Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-638-2
MDL number:
Specific activity:
≥1,000 units/mg protein (Lowry)
Biological source:
Bacillus sp. (Bacillus cereus)
biological source
Bacillus sp. (Bacillus cereus)
form
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.
2-8°C
Quality Level
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.
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).
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
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)
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)
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)
Related Content
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