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Cholesterol Oxidase from Streptomyces sp. Proteins Molecular Depot
Cholesterol Oxidase from Streptomyces sp. Proteins Molecular Depot

Cholesterol Oxidase from Streptomyces sp.

$387.00

    Catalog #: P2010002 – 250 U

    Cholestrerol Oxidase (250 U) consists of a highly purified powdered Cholesterol Oxidase enzyme, a flavoprotein involved in the first step of cholesterol catabolism. The enzyme first oxidizes cholesterol to cholest-5-en-3-one then isomerizes it to cholest-4-en-3-one while producing hydrogen peroxide H2O2. Custom bulk orders of this product are available upon request.

    Products are for in vitro research use only (RUO)

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Cholesterol Oxidase from Streptomyces sp.

Catalog # P2010002
Size 250 U
Molecular Weight 34 kDa
Reaction Catalyzed Cholesterol + O₂ → Cholest-4-en-3-one + H₂O₂
Unit Definition One enzymatic unit converts 1.0 μmol of cholesterol to 4-cholesten-3-one per min at pH 7.5 at 25 °C.
Specific Activity 21 U/mg
Storage -20°C. Avoid repeated freeze/thaw cycles.
Supplied as Yellow lyophilized powder (11.9 mg)
Application Assaying cholesterol
Keywords Cholesterol oxidase, cholesterol, flavoprotein

About Cholesterol Oxidase

Cholesterol oxidase belongs to the oxidoreductase family, acting specifically on the CH–OH functional group. Its systematic name is cholesterol:oxygen oxidoreductase, and it’s also referred to as cholesterol-O₂ oxidoreductase, 3β-hydroxy steroid oxidoreductase, and 3β-hydroxysteroid:oxygen oxidoreductase. It plays key roles in bile acid biosynthesis.

Cholesterol Oxidase from Streptomyces sp. is a high-purity flavoprotein enzyme used extensively in cholesterol quantification, biosensor development, and oxidative stress research. This enzyme catalyzes the oxidation of cholesterol to cholest-4-en-3-one with the concurrent production of hydrogen peroxide, a reaction that serves as the basis for many colorimetric and fluorometric assays. With a molecular weight of 34 kDa and a specific activity of 21 U/mg, this reagent is supplied as a yellow lyophilized powder and retains high enzymatic integrity when stored at –20°C.

Researchers in clinical diagnostics, lipid metabolism, and microbial biotransformation rely on cholesterol oxidase for its precision and reproducibility. Its ability to generate H₂O₂ as a measurable byproduct makes it ideal for coupling with peroxidase-based detection systems. The enzyme’s activity at physiological pH (7.5) and temperature (25°C) ensures compatibility with standard assay conditions. Additionally, its role in bile acid biosynthesis and steroid transformation has made it a valuable tool in both basic and applied biosciences. Whether you're developing a cholesterol biosensor, studying membrane dynamics, or screening for cholesterol-modulating compounds, this enzyme offers robust performance across a wide range of experimental platforms.

Key benefits:

  • Oxidizes cholesterol to cholest-4-en-3-one with H₂O₂ generation

  • Specific activity of 21 U/mg and molecular weight of 34 kDa

  • Ideal for cholesterol assays, biosensors, and oxidative stress studies

  • Active at pH 7.5 and 25°C for compatibility with standard protocols

  • Supplied as a stable lyophilized powder for long-term storage

Products are for in vitro research use only (RUO).

References Related to Cholesterol Oxidase from Streptomyces sp.

  • Kreit, J., Sampson, N. S. (2009). Cholesterol oxidase: physiological functions. FEBS Journal, 276(23), 6844–6856.
  • Vrielink, A., and Ghisla, S. (2009). Cholesterol oxidase: biochemistry and structural features. FEBS Journal, 276(23), 6826–6843.
  • Vrielink, A. (2010). Cholesterol Oxidase: Structure and Function. Cholesterol Binding and Cholesterol Transport Proteins: Subcellular Biochemistry, 137–158.
  • Niwas, R., Singh, V., Singh, R., Pant, G., Mitra, K., and Tripathi, C. K. M. (2014). Cholesterol oxidase production from entrapped cells of Streptomyces sp. Journal of Basic Microbiology, 54(11), 1233–1239.
  • Pollegioni, L. (2009). Cholesterol oxidase: a model flavoprotein oxidase and a biotechnological tool. FEBS Journal, 276(23), 6825–6825.
  • Olivares-Rubio HF, Salazar-Coria L, Romero-López JP, Domínguez-López ML, García-Latorre EA, Vega-López A. Fatty acid metabolism and brain mitochondrial performance of juvenile Nile tilapia (Oreochromis niloticus) exposed to the water-accommodated fraction of Maya crude oil. Ecotoxicol Environ Saf. 2020 Apr 14;197:110624.
  • El-Naggar NE, El-Shweihy NM. Identification of cholesterol-assimilating actinomycetes strain and application of statistical modeling approaches for improvement of cholesterol oxidase production by Streptomyces anulatus strain NEAE-94. BMC Microbiol. 2020 Apr 10;20(1):86.

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Product Resources:

Manual Manual
Brochure Brochure

Copy of Technical Specifications

FeatureDetails
Viewing Head Siedentopf type trinocular head, inclined at 30°, Interpupillary adjustment 53mm to 75mm, graduated diopter on left eyetube (30mm I.D. eyetubes)
Eyepieces SWH10X Widefield high eyepoint eyepiece, Field No. 22, tube O.D. 30.0 mm
Nosepiece Quintuple
Quintuple LWD Planachromat Phase 10x, 20x
Condenser TC Condenser N.A. 0.30, W.D. 73.0mm
Stage180mm(X) x 245mm(Y) plain stage with replaceable glass insert with 45mm opening, Glass Stage plate insert
IlluminationKoehler without iris, with phase slider, 3W LED
WarrantyLIMITED LIFETIME WARRANTY

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