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Ascorbate Oxidase Proteins Molecular Depot
Ascorbate Oxidase Proteins Molecular Depot

Ascorbate Oxidase

$275.00

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Ascorbate Oxidase (Microbial)

Catalog # P2010007
Size 1000 U
Unit Definition Oxidizes 1 µmol of ascorbate/min at 30 °C
Molecular Weight 80 kDa
Specific Activity 350 U/mg
Purity Uricase, phosphatase < 0.001%
Storage –20°C; avoid freeze/thaw cycles
Supplied as Light blue lyophilized powder
Keywords Ascorbate oxidase, L-ascorbic acid oxidase, ascorbic acid

Ascorbate Oxidase is a copper-containing enzyme that catalyzes the oxidation of L-ascorbic acid (vitamin C) to dehydroascorbate. This microbial-derived preparation is supplied as a light blue lyophilized powder and exhibits a specific activity of 350 U/mg, with a molecular weight of approximately 80 kDa. It is ideal for use in antioxidant assays, biosensor development, and redox biology research.

With a unit definition based on the oxidation of 1 µmol of ascorbate per minute at 30 °C, this enzyme is highly active and consistent across batches. Its purity (<0.001% uricase and phosphatase) ensures minimal interference in sensitive biochemical workflows. The product is stable at –20°C and should be reconstituted in sterile buffer for optimal performance. Researchers can use this enzyme to study oxidative stress, vitamin C metabolism, and enzymatic colorimetric reactions.

Key benefits:

  • Microbial source with high specific activity (350 U/mg)
  • Lyophilized format for long-term stability
  • Minimal contaminating enzymatic activity (<0.001%)
  • Supports redox biology and antioxidant research
  • Validated for colorimetric and biosensor applications

Indication for Use:
This product is for Research Use Only (RUO). It is not intended for human or animal use, diagnostic procedures, or therapeutic applications.

References:

  • Ferdinandusse S et al. ACOX2 deficiency and peroxisomal oxidase. BBA Mol Basis Dis. 2018;1864(3):952–958.
  • So CR et al. Oxidase activity in barnacle adhesive. ACS Appl Mater Interfaces. 2017;9(13):11493–11505.
  • Le TC et al. Zymographic oxidase activity determination. Methods Mol Biol. 2018;1853:207–221.
  • Le Laz S et al. Role of terminal oxidases in respiration. PLoS One. 2014;9(1):e86343.
  • Hakulinen N et al. Structure of catechol oxidase from Aspergillus. J Biol Inorg Chem. 2013;18(8):917–929.
  • Ignatov A et al. Immunoblot analysis of oxidase isozyme. Arch Biochem Biophys. 1997;347(2):208–212.
  • Yu Y et al. Tuning oxidase activity with unnatural tyrosine. J Am Chem Soc. 2015;137(14):4594–4597.

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    Product Use & Eligibility
    Products are for in vitro research use only (RUO). They are not intended for human or animal use, diagnosis, therapy, resale to consumers, or residential delivery. Sales are limited to verified business addresses.

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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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