Phospholipase C gamma 1 phospho Y783

GWB-4C30EF

Synthetic peptide (Human) derived from the region of Phospholipase C gamma that contains tyrosine 783 based on the human sequence. This region is conserved among many species including human rat bovine and frog (Xenopus laevis).

Phosphorylation site-specific antibody selective for the phosphorylated form of the Phospholipase C gamma 1 containing a phosphate on tyrosine 783. The antibody has been shown to recognize the endogenous form of Phospholipase C gamma when phosphorylated on tyrosine 783 in a variety of cell types following treatment by a broad range of extracellular stimuli. Applications include NIH 3T3 cells +/- PDGF. The antibody does not react with a site directed mutant (Y783F).

Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using i) a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with nonphosphorylated Phospholipase C gamma enzymes and (ii) a generic tyrosine phosphorylated peptide to remove antibody that is reactive with phosphotyrosine irrespective of the sequence. The final product is generated by affinity chromatography using an Phospholipase C gamma-derived peptide that is phosphorylated at tyrosine 783. Storage

WB: Use at a dilution of 1/1000. Predicted

PLC-gamma is a major substrate for heparin-binding growth factor 1 (acidic fibroblast growth factor)-activated tyrosine kinase.

Interacts with CENTG1 via its SH3 domain (By similarity). Interacts with phosphorylated LAT upon TCR activation. Interacts with the Pro-rich domain of TNK1 via its SH3 domain. Associates with BLNK VAV1 GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1 and MIST (By similarity). Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein.

The receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2 involves their phosphorylation by tyrosine kinases in response to ligation of a variety of growth factor receptors and immune system receptors.

Contains 1 C2 domain.

Contains 2 PH domains.

Contains 1 PI-PLC Y-box domain.

Contains 1 SH3 domain.