||A synthetic phospho-peptide corresponding to residues surrounding Tyr1234/Tyr1235 of human phospho Met
||Predicted to work with mouse, rat and other homologues.
||1X PBS, 0.02% NaN3, 50% Glycerol, 0.1% BSA
||1.0 - 0.1 µg/ml. Optimum concentration should be determined by the user.
The Mesenchymal Epithelial Transition (MET) receptor belongs to a family of receptor tyrosine kinases (RTKs). Dyregulation of the MET signaling pathway occurs in wide range of human tumors (1,2). The MET receptor is a glycoprotein heterodimer consisting of an extracellular α-subunit linked to transmembrane β-subunit by a disulfide bond (3). The MET receptor is widely expressed on the surface of epithelial and endothelial cells. MET ligand is known as the hepatocyte growth factor (HGF), also called the scatter factor (SF). HGF/SF is a serine protease and produced in cells of mesenchymal origin. HGF is secreted as a s ingle chain, biologically inactive protein which is further processed into its mature form by a cleavage process catalyzed by extracellular proteases (4-6). MET and its ligand HGF are involved in several normal and pathological processes, such as fetal liver, placenta and muscle development, as well as development of the nervous system (7-9). MET signal transduction is involved in tumor growth, invasion, resistance to therapy, angiogenesis and specially in the generation and maintenance of cancer stem cells (CSCs) (10-12).
Upon HGF binding, the MET receptor at the plasma membrane forms a stable dimer of two molecules of MET which leads to subsequent activation and trans-phosphorylation of the two tyrosine residues in the catalytical regions Y1234 and Y1235, followed by trans-phosphorylation of two docking tyrosines (Y1349 and Y1356) in the carboxy-terminal site. These phosphorylations enable MET to bind to multiple substrates and activate a variety of signaling pathways including MAPK, PI3K-AKT cascades, STAT and NF-κB (13-15).
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8. Uehara Y, et al., (1995) Nature 373:702–5.
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10. Zhang Y, et al., (2105) Agents for Cancer Treatment Biomedicines. 3:149–181.
11. Bussolino F, et al., (1992) J. Cell Biol. 119:629–41.
12. Boccaccio C, and Comoglio PM. (2014) Curr. Opin. Cell Biol. 31:98–105.
13. Ponzetto C, et al., (1994) Cell 77:261–71.
14. Johnson GL, and Lapadat R. (2002) Science. 298:1911–2.
15. Muller M, ett al., (2002) Mol. Cell Biol. 22:1060–72.
This product was added to our catalog on Sunday 04 December, 2016.