Anti-c-Met Antibody, clone seeMet 13 clone seeMet 13, from mouse

Hepatocyte growth factor receptor (EC 2.7.10.1; UniProt P08581; also known as HGF receptor, HGF/SF receptor, Proto-oncogene c-Met, Scatter factor receptor, SF receptor, Tyrosine-protein kinase Met) is encoded by the MET (also known as AUTS9, HCC, RCCP) gene (Gene ID 4233) in human. HGF receptor or c-Met is initially produced as a 1390-a.a. precursor protein with an N-terminal signal peptide, postranslational proteolytic cleavage yields the mature tyrosine kinase receptor composed of an extracellular alpha chain (a.a. 25-307) linked via a disulfide bond to a transmembrane beta chain with an extracellular domain (a.a. 308-932), transmembrane helix (a.a. 933-955), and a cytoplasmic domain (a.a. 956-1390). The alpha-chain and the extracellular portion of beta-chain form the Sema domain that mediates receptor dimerization and ligand binding. The cytoplasmic portion of beta-chain contains the kinase domain (a.a. 1078-1345) and a C-terminal tail that contains a docking region (a.a. 1212-1390) for effector and adapter proteins essential for downstream signaling. Hepatocyte growth factor (HGF) is the only known c-Met ligand. HGF binding induces c-Met dimerization and autophosphorylation on Y1230, Y1234 and Y1235, leading to a conformation change and further phosphorylation on Y1349 and Y1356, making C-terminal tail docking region available for adaptor and signalling molecules. c-Met mediates a wide-range of biological activities, including cell proliferation, motility, angiogenesis and morphogenesis, and is an attractive target for cancer therapy. Aberrant c-Met activation/signalling promotes cancer cell proliferation and is associated with poor prognosis in various human cancers. Upregulated c-Met expression is also known to cause resistance against HER2, EGFR and B-RAF inhibitory drugs in cancer treatment.