ADENOVIRUS-PLCGAMMA2

Vector Biolabs

ADENOVIRUS-PLCGAMMA2

5

Other Application

Research Use Only

1E10 PFU/ml

Phospholipase C y1 (PLC y1), a phosphatidylinositol-4,5-bisphosphate (PI-4,5-P2)-specific phosphodiesterase plays a critical 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. A total of nine mammalian PLC isozymes have been described (PLC B1, PLC B2, PLC B3, PLC B4, PLC y1, PLC y2, PLC delta1, PLC delta2 and PLC epsilon) with molecular weights ranging from 85 to 255 kDa. The y-type enzymes are unique in that they contain SH2 and SH3 domains. Moreover, the two y-type enzymes, but not the B and delta isozymes, are subject to activation by a number of protein tyrosine kinases, which associate with SH2 domains and induce their activation by phosphorylation. In contrast, activation of PLC B1, PLC B2 and PLC y3 is mediated by the a subunits of the Gq class of heterotrimeric G proteins and by certain G protein By subunits. PLC-L (for PLC-deleted in lung carcinoma) plays a role in inositol phospholipid-based intracellular signaling and contributes to the progression of human lung carcinoma. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1) and C-gamma-2 (PLCG2) enzymes are controlled by receptor tyrosine kinases. The C-gamma-1 and C-gamma-2 enzymes are composed of phospholipase domains that flank regions of homology to noncatalytic domains of the SRC oncogene product, SH2 and SH3.

-80°C

41106621