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

R&D Systems, part of Bio-Techne | Catalog # 7065-ME

R&D Systems, part of Bio-Techne
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7065-ME-100
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Key Product Details

Source

NS0

Accession #

P16056

Conjugate

Unconjugated

Applications

Bioactivity

View all HGFR/c-MET Proteins and Enzymes »

Product Specifications

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

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.

N-terminal Sequence Analysis

Glu25 & Ser307

Predicted Molecular Mass

96 & 32 kDa (monomer)

SDS-PAGE

110-120 kDa & 40-43 kDa, reducing conditions

Activity

Measured by its ability to bind recombinant mouse HGF in a functional ELISA with an estimated KD <0.2 nM.

Formulation, Preparation and Storage

7065-ME
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 200 μg/mL in PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.

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  alpha6/ beta4, 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

    Alternate Names

    c-MET, cMET, HGF R, MET

    Entrez Gene IDs

    4233 (Human); 17295 (Mouse); 102123512 (Cynomolgus Monkey)

    Gene Symbol

    MET

    UniProt

    P16056

    Additional HGFR/c-MET Products

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

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    For research use only

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