Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein, CF

Measured by its binding ability in a functional ELISA. When Recombinant Human HGF (NS0-expressed) Protein (11352-HG) is immobilized at 0.250 μg/mL (100 μL/well), Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein (Catalog # 11267-ME) binds with an ED50 of 2.50-25.0 ng/mL.

2 μg/lane of Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein (Catalog # 11267-ME) was resolved with SDS-PAGE and visualized by Coomassie® Blue staining, showing bands at 135-150 kDa, 40-45 kDa, and 103-115 kDa under reducing (R) conditions and a single band at 270-310 kDa under non-reducing (NR) conditions.

• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human HGF (NS0-expressed) Protein (Catalog # 11352-HG) is immobilized at 0.250 μg/mL (100 μL/well), Recombinant Cynomolgus Monkey HGFR/c-MET Fc Chimera (Catalog # 11267-ME) binds with an ED₅₀ of 2.50-25.0 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived cynomolgus monkey HGFR/c-MET protein
  

  Cynomolgus HGFR/c-MET (Glu25-Thr932) Accession # EHH52447.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: EHH52447.1
• N-terminal Sequence: Glu25 ( alpha chain) & Ser308 ( beta chain)
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 128 kDa, 33 kDa ( alpha chain), and 96 kDa ( beta chain).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 135-150 kDa, 40-45 kDa, and 103-115 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Cynomolgus HGFR/c-MET Fc Chimera Protein, CF

• 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

Background

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. Based on the high homology (98%) between cynomolgus and human HGF R, cynomolgus HGF R is predicted to be 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 alternative 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, 7). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (8, 9). HGF stimulation induces HGF R down-regulation via internalization and proteasome-dependent degradation (10). In the absence of ligand, HGF R forms noncovalent 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 (11-18). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (11 - 18). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (11, 15, 16). 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 (19). 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% aa sequence identity with canine, mouse, and rat HGF R.

1. Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915.
2. Grzelakowska-Sztabert, B. and M. Dudkowska (2011) Growth Factors 29:105.
3. Gherardi, E. et al. (2003 ) Proc. Natl. Acad. Sci. 100:12039.
4. Park, M. et al. (1987) Proc. Natl. Acad. Sci. 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.

Bioinformatics

• Uniprot:
  • EHH52447.1()