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P7633

Sigma-Aldrich

Phospholipase C from Clostridium perfringens (C. welchii)

greener alternative

Type I, lyophilized powder, 10-50 units/mg protein

Sinónimos:

PC-PLC

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About This Item

Número de CAS:
9001-86-9
Comisión internacional de enzimas:
3.1.4.3 (BRENDA, IUBMB)
EC Number:
232-638-2
MDL number:
MFCD00131895
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

bacterial (Clostridium perfringens)

Quality Level

200

type

Type I

form

lyophilized powder

specific activity

10-50 units/mg protein

composition

protein, 20-40%

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

application(s)

diagnostic assay manufacturing

greener alternative category

, Enabling

storage temp.

−20°C

Gene Information

Clostridium perfringens str. 13 ... plc(988262)

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General description

We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in biodiesel research. For more information see the article in biofiles.

Application

Phospholipase C (PLC) has been used to study adrenoceptor-mediated transmembrane signaling. It is also used to degrade inositol-containing phospholipids. Furthermore, it has been used to study 9E3 gene activation.

Biochem/physiol Actions

PLC hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol. This enzyme also hydrolyzes the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids. Phospholipase C is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid.
Hydrolyzes the phosphate bond on phosphatidylcholine and other glycerophospholipids yielding diacylglycerol; this enzyme will also hydrolyze the phosphate bonds of sphingomyelin, cardiolipin, choline plasmalogen and ceramide phospholipids.

Unit Definition

One unit will liberate 1.0 μmole of water soluble organic phosphorus from egg yolk L-α-phosphatidylcholine per min at pH 7.3 at 37 °C.

Inhibitor

Referencia del producto
Descripción
Precios

Substrate

Referencia del producto
Descripción
Precios

N5879

O-(4-Nitrophenylphosphoryl)choline

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Mojtaba Alimolaei et al.
Probiotics and antimicrobial proteins, 10(2), 251-257 (2017-04-13)
The alpha-toxin is one of the virulence factors of Clostridium perfringens for gas gangrene in humans and animals or necrotic enteritis in poultry. The C-terminal domain of this toxin ( cpa 247-370 ) was synthesized and cloned into pT1NX vector
R Spangler et al.
Proceedings of the National Academy of Sciences of the United States of America, 86(18), 7017-7021 (1989-09-01)
Induction of the transformation-related gene 9E3 by the v-src and v-fps gene products (v-Src and v-Fps) is blocked in chicken embryo fibroblasts depleted of protein kinase C (PKC). PKC agonists induce 9E3 gene expression. Protein kinase inhibitors block v-Src- and
Caterina Casari et al.
The Journal of clinical investigation, 123(12), 5071-5081 (2013-11-26)
von Willebrand disease type 2B (vWD-type 2B) is characterized by gain-of-function mutations in von Willebrand factor (vWF) that enhance its binding to the glycoprotein Ib-IX-V complex on platelets. Patients with vWD-type 2B have a bleeding tendency that is linked to
Purification of Clostridium perfringens phospholipase C (alpha-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein.
T Takahashi et al.
Biochimica et biophysica acta, 351(1), 155-171 (1974-05-10)
Sina Koch et al.
Developmental cell, 28(6), 633-646 (2014-03-25)
Neuropilin 1 (NRP1) modulates angiogenesis by binding vascular endothelial growth factor (VEGF) and its receptor, VEGFR2. We examined the consequences when VEGFR2 and NRP1 were expressed on the same cell (cis) or on different cells (trans). In cis, VEGF induced
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