Recombinant Canine HGFR/c-MET Protein, CF

Catalog # Availability Size / Price Qty
4140-ME-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Canine HGFR/c-MET Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to bind rcaHGF with an estimated KD <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 #
N-terminal Sequence
Analysis
Glu25 ( alpha chain) & Ser309 ( beta chain)
Predicted Molecular Mass
32.6 kDa ( alpha chain) and 70.1 kDa ( beta chain)
SDS-PAGE
90 -100 kDa and 42-47 kDa, reducing conditions

Product Datasheets

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4140-ME

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

4140-ME

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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Background: HGFR/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 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.

 

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. 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.
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

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