A total of eight mammalian PLC isozymes have been described (PLC β1, PLC β2, PLC β3, PLC β4, PLC γ1, PLC γ2, PLC δ1 and PLC δ2) with molecular weights ranging from 85 to 150 kDa. The γ-type enzymes are unique in that they contain SH2 and SH3 domains. Moreover, the two γ-type enzymes, but not the β and δ isozymes, are subject to activation by a number of protein tyrosine kinases which associate with their SH2 domains and induce their activation by phosphoryation. In contrast, activation of PLC β1, PLC β2 and PLC β3 is mediated by the α subunits of the Gq class of heterotrimeric G proteins and by certain βγ G protein subunits. The regulatory mechanisms for PLC δ1 and PLC δ2 are as yet not resolved.

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase β-3; Phosphoinositide phospholipase C-β-3; Phospholipase C-β-3; PLC-β3; 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3; Phosphoinositide phospholipase C-beta-3; Phospholipase C-beta-3; PLC-beta-3; PLCB3; PLCβ3

q01970

Human,Mouse,Rat

WB,IHC

WB 1:500-1:1000
IHC 1:50-1:200

~ 150 kDa

Rabbit

This antibody detects endogenous levels of PLC β3 protein.

Synthetic peptide, corresponding to amino acids 1080-1130 of Human PLC β3.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.