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:


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)

Looking for similar products? Visit Product Comparison Guide

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

Ligand binding characteristics of a glycosylphosphatidyl inositol membrane-anchored HeLa cell folate receptor epitope-related to human milk folate binding protein
Holm J, et al.
Bioscience Reports, 20(2), 109-118 (2000)
Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl (alpha1? 6)-d-myo-inositol, an essential fragment of GPI anchors
Heinz DW, et al.
Biochemistry, 35(29), 9496-9504 (1996)
High-level expression of recombinant phospholipase C from Bacillus cereus in Pichia pastoris and its characterization
Seo KH and Rhee JI
Biotechnology Letters, 26(19), 1475-1479 (2004)
Lynx1 shifts alpha4beta2 nicotinic receptor subunit stoichiometry by affecting assembly in the endoplasmic reticulum
Nichols WA, et al.
The Journal of Biological Chemistry, 289(45), 31423-31432 (2014)
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)
GPI Anchored Glycoproteins
Read More

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon


Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.