Recombinant Cynomolgus HGFR/c-MET His-tag Protein, CF

Catalog # Availability Size / Price Qty
11390-ME-100
Recombinant Cynomolgus Monkey HGFR/c-MET His-tag Protein Binding Activity.
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Recombinant Cynomolgus HGFR/c-MET His-tag Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. Recombinant Cynomolgus Monkey HGFR/c-MET His-tag (Catalog # 11390-ME) binds to Recombinant Human HGF (NS0-expressed) Protein (Catalog # 294-HGN) with a ED50 of <0.400 μg/mL.
Source
Human embryonic kidney cell, HEK293-derived cynomolgus monkey HGFR/c-MET protein
Alpha Chain Glu25-Arg307 & Beta Chain Ser308-Thr932
Accession #
N-terminal Sequence
Analysis
Glu25 & Ser308
Predicted Molecular Mass
33 kDa & 70 kDa
SDS-PAGE
41-46 kDa (alpha chain) & 76-84 kDa (beta chain) under reducing conditions.

Product Datasheets

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11390-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.

11390-ME

Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Reconstitution Reconstitute at 200 μg/mL in PBS.
Shipping The product is shipped with polar packs. 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.

Scientific Data

Binding Activity View Larger

Measured by its binding ability in a functional ELISA. Recombinant Cynomolgus Monkey HGFR/c-MET His-tag Protein (Catalog # 11390-ME) binds to Recombinant Human HGF (NS0-expressed) Protein (294-HGN) with a ED50 of <0.400 μg/mL.

SDS-PAGE View Larger

2 μg/lane of Recombinant Cynomolgus Monkey HGFR/c-MET His-tag Protein (Catalog # 11390-ME) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 41-46 kDa (alpha chain) & 76-84 kDa (beta chain) under reducing conditions and a single band at 110-130 kDa under non-reducing (NR) conditions.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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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. 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, cynomolgus HGF R shares 98% aa sequence identity with human HGF R.

References
  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.
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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