More info
Assay Range | 62.5--4000 pg/mL |
Sensitivity | 5.0 pg/mL |
Size | 96T |
Storage | Store at 2 - 8ºC. Keep reconstituted standard and detection Ab at -20 ºC |
Assay Principle | Sandwich ELISA |
Sample volume | 100 µL final volume, dilution factor varies on samples |
Detection Method | Chromogenic |
Kit Components
1. Recombinant Mouse C-MET standard: 2 vials
2. One 96-well plate precoated with anti- Mouse C-MET Ab
3. Sample diluent buffer: 12 mL - 1
4. Detection antibody: 130 µL, dilution 1:100
5. Streptavidin-HRP: 130 µL, dilution 1:100
6. Antibody diluent buffer: 12 mL x1
7. Streptavidin-HRP diluent buffer: 12 mL x1
8. TMB developing agent: 10 mL x1
9. Stop solution: 10 mL x1.
10. Washing solution (20x): 25 mL x1.
Background
HGF R (Hepatocyte growth factor receptor), also known as proto-oncogene c-Met (c-Met), is encoded by the MET gene in humans. Mature HGF R is a disulfide-linked dimer composed of a 50 kDa extracellular α chain and a 145 kDa transmembrane β chain. The extracellular domain (ECD) contains a seven bladed β propeller sema domain, a cysteine-rich PSI/MRS, and four Ig-like E-set domains, while the cytoplasmic region includes the tyrosine kinase domain. Proteolysis and alternative splicing generate additional forms of human HGF R with variable functional domains. The ECD of mouse HGF R shares 87% and 84% aa sequence identity with, human and rat HGF R. HGF R plays a central role in epithelial morphogenesis and cancer development. In the absence of ligand, HGF R forms non-covalent complexes with a variety of membrane proteins including CD44v6, CD151, EGF R, Fas, integrin α6/β4, Plexins B1, 2, 3, and MSP R/Ron. HGF stimulation induces HGF R downregulation via internalization and proteasome-dependent degradation. Ligation of one complex component triggers activation of the other, followed by cooperative signaling effects. Formation of some of these heteromeric complexes is a requirement for epithelial cell morphogenesis and tumor cell invasion. Genetic polymorphisms, chromosomal translocation, overexpression, and additional splicing and proteolytic cleavage of HGF R have been found in a wide range of cancers.