Recombinant Canine HGFR/c-MET Protein, CF

• Reactivity: Ca
• Applications: Binding Activity
• Format: Carrier-Free

Recombinant Canine HGFR/c-MET Protein, CF Summary

• Details of Functionality: Measured by its ability to bind rcaHGF with an estimated K_D <0.8 nM.
• Source: Mouse myeloma cell line, NS0-derived canine HGF R/c-MET protein
  Glu25-Arg308 ( alpha chain) & Ser309-Leu935 ( beta chain), with a C-terminal 6-His tag
• Accession #: Q75ZY9
• N-terminal Sequence: Glu25 ( alpha chain) & Ser309 ( beta chain)
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Binding Activity
• Theoretical MW: 32.6 kDa ( alpha chain) and 70.1 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: 90 -100 kDa and 42-47 kDa, 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.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Canine HGFR/c-MET 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. HGF R is synthesized as a single chain precursor which undergoes posttranslational 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 region, and four Ig-like E-set domains, while the cytoplasmic region includes a tyrosine kinase domain (3). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 4). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (5, 6). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (7). 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, B2, and B3, and MSP R/Ron (8 - 15). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (8 - 15). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (8, 12, 13). HGF released from neighboring mesenchymal cells stimulates HGF R on undifferentiated epithelium and induces epithelial cell scattering and branching tubulogenesis (16). Genetic polymorphisms, chromosomal translocation, overexpression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, canine HGF R shares 85% - 88% amino acid sequence identity with human, mouse and rat HGF R.

 

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. Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.
5. Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.
6. Ponzetto, C. et al. (1994) Cell 77:261.
7. Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.
8. Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.
9. Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.
10. Jo, M. et al. (2000) J. Biol. Chem. 275:8806.
11. Wang, X. et al. (2002) Mol. Cell 9:411.
12. Trusolino, L. et al. (2001) Cell 107:643.
13. Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.
14. Conrotto, P. et al. (2004) Oncogene 23:5131.
15. Follenzi, A. et al. (2000) Oncogene 19:3041.
16. Sonnenberg, E. et al. (1993) J. Cell Biol. 123:223.

Bioinformatics

• Uniprot:
  • Q75ZY9()