Mouse HGFR/c-MET Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF527
Product Details
Citations (2)
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Mouse HGFR/c-MET Biotinylated Antibody Summary

Species Reactivity
Mouse
Specificity
Detects mouse HGF R/c‑MET in ELISAs and Western blots. In sandwich immunoassays, less than 0.2% cross-reactivity with recombinant human HGF R, recombinant mouse (rm) HGF A, and rmMSP R is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse HGF R/c‑MET
Glu25-Asn929
Accession # P16056
Formulation
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Label
Biotin

Applications

Recommended Concentration
Sample
Western Blot
0.1 µg/mL
Recombinant Mouse HGF R/c-MET Fc Chimera (Catalog # 527-ME)
Immunohistochemistry
5-15 µg/mL
Immersion fixed frozen sections of mouse embryo (E13)

Mouse HGF R/c-MET Sandwich Immunoassay

Recommended Concentration
Reagent
ELISA Detection (Matched Antibody Pair)
0.1-0.4 µg/mL 

Use in combination with:

Capture Reagent: Mouse HGFR/c-MET Antibody (Catalog # MAB5271)

Standard: Recombinant Mouse HGFR/c-MET Fc Chimera His-tag Protein, CF (Catalog # 527-ME)

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Reconstitution Calculator

Reconstitution Calculator

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Preparation and Storage

Reconstitution
Reconstitute at 0.2 mg/mL in sterile PBS.
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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.
  • 6 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  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. 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.
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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Citations for Mouse HGFR/c-MET Biotinylated Antibody

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.

2 Citations: Showing 1 - 2
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  1. Soluble c-Met receptors inhibit phosphorylation of c-Met and growth of hepatocyte growth factor: c-Met-dependent tumors in animal models.
    Authors: Coxon A, Rex K, Meyer S, Sun J, Sun J, Chen Q, Radinsky R, Kendall R, Burgess TL
    Mol. Cancer Ther., 2009-05-12;0(0):.
    Species: Mouse
    Sample Types: Cell Lysates
    Applications: Electrochemiluminescent Assay
  2. Bmi-1-green fluorescent protein-knock-in mice reveal the dynamic regulation of bmi-1 expression in normal and leukemic hematopoietic cells.
    Authors: Hosen N, Yamane T, Muijtjens M, Pham K, Clarke MF, Weissman IL
    Stem Cells, 2007-03-29;25(7):1635-44.
    Species: Mouse
    Sample Types: Whole Cells
    Applications: ICC

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