• Species Reactivity

  Human

• Specificity

  Detects human HGF R/c-MET.

• Source

  Monoclonal Mouse IgG    ₁ Clone # 95106

• Purification

  Protein A or G purified from hybridoma culture supernatant

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant human HGF R/c-MET    
  Glu25-Thr932    
  Accession # P08581

• Formulation

  Supplied in a saline solution containing BSA and Sodium Azide.

• Label

  Alexa Fluor 700

Applications

• 
  

  Recommended    
  Concentration

  Sample

• Flow Cytometry

  5 μL/10    ⁶ cells

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Shipping

  The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

• Stability & Storage

  Protect from light.    Do not freeze.    

• 12 months from date of receipt, 2 to 8 °C as supplied.

Background: HGF R/c-MET

HGF R, also known as Met (from N-methyl-N’-nitro-N-nitrosoguanidine induced), is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. This generates a mature HGF R that is a disulfide-linked dimer composed of a 50 kDa extracellular alpha chain and a 145 kDa transmembrane beta chain (1, 2). The extracellular domain (ECD) contains a seven bladed beta -propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain (3, 4). Proteolysis and alternate splicing generate additional forms of human HGF R which either lack of the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the alpha and beta chains (5-7). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 8). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (9, 10). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (11). In the absence of ligand, HGF R forms non-covalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, Integrin alpha 6/ beta 4, Plexins B1, 2, 3, and MSP R/Ron (12-19). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (12-19). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (12, 16, 17). Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells (20). Genetic polymorphisms, chromosomal translocation, over-expression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, human HGF R shares 86-88% amino acid sequence identity with canine, mouse, and rat HGF R.

• References:

1. Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915.

2. Corso, S. et al. (2005) Trends Mol. Med. 11:284.

3. Gherardi, E. et al. (2003) Proc. Natl. Acad. Sci. USA 100:12039.

4. Park, M. et al. (1987) Proc. Natl. Acad. Sci. USA 84:6379.

5. Crepaldi, T. et al. (1994) J. Biol. Chem. 269:1750.

6. Prat, M. et al. (1991) Mol. Cell. Biol. 12:5954.

7. Rodrigues, G.A. et al. (1991) Mol. Cell. Biol. 11:2962.

8. Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.

9. Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.

10. Ponzetto, C. et al. (1994) Cell 77:261.

11. Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.

12. Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.

13. Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.

14. Jo, M. et al. (2000) J. Biol. Chem. 275:8806.

15. Wang, X. et al. (2002) Mol. Cell 9:411.

16. Trusolino, L. et al. (2001) Cell 107:643.

17. Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.

18. Conrotto, P. et al. (2004) Oncogene 23:5131.

19. Follenzi, A. et al. (2000) Oncogene 19:3041.

20. Sonnenberg, E. et al. (1993) J. Cell Biol. 123:223.

• Long Name:

  Hepatocyte Growth Factor Receptor

• Entrez Gene IDs:

  4233 (Human); 17295 (Mouse)

• Alternate Names:

  AUTS9; cMET; c-MET; EC 2.7.10; EC 2.7.10.1; hepatocyte growth factor receptor; HGF R; HGF receptor; HGF/SF receptor; HGFR; Met (c-Met); met proto-oncogene (hepatocyte growth factor receptor); met proto-oncogene tyrosine kinase; MET; oncogene MET; Proto-oncogene c-Met; RCCP2; Scatter factor receptor; SF receptor; Tyrosine-protein kinase Met