Összes fotó(1)
Fontos dokumentumok
C8868
Cholesterol Oxidase from microorganisms
lyophilized powder, ≥50 units/mg protein, recombinant, expressed in E. coli
Szinonimák:
Cholesterol: oxygen oxidoreductase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
Javasolt termékek
rekombináns
expressed in E. coli
Minőségi szint
Forma
lyophilized powder
specifikus aktivitás
≥50 units/mg protein
molekulatömeg
64 kDa
összetétel
Protein, ≥15% biuret
tárolási hőmérséklet
−20°C
Alkalmazás
Cholesterol oxidase has been used in a study to demonstrate that microheterogeneity in hydrophobic-hydrophilic block copolymer systems can be exploited for immobilizing enzymes and to carry out enzymatic reactions. Cholesterol oxidase has also been used in a study that concluded that amphipaths that activate cholesterol might be useful in treating NPC disease.
Cholesterol oxidase is used to determine serum cholesterol. The enzyme also finds application in the microanalysis of steroids in food samples and in distinguishing 3-ketosteroids from 3β-hydroxysteroids. Transgenic plants expressing cholesterol oxidase are being investigated in the fight against the cotton boll weevil. CHOD has also been used as a molecular probe to elucidate cellular membrane structures.
Biokémiai/fiziológiai hatások
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, which is then isomerized to cholest-4-en-3-one with the release of H2O2.
Fizikai tulajdonságok
Type II cholesterol oxidase containing FAD cofactor covalently linked to the enzyme.
Egység definíció
One unit will convert 1.0 μmole of cholesterol to 4-cholesten-3-one per min at pH 7.5 at 25 °C. Note: 4-cholesten-3-one may undergo isomerization.
Fizikai forma
Supplied as a lyophilzed powder containing sucrose
Figyelmeztetés
Danger
Figyelmeztető mondatok
Óvintézkedésre vonatkozó mondatok
Veszélyességi osztályok
Resp. Sens. 1
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 3
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Egyéni védőeszköz
Eyeshields, Gloves, type N95 (US)
Válasszon a legfrissebb verziók közül:
Analitikai tanúsítványok (COA)
Lot/Batch Number
Nem találja a megfelelő verziót?
Ha egy adott verzióra van szüksége, a tétel- vagy cikkszám alapján rákereshet egy adott tanúsítványra.
Már rendelkezik ezzel a termékkel?
Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Az ügyfelek ezeket is megtekintették
Block copolymer microdomains: a novel medium for enzymatic reactions
Gupte, A., et al.
Biotechnology Progress, 7, 348-354 (2012)
Meihe Zhang et al.
Biosensors & bioelectronics, 32(1), 288-292 (2011-12-31)
A novel cholesterol biosensor was prepared based on gold nanoparticles-catalyzed luminol electrogenerated chemiluminescence (ECL). Firstly, l-cysteine-reduced graphene oxide composites were modified on the surface of a glassy carbon electrode. Then, gold nanoparticles (AuNPs) were self-assembled on it. Subsequently, cholesterol oxidase
Laura Caldinelli et al.
The Journal of biological chemistry, 280(24), 22572-22581 (2005-04-09)
Cholesterol oxidase from Brevibacterium sterolicum is a monomeric flavoenzyme catalyzing the oxidation and isomerization of cholesterol to cholest-4-en-3-one. This protein is a class II cholesterol oxidases, with the FAD cofactor covalently linked to the enzyme through the His(69) residue. In
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
Protocols
Enzymatic activity assay for cholesterol oxidase, excluding specific product numbers, providing guidelines for accurate cholesterol oxidase assays.
Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.
Lépjen kapcsolatba a szaktanácsadással