Merck, P8804-5UN, Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus

General description
Phospholipase C (PI-PLC) from Bacillus cereus has irregular triosephosphate isomerase (TIM)-barrel structure with eight-standard parallel β barrel. It is a 28 kDa protein.
Application
Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus has been used:
in the hydrolysis of substrates p-nitrophenylphosphorylcholine (p-NPPC) and p-nitrophenylphosphorylphosphate (p-NPP)
to cleave glycosylphosphatidylinositol (GPI) anchor of lynx1 protein and its detachment from plasma membrane
to cleave immunolabeled HeLa cells

Biochem/physiol Actions
Used for the release of GPI anchored proteins from the membrane.
Phospholipase C (PI-PLC) releases diacylglycerol by cleaving the glycosylphosphatidylinositol. It has broad substrate specificity and its activity is influenced by metal ions and surfactants.
Physical form
Solution in 60% (v/v) glycerol containing 10 mM Tris-HCl, pH 8.0 and 10 mM EDTA
Analysis Note
Acetylcholinesterase is measured according to Ellman, et al.
Other Notes
One unit will liberate one unit of acetylcholinesterase per minute from a membrane-bound crude preparation at pH 7.4 at 30 °C (10 minute incubation).