|Tested species reactivity||Human, Mouse, Non-human primate, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||A synthetic phosphopeptide derived from human PLCG1 around the phosphorylation site of Tyr771 (P-D-YP-G-A)|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.4, with 150mM NaCl, 50% glycerol|
|Contains||0.02% sodium azide|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1:50-1:100|
|Western Blot (WB)||1:500-1:1000|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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 alpha1 beta1 Integrin and modulates alpha1 beta1 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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.