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|This affinity purified antibody was prepared from whole rabbit serum produced by repeated immunizations with a synthetic peptide corresponding to residues surrounding Y1349 and Y1356 of human c-Met protein.|
|human, mouse, rat
||Lot dependent; please refer to CoA along with shipment
||ELISA: 1:93,000, WB: 1ug/mL
|0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2|
|This antibody is designed, produced, and validated for Cancer, Immunology and Nuclear Signaling research. Anti-c-MET is the receptor for hepatocyte growth factor (also known as scatter factor, HGF/SF), and belongs to the tyrosine kinase superfamily. Interaction of c-Met with HGF results in autophosphorylation of c-Met at multiple tyrosines. Phosphorylation of Y1234/1235 in the c-Met kinase domain is critical to kinase activation. When phosphorylated, Y1349 and Y1356, along with surrounding amino acids, form a unique bidentate docking site for substrates such as Gab1, Grb2, phosphatidylinositol 3-kinase (PI3K) and others. C-Met mainly uses the Gab1 scaffolding adaptor in its initial step of signal transmission. Well-characterized downstream signalling pathways that are activated by c-Met include the ERK/MAPK, PI3K–Akt/PKB, Crk–Rap and Rac–Pak pathways, resulting in proliferation and increased cell survival.
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Western blot using affinity purified anti-c-Met pY1349pY1356 antibody shows detection of phosphorylated c-Met. Human mammary B5/589 epithelial cells were serum-deprived and treated with or without HGF. Cell lysates were immunoprecipated with the anti-c-Met antibody, resolved by SDS-PAGE, transferred to PVDF membrane, and probed with anti-c-Met pY1349pY1356. Personal communication, D. Bottaro and T. Ito, NCI, Bethesda, MD
WB using Anti-c-Met pY1349pY1356 shows detection of phosphorylated c-Met. Human mammary epithelial cells (B5/589) were serum deprived and stimulated with (+) and without (-) HGF. Cell lysates were IP'd using human anti-c-Met, and probed using various antibodies. Lane 1 and 2 where probed using the anti-c-Met pY1349pY1356, lane 3 and 4 where probed using an anti-phosphotyrosine as phosphorylation control and lane 5 and 6 where probed using an anti-cMet as a total Met loading control. Bands recognized at MW of ~170 kDa are total Met, ~145 kDa phosphorylated Met beta chain in HGF +, ~150 kDa phosphorylated Met in +/- HGF, ~50kDa phosphorylated Met alpha chain.