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Merck

C1235

Cholesterol Oxidase microbial

recombinant, lyophilized powder, ≥10 units/mg protein

Synonim(y):

Cholesterol: oxygen oxidoreductase

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100 UNITS

1070,00 zł

1070,00 zł


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Informacje o tej pozycji

Numer CAS:
NACRES:
NA.54
UNSPSC Code:
12352204
EC Number:
232-842-1
MDL number:
Numer WE:
Specific activity:
≥10 units/mg protein

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form

lyophilized powder

specific activity

≥10 units/mg protein

mol wt

55 kDa

solubility

50 mM potassium phosphate buffer, pH 7.0: soluble

storage temp.

−20°C

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Ta pozycja
C8868C5421C8649
specific activity

≥10 units/mg protein

specific activity

≥50 units/mg protein

specific activity

≥30 units/mg protein (biuret)

specific activity

≥20 units/mg protein

form

lyophilized powder

form

lyophilized powder

form

aqueous solution

form

lyophilized powder

solubility

50 mM potassium phosphate buffer, pH 7.0: soluble

solubility

-

solubility

50 mM potassium phosphate buffer, pH 7.0: soluble (Cold)

solubility

50 mM potassium phosphate buffer, pH 7.0: soluble (Cold)

storage temp.

−20°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

mol wt

55 kDa

mol wt

64 kDa

mol wt

62 kDa

mol wt

~34 kDa

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

200

Application

Cholesterol oxidase is used to determine serum cholesterol.[1][2] The enzyme also finds application in the microanalysis of steroids in food samples and in distinguishing 3-ketosteroids from 3b-hydroxysteroids.[3] Transgenic plants expressing cholesterol oxidase are being investigated in the fight against the cotton boll weevil.[4] CHOD has also been used as a molecular probe to elucidate cellular membrane structures.[5][6]

Biochem/physiol Actions

Cholesterol oxidase (CHOD) is a monomeric flavoprotein containing FAD that catalyzes the first step in cholesterol catabolism. This bifunctional enzyme oxidizes cholesterol to cholest-5-en-3-one in an FAD-requiring step. This is subsequently isomerized to cholest-4-en-3-one with the release of H2O2. Optimum pH of the enzyme is 7.0. Hg2+, Ag+, ionic detergents inhibit the enzyme activity.

Preparation Note

Dissolves in cold 50 mM potassium phosphate buffer, pH 7.0. Solution is to be prepared just before use.

Other Notes

One unit will convert 1.0 μmol of cholesterol to 4-cholesten-3-one per minute at 37 °C and pH 7.0 in a peroxidase linked system.
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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Klasa składowania

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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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

Bruno M Castro et al.
The Journal of biological chemistry, 284(34), 22978-22987 (2009-06-13)
A uniquely sensitive method for ceramide domain detection allowed us to study in detail cholesterol-ceramide interactions in lipid bilayers with low (physiological) ceramide concentrations, ranging from low or no cholesterol (a situation similar to intracellular membranes, such as endoplasmic reticulum)
Christophe A Marquette et al.
Analytical and bioanalytical chemistry, 390(1), 155-168 (2007-10-03)
The present review draws a general picture of the bioanalytical applications of electro-chemiluminescent reactions (ECL). Only the two main ECL reactions-i.e. the luminol-based and Ru(bpy)(3)(2+)-based reactions-are considered for application in the fields of enzyme biosensors, immunochemical biosensors, DNA biosensors, and
Porntip H Lolekha et al.
Clinica chimica acta; international journal of clinical chemistry, 339(1-2), 135-145 (2003-12-23)
Cholesterol oxidase is used for the determination of serum cholesterol. It can be derived from Streptomyces, Pseudomonas fluorescens, Cellulomonas, and Brevibacterium. This study compared the performance characteristics of four enzymes in the endpoint cholesterol determination. Using the Mega analyzer, we
Kwang-wook Ahn et al.
Biochemistry, 43(3), 827-836 (2004-01-21)
We investigated the dependence of cholesterol oxidase catalytic activity and membrane affinity on lipid structure in model membrane bilayers. The binding affinities of cholesterol oxidase to 100-nm unilamellar vesicles composed of mixtures of DOPC or DPPC and cholesterol are not
Vandana Praveen et al.
Applied biochemistry and biotechnology, 165(5-6), 1414-1426 (2011-09-13)
An extracellular cholesterol oxidase (cho) enzyme was isolated from the Streptomyces parvus, a new source and purified 18-fold by ion exchange and gel filtration chromatography. Specific activity of the purified enzyme was found to be 20 U/mg with a 55

Protokoły

Enzymatic activity assay for cholesterol oxidase, excluding specific product numbers, providing guidelines for accurate cholesterol oxidase assays.

Numer pozycji handlu globalnego

SKUNUMER GTIN
C1235-100UN04061833467190

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