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Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus

buffered aqueous glycerol solution, ≥1,000 units/mg protein (Lowry)

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1-Phosphatidyl-D-myo-inositol inositol phosphohydrolase, cyclic-phosphate forming, PI-PLC
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:

biological source

Bacillus sp. (Bacillus cereus)

Quality Level


buffered aqueous glycerol solution

specific activity

≥1,000 units/mg protein (Lowry)

mol wt

28 kDa

foreign activity

Phopholipase C (lecithinase) ≤1 units/mg protein
Sphingomyelinase ≤40 units/mg protein

storage temp.


Gene Information

Bacillus cereus E33L ... BCZK3513(3026815)

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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.


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

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.
Used for the release of GPI anchored proteins from the membrane.

Unit Definition

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).

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.

Storage Class

11 - Combustible Solids




Not applicable


Not applicable


Eyeshields, Gloves, type N95 (US)

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