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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

Synonyme(s) :

PC-PLC

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About This Item

Numéro CAS:
9001-86-9
Numéro de classification (Commission des enzymes):
3.1.4.3 (BRENDA, IUBMB)
Numéro CE :
232-638-2
Numéro MDL:
MFCD00131895
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Clostridium perfringens)

Niveau de qualité

200

Type

Type I

Forme

lyophilized powder

Activité spécifique

10-50 units/mg protein

Composition

protein, 20-40%

Caractéristiques du produit alternatif plus écologique

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

sustainability

Greener Alternative Product

Application(s)

diagnostic assay manufacturing

Autre catégorie plus écologique

, Enabling

Température de stockage

−20°C

Informations sur le gène

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

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Catégories apparentées

Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
N Sieger et al.
Arthritis and rheumatism, 65(3), 770-779 (2012-12-13)
CD22 is a surface molecule exclusively expressed on B cells that regulates adhesion and B cell receptor (BCR) signaling as an inhibitory coreceptor of the BCR. Central downstream signaling molecules that are activated upon BCR engagement include spleen tyrosine kinase
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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