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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)
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Analysis Note
Acetylcholinesterase is measured according to Ellman, et al.
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
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.
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.
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).
Physical form
Solution in 60% (v/v) glycerol containing 10 mM Tris-HCl, pH 8.0 and 10 mM EDTA
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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)
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)
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)
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
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