Recombinant Human HGFR/c-MET Fc Chimera Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 8614-MT

(HEK293-expressed)
R&D Systems, part of Bio-Techne
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8614-MT-100
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Key Product Details

Source

HEK293

Accession #

P08581 (HGF R alpha) & P08581 (HGF R beta)

Structure / Form

Tetramer containing two disulfide-linked alpha and beta subunits

Conjugate

Unconjugated

Applications

Bioactivity

View all HGFR/c-MET Proteins and Enzymes »

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived human HGF R/c-MET protein
Human HGF R alpha
(Glu25-Arg307)
Accession # P08581
Human HGF R beta
(Ser308-Thr932)
Accession # P08581		 HIEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus

Purity

>85%, by SDS-PAGE with silver staining.

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Glu25 & Ser308

Predicted Molecular Mass

33 kDa & 96 kDa

SDS-PAGE

34-48 kDa and 103-126 kDa, reducing conditions

Activity

Measured by its ability to bind immobilized recombinant human HGF in a functional ELISA with an estimated Kd <0.15 nM.

Formulation, Preparation and Storage

8614-MT
Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution
Reconstitute at 250 μg/mL in PBS.

Reconstitution Buffer Available:
Size / Price
Qty
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.

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). 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  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, over-expression, and additional splicing and proteolytic cleavage of HGF R have been described in a wide range of cancers (1). Within the ECD, human HGF R shares 86%-88% aa sequence identity with canine, mouse, and rat 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

Alternate Names

c-MET, cMET, HGF R, MET

Entrez Gene IDs

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

Gene Symbol

MET

UniProt

P08581 (HGF R alpha) & P08581 (HGF R beta)

Additional HGFR/c-MET Products

Product Documents for Recombinant Human HGFR/c-MET Fc Chimera Protein, CF

Product Datasheets

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Product Specific Notices for Recombinant Human HGFR/c-MET Fc Chimera Protein, CF

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