Rabbit Anti-PLCG1 monoclonal antibody for WB, ICC, IP. 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 ?1, PLC ?2, PLC ?3, PLC ?4, PLC ?1, PLC ?2, PLC ?1, PLC ?2 and PLC?. PLC ?1 is widely distributed in bronchiolar epithelium, type I and II pneumocytes and fibroblasts of the interstitial tissue. Actin-regulatory protein Villin is tyrosine phosphorylated and associates with PLC ?1 in the brush border of intestinal epithelial cells. Villin regulates PLC ?1 activity by modifying its own ability to bind phosphatidylinositol 4,5-biphosphate. PLC ?1 binds Integrin ?1/?1 and modulates Integrin ?1/?-specific adhesion. PLC ?1 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. PLC ?1 is rapidly activated in response to growth factor stimulation and plays an important role in regulating cell proliferation and differentiation. It may also have a protective function during cellular response to oxidative stress.
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