c-Met antibody

Hepatocyte growth factor receptor (HGF R), a product of the proto-oncogene c-Met, is a heterodimeric transmembrane glycoprotein that is a receptor-type tyrosine kinase. The c-Met heterodimer is composed of an alpha chain that is disulfide-linked to a beta chain. Each alpha and beta subunit heterodimer contain 1152 amino acid residues with a calculated molecular mass of approximately 129 kDa. The alpha chain is exposed to the cell surface and the beta chain spans the plasma membrane. c-Met is synthesized as a single-chain precursor which undergoes cotranslational glycosylation and proteolytic cleavage producing the heterodimeric mature form. Human and mouse HGF receptors share 89% amino acid identity. HGF is the ligand for the HGF receptor. Human HGF can bind to the mouse HGF receptor.Hepatocyte growth factor (HGF), also known as scatter factor (SF), is a multifunctional cytokine that promotes mitogenesis, migration, invasion, and morphogenesis. HGF stimulates hepatocytes and other epithelial and endothelial cells by various biological actions. HGF binding involves the beta chain of the HGF receptor, but alpha chain participation cannot be ruled out. HGF binding to c-Met triggers dimerization and subsequent tyrosine autophosphorylation of the receptor beta chain. Autophophorylation at two tyrosines upregulates kinase activity while phosphorylation at two other tyrosines generates SH2 docking sites for adapter proteins such as Shc, Grb2, CrK/CRKL, and Gab1. Receptor activation has been correlated to the activation of the Ras pathway, which culminates in the activation and consequent nuclear translocation of MAP kinase. c-Met can also be negatively modulated by phosphorylation of Ser 985 by protein kinase C. Other ligand-receptor activities involve binding that leads to enhanced integrin-mediated B cell and lymphoma cell adhesion. Normal HGF-Met signaling is needed for embryonic development and abnormal signaling and has been implicated in tumorigenesis.