This antibody detects endogenous levels of PLC-gamma 2 only when phosphorylated at Tyrosine 1217.
Purification
Immunoaffinity Chromatography: The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Immunogen
The antiserum was produced against synthesized phosphopeptide derived from Human PLC-gamma 2 around the phosphorylation site of Tyrosine 1217 (F-L-Yp-D-T).
Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water soluble phosphorylated derivatives of the lipid head groups. A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide specific phospholipase C enzymes, C beta is regulated by heterotrimeric G protein coupled receptors, while the closely related C gamma 1 and C gamma 2 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.Synonyms: 1-phosphatidylinositol-4, 5-bisphosphate phosphodiesterase gamma-2, PLC-IV, PLC-gamma-2, Phosphoinositide phospholipase C-gamma-2, Phospholipase C-IV, Phospholipase C-gamma-2