BACKGROUND The c-Met proto-oncogene, widely expressed in mammalian tissues, encodes a transmembrane receptor with tyrosine kinase activity. The c-Met receptor tyrosine kinase and its ligand HGF (hepatocyte growth factor), also known as scatter factor (SF), have been shown to be involved in angiogenesis, cellular motility, growth, invasion, and differentiation. The full receptor protein is a 190-kDa heterodimer made of a 50-kDa extracellular alpha-subunit linked by a disulfide bridge to a 145-kDa transmembraneous catalytic beta-subunit.1 Multiple signaling pathways have been associated with the biological responses mediated by c-Met activation. In response to HGF, phosphorylated tyrosine residues of c-met act as a binding site for Src Homology (SH2) domain-containing intracellular proteins including Gab-1, Grb2 etc.2, which led to downstream activation of Ras, Rac, phosphoinositide 3-kinase (PI3-kinase) and mitogen-activated protein kinase (MAPK).2 It was demonstrated that c-Met signaling also contributes to oncogenesis and tumor progression in several human cancers and promotes aggressive cellular invasiveness that is strongly linked to tumor metastasis. Thus, c-Met is a potentially therapeutic target for cancer treatment.3
1. Abounader, A et al: J. Neurochem. 76 : 1497, 2001.
2. Sachs, M. et al: J. Cell. Biol. 150:1375, 2000.
3. Perruzi, B. & Bottaro, D.: Clin. Can. Res. 12: 3657, 2006
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E. coli-expressed cytoplasmic carboxyl domain of human c-Met proteins.
Species & predicted
reactivity ( ):
Human, Mouse, Rat
Weight of protein:
Detects endogenous levels of c-Met beta subunits
Store at -20°C, 4°C for frequent use. Avoid repeated freeze-thaw cycles.
*Optimal working dilutions must be determined by end user.