HGFR/c-MET Antibody (118627) [Alexa Fluor® 350]

• Reactivity: Mu
• Applications: ELISA(Cap), ELISA(Det)
• Clone: 118627
• Clonality: Monoclonal
• Host: Rat
• Conjugate: Alexa Fluor 350

HGFR/c-MET Antibody (118627) [Alexa Fluor® 350] Summary

• Immunogen: S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse HGF R
  Glu25-Asn929
  Accession # P16056
• Specificity: Detects mouse HGF R in ELISAs. In a sandwich ELISA, no cross-reactivity or interference was observed with recombinant human (rh) HGF R, rmHGFA, or rhMSP R.
• Isotype: IgG2a
• Clonality: Monoclonal
• Host: Rat
• Purity Statement: Protein A or G purified

Applications/Dilutions

• Dilutions:
  • ELISA Capture (Matched Antibody Pair)
  • ELISA Detection (Matched Antibody Pair)

Packaging, Storage & Formulations

• Storage: Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied
• Buffer: Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide

Notes

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

Alternate Names for HGFR/c-MET Antibody (118627) [Alexa Fluor® 350]

• 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.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.