Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus

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

1-Phosphatidyl-D-myo-inositol inositol phosphohydrolase, cyclic-phosphate forming, PI-PLC
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
Pricing and availability is not currently available.


buffered aqueous glycerol solution

Quality Level

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


5, 25 units in poly bottle

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Critical evaluation of p-nitrophenylphosphorylcholine (p-NPPC) as artificial substrate for the detection of phospholipase C
Flieger A, et al.
Enzyme and Microbial Technology, 26(5-6), 451-458 (2000)
Sequence of the Bacillus thuringiensis phosphatidylinositol specific phospholipase C.
D J Henner et al.
Nucleic acids research, 16(21), 10383-10383 (1988-11-11)
M G Low et al.
The Biochemical journal, 167(1), 281-284 (1977-10-01)
Purified phosphatidylinositol-specific phospholipase C from Staphylococcus aureus released a substantial proportion of the total alkaline phosphatase activity from a wide range of tissues from several mammalian species. Co-purification of the phospholipase C and alkaline phosphatase-releasing activities and the inhibition of...
Vincenza Rita Lo Vasco et al.
Journal of cellular biochemistry, 100(4), 952-959 (2006-10-26)
Signal transduction from plasma membrane to cell nucleus is a complex process depending on various components including lipid signaling molecules, in particular phosphoinositides and their related enzymes, which act at cell periphery and/or plasma membrane as well as at nuclear...
D B Rawool et al.
International journal of food microbiology, 113(2), 201-207 (2006-09-19)
Clinical samples (n=725) were collected from bovines (n=243) which were positive for mastitis using the California mastitis test (CMT) and somatic cell count (SCC). The clinical samples comprising blood (n=239), milk (n=243), and faecal swabs (n=243) were examined for the...
GPI Anchored Glycoproteins
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