Recombinant Mouse HGFR/c-MET Fc Chimera (NS0-expressed), CF

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7065-ME-100
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Mouse HGFR/c-MET Fc Chimera (NS0-expressed), CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to bind recombinant mouse HGF in a functional ELISA with an estimated KD <0.2 nM.
Source
Mouse myeloma cell line, NS0-derived mouse HGF R/c-MET protein
Mouse HGF R/c-Met
(Met1 - Asn929)
Accession # P16056
DIEGRMDP Mouse IgG2A
(Glu98 - Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Glu25 & Ser307
Predicted Molecular Mass
96 & 32 kDa (monomer)
SDS-PAGE
110-120 kDa & 40-43 kDa, reducing conditions

Product Datasheets

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7065-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.

7065-ME

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
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.
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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 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). An alternately spliced form of mouse HGF R lacks a cytoplasmic juxtamembrane region important for regulation of signal transduction (5, 6). 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 downregulation 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, overexpression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, mouse HGF R shares 87%, 87%, and 94% amino acid sequence identity with canine, human, and rat HGF R, respectively.

References
  1. Birchmeier, C. et al. (2003) Nat. Rev. Mol. Cell Biol. 4:915.
  2. Grzelakowska-Sztabert, B. and M. Dudkowska (2011) Growth Factors June 2 epub.
  3. Gherardi, E. et al. (2003) Proc. Natl. Acad. Sci. 100:12039.
  4. Chan, A.M. et al. (1988) Oncogene 2:593.
  5. Lee, C.-C. and K.M. Yamada (1994) J. Biol. Chem. 269:19457.
  6. Lee, C.-C. et al. (1995) J. Biol. Chem. 270:507.
  7. Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.
  8. Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.
  9. Ponzetto, C. et al. (1994) Cell 77:261.
  10. Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.
  11. Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.
  12. Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.
  13. Jo, M. et al. (2000) J. Biol. Chem. 275:8806.
  14. Wang, X. et al. (2002) Mol. Cell 9:411.
  15. Trusolino, L. et al. (2001) Cell 107:643.
  16. Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.
  17. Conrotto, P. et al. (2004) Oncogene 23:5131.
  18. Follenzi, A. et al. (2000) Oncogene 19:3041.
  19. 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

    Citation for Recombinant Mouse HGFR/c-MET Fc Chimera (NS0-expressed), CF

    R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

    1 Citation: Showing 1 - 1

    1. A pilot study on nitration/dysfunction of NK1 segment of myogenic stem cell activator HGF
      Authors: A Elgaabari, N Imatomi, H Kido, M Seki, S Tanaka, Y Matsuyoshi, T Nakashima, S Sawano, W Mizunoya, T Suzuki, M Nakamura, JE Anderson, R Tatsumi
      Biochemistry and Biophysics Reports, 2022-06-11;31(0):101295.
      Species: Rat
      Sample Types: Whole Cells
      Applications: Bioassay

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