Phosphoinositide-specific phospholipase C (PLC) plays a crucial role in the initiation of receptor mediated signal transduction through the generation of the two second messengers, inositol 1,4,5-triphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. There are many mammalian PLC isozymes, including PLC beta1, PLC beta2, PLC beta3, PLC beta4, PLC gamma1, PLC gamma2, PLC delta1, PLC delta2 and PLC epsilon. PLC gamma1 is widely distributed in bronchiolar epithelium, type I and II pneumocytes and fibroblasts of the interstitial tissue. Actinregulatory protein Villin is tyrosine phosphorylated and associates with PLC gamma1 in the brush border of intestinal epithelial cells. Villin regulates PLC gamma1 activity by modifying its own ability to bind phosphatidylinositol 4,5-biphosphate. PLC gamma1 binds alpha1beta1 Integrin and modulates alpha1beta1 Integrin-specific adhesion. PLC gamma1 and Ca2+ play a direct role in VEGF-regulated endothelial growth, however this signaling pathway is not linked to FGF-mediated effects in primary endothelial cells.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
