The c-Met receptor, also called hepatocyte growth factor receptor (HGFR), is a member of the receptor tyrosine kinase family. It consists of an extracellular ligand-binding domain and an intracellular kinase domain. The receptor is activated by ligand binding followed by dimerization and phosphorylation within the intracellular kinase domains. Structurally, the extracellular domain is composed of a semaphorin (sema) domain, a cysteine-rich hinge known as plexin, semaphorin and integrin (PSI) domain followed by four immunoglobulin-like domains. In humans, HGF is the only known activating ligand of c-Met that induces cellular responses such as cell proliferation, cell survival, cell motility and invasion. In healthy tissues, c-Met signaling is implicated in embryonic development, wound healing and liver regeneration. In human malignancies, c-Met can be deregulated by protein overexpression, gene amplification, somatic or germline mutations or the production of HGF-dependent autocrine loops.
Anti-Human Met (D1C2)-167Er—25 µg