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Merck

P8804

Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus

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

Sinónimos:

1-Phosphatidyl-D-myo-inositol inositol phosphohydrolase, cyclic-phosphate forming, PI-PLC

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.32
EC Number:
232-638-2
MDL number:
Número CE:

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Nombre del producto

Phospholipase C, Phosphatidylinositol-specific from Bacillus cereus, buffered aqueous glycerol solution, ≥1,000 units/mg protein (Lowry)

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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Este artículo
P5542525186P6621
specific activity

≥1,000 units/mg protein (Lowry)

specific activity

≥1,000 units/mg protein (Lowry)

specific activity

≥50 units/mg dry wt.

specific activity

≥200 units/mg protein

biological source

Bacillus sp. (Bacillus cereus)

biological source

-

biological source

-

biological source

-

Gene Information

Bacillus cereus E33L ... BCZK3513(3026815)

Gene Information

Bacillus cereus E33L ... BCZK3513(3026815)

Gene Information

-

Gene Information

Bacillus cereus ATCC 10987 ... plC(2749087)

form

buffered aqueous glycerol solution

form

lyophilized powder

form

solid

form

lyophilized powder

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−20°C

mol wt

28 kDa

mol wt

-

mol wt

-

mol wt

23-27 kDa by SDS-PAGE

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)[1]
  • to cleave glycosylphosphatidylinositol (GPI) anchor of lynx1 protein and its detachment from plasma membrane[2]
  • to cleave immunolabeled HeLa cells[3]

Biochem/physiol Actions

Phospholipase C (PI-PLC) releases diacylglycerol by cleaving the glycosylphosphatidylinositol.[4] It has broad substrate specificity and its activity is influenced by metal ions and surfactants.[5]
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.[4] It is a 28 kDa protein.[5]

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

related product

Referencia del producto
Descripción
Precios

Clase de almacenamiento

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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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.

Visite la Librería de documentos

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)
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)
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)
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)

Artículos

Glycosylphosphatidylinisotol- (GPI) anchored proteins have been identified throughout a broad range of eukaryotic species ranging from humans to insects, yeasts, bacteria, and fungi, suggesting that they are an ancient modification.

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