Recombinant Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

Order Details

Recombinant Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF Summary

Details of Functionality
Measured by its ability to bind rmHGF in a functional ELISA with an estimated
KD <0.2 nM.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse HGF R/c-MET protein
Mouse HGF R
(Met1 - Asn929)
Accession # P16056
DIEGRMD Human IgG1
(Pro100 - Lys330)
6-His tag
N-terminus C-terminus


Accession #
N-terminal Sequence
Glu25 ( alpha chain) & Ser307 ( beta chain)
Structure / Form
Tetramer; disulfide-linked homodimer of disulfide-linked heterodimers
Protein/Peptide Type
Recombinant Proteins
Gene
Met
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
32 kDa ( alpha chain) & 96 kDa ( beta chain) (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
35-40 kDa & 100-110 kDa, reducing conditions
Publications
Read Publications using
527-ME in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF

  • 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

Background

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.

  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. 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.

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Publications for HGFR/c-MET (527-ME)(3)

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Bioinformatics

Gene Symbol Met
Uniprot