P6621
Phospholipase C from Bacillus cereus
≥200 units/mg protein
Sinónimos:
PC-PLC
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
form
lyophilized powder
Quality Level
specific activity
≥200 units/mg protein
mol wt
23-27 kDa by SDS-PAGE
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
solubility
H2O: soluble 1.0 mg/mL, faintly hazy to hazy
greener alternative category
storage temp.
−20°C
Gene Information
Bacillus cereus ATCC 10987 ... plC(2749087)
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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) is used to study adrenoceptor-mediated transmembrane signaling. It is used to degrade inositol-containing phospholipids. Phospholipase C from Bacillus, product P6621, has been used to study how flhF affects the export of PLC and other secretory virulence factors.
The enzyme from Sigma has been used in the digestion of phosphatidylserine fraction of Schistosoma mansoni adult worms.
Biochem/physiol Actions
Phospholipase C is induced by thrombin and platelet-activating factor, forming 1,2-diacylglycerol and phosphatidic acid. PLC 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.
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 L-α-phosphatidylcholine per min at pH 7.3 at 37 °C.
Physical form
Lyophilized powder containing approx. 10% protein. Remainder; trehalose, zinc sulfate, and potassium phosphate
signalword
Danger
hcodes
pcodes
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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Desiree van der Kleij et al.
The Journal of biological chemistry, 277(50), 48122-48129 (2002-10-03)
Schistosome infections are characterized by prominent T cell hyporesponsiveness during the chronic stage of infection. We found that schistosome-specific phosphatidylserine (PS) activated TLR2 and affected dendritic cells such that mature dendritic cells gained the ability to induce the development of
W Siess et al.
The Journal of biological chemistry, 259(13), 8286-8292 (1984-07-10)
The present study compares the molecular mechanism by which thrombin, platelet-activating factor, and epinephrine induce platelet activation. Thrombin and platelet-activating factor induce an initial activation of phospholipase C, as measured by formation of 1,2-diacylglycerol and phosphatidic acid, during platelet shape
T Das et al.
The Journal of biological chemistry, 268(36), 27398-27405 (1993-12-25)
Our studies on the alpha 1-adrenoceptor signaling have demonstrated that the Gh family is a signal mediator. We report here that a 69-kDa phospholipase C (PLC) is the effector in this signal pathway. The enzyme was isolated by dissociating a
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Sara Salvetti et al.
Microbiology (Reading, England), 153(Pt 8), 2541-2552 (2007-07-31)
Flagellar arrangement is a highly conserved feature within bacterial species. However, only a few genes regulating cell flagellation have been described in polar flagellate bacteria. This report demonstrates that the arrangement of flagella in the peritrichous flagellate Bacillus cereus is
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