2 = A;X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = S; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D.

31. The use, method or pharmaceutical combination according to any one of claims 28-30, wherein X1 = N; X2 = G; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D; or X1 = N; X2 = A; X3 = D; X4 = R; X5 = H; X6 = W and X7 = D.

32. The use, method or pharmaceutical combination according to any one of claims 28-31, wherein the heavy chain variable region of the second variable domain comprises the amino acid sequence of one of the sequences of SEQ ID NO: 1-3; 7; 8; 10; 13; 15; 16; 17; 21; 22 or 23 with 0-10 preferably 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof.

33. The use, method or pharmaceutical combination according to any one of claims 28-32, wherein the heavy chain variable region of the second variable domain comprises the amino acid sequence of one of the sequences of SEQ ID NO: 2; 7; 8; 10; 13 or 23 with 0-10 preferably 0-5 amino acid insertions, deletions, substitutions, additions or a combination thereof.

34. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP.

35. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY and wherein the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP.

36. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first and second variable domain comprise a light chain with a CDR1, CDR2 and CDR3 amino acid sequence of QSISSY, AAS, and QQSYSTP, respectively.

37. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNGNTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, the second variable domain comprises a heavy chain variable region with a CDR1 sequence SYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 sequence ETYYYDRGGYPFDP, andwherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin.

38. The use, method or pharmaceutical combination according to any one of the preceding claims, wherein the first variable domain comprises a heavy chain variable region with a CDR1 sequence SYGIS; a CDR2 sequence WISAYNANTNYAQKLQG and a CDR3 comprising the sequence DRHWHWWLDAFDY, the second variable domain comprises a heavy chain variable region with a CDR1 sequence TYSMN; a CDR2 sequence WINTYTGDPTYAQGFTG and a CDR3 comprising the sequence ETYFYDRGGYPFDP, and wherein the first and second variable domain comprise a common light chain having a CDR1 sequence QSISSY, a CDR2 sequence AAS and a CDR3 sequence QQSYSTPPT and wherein said chemotherapeutic agent is or comprises paclitaxel and carboplatin.

39. A method of treating cancer in a subject, comprising - identifying a subject as having an acquired tyrosine kinase inhibitor resistance, such as to osimertinib, and - administering to the subject a therapeutically effective amount of said bispecific antibody and a chemotherapeutic agent, thereby treating the cancer in the subject.

40. A bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and a chemotherapeutic agent for use in the treatment of cancer in a subject, comprising - providing a sample from the cancer of said subject, and - determining the presence or absence of an acquired tyrosine kinase inhibitor resistance in the sample, wherein if the sample is determined to comprise the presence of said acquired tyrosine kinase inhibitor resistance, said subject is administered a therapeutically effective amount of said bispecific antibody and of said chemotherapeutic agent, thereby treating the cancer in the subject.

41. A method of treating a subject from having cancer, comprising - providing a sample from the cancer of said subject, and - determining the presence or absence of an acquired tyrosine kinase inhibitor resistance in the sample, wherein if the sample is determined to comprise the presence of said resistance, said subject is administered an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent, thereby treating the cancer in the subject.

42. A method of treating cancer in a subject identified as having an acquired tyrosine kinase inhibitor resistance, such as to osimertinib, comprising administering to thesubject an effective amount of a bispecific antibody that comprises a first variable domain that can bind an extracellular part of human epidermal growth factor receptor (EGFR) and a second variable domain that can bind an extracellular part of human MET Proto-Oncogene, Receptor Tyrosine Kinase (cMET) and an effective amount of a chemotherapeutic agent, thereby treating the cancer in the subject.