Canine HGFR/c-MET Biotinylated Antibody

Catalog # Availability Size / Price Qty
BAF4140
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Canine HGFR/c-MET Biotinylated Antibody Summary

Species Reactivity
Canine
Specificity
Detects canine HGF R in ELISAs and Western blots. In sandwich immunoassays, less than 7% cross-reactivity with recombinant mouse HGF R is observed and less than 0.2% cross-reactivity with recombinant human HGF R is observed.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant canine HGF R
Glu25-Leu935
Accession # Q75ZY9
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 Canine HGF R/c-MET (Catalog # 4140-ME)

Canine 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: Canine HGFR/c-MET Antibody (Catalog # AF4140)

Standard: Recombinant Canine HGFR/c-MET Protein, CF (Catalog # 4140-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.

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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 posttranslational 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 region, and four Ig-like E-set domains, while the cytoplasmic region includes a tyrosine kinase domain (3). The sema domain, which is formed by both the alpha and beta chains of HGF R, mediates both ligand binding and receptor dimerization (3, 4). Ligand-induced tyrosine phosphorylation in the cytoplasmic region activates the kinase domain and provides docking sites for multiple SH2-containing molecules (5, 6). HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation (7). 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, B2, and B3, and MSP R/Ron (8‑15). Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects (8‑15). Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion (8, 12, 13). HGF released from neighboring mesenchymal cells stimulates HGF R on undifferentiated epithelium and induces epithelial cell scattering and branching tubulogenesis (16). 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, canine HGF R shares 85%‑88% amino acid sequence identity with human, mouse and rat HGF R.

 

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. USA 100:12039.
  4. Kong-Beltran, M. et al. (2004) Cancer Cell 6:75.
  5. Naldini, L. et al. (1991) Mol. Cell. Biol. 11:1793.
  6. Ponzetto, C. et al. (1994) Cell 77:261.
  7. Jeffers, M. et al. (1997) Mol. Cell. Biol. 17:799.
  8. Orian-Rousseau, V. et al. (2002) Genes Dev. 16:3074.
  9. Klosek, S.K. et al. (2005) Biochem. Biophys. Res. Commun. 336:408.
  10. Jo, M. et al. (2000) J. Biol. Chem. 275:8806.
  11. Wang, X. et al. (2002) Mol. Cell 9:411.
  12. Trusolino, L. et al. (2001) Cell 107:643.
  13. Giordano, S. et al. (2002) Nat. Cell Biol. 4:720.
  14. Conrotto, P. et al. (2004) Oncogene 23:5131.
  15. Follenzi, A. et al. (2000) Oncogene 19:3041.
  16. 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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