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A0157

Sigma-Aldrich

Ascorbate Oxidase from Cucurbita sp.

lyophilized powder, 1,000-3,000 units/mg protein

Synonym(s):

L-Ascorbate:oxygen oxidoreductase, Ascorbase

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About This Item

CAS Number:
9029-44-1
Enzyme Commission number:
1.10.3.3 (BRENDA, IUBMB)
EC Number:
232-852-6
MDL number:
MFCD00130560
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

plant (Cucurbita spp.)

Quality Level

200

form

lyophilized powder

specific activity

1,000-3,000 units/mg protein

storage temp.

2-8°C

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General description

Ascorbate oxidase is a homodimeric enzyme, which comprises 552 amino acid residues per subunit (zucchini). It corresponds to a molecular mass of 70kDa per subunit. This enzyme is mainly found in plants, fungi and eubacteria.

Application

Ascorbate Oxidase from Cucurbita sp. has been used:
  • as a supplement in the culture medium for differentiation into osteoblasts
  • to oxidize ascorbic acid producing monodehydroascorbate in monodehydroascorbate reductase assay
  • in determining ascorbate (AsA) and dehydroascorbate (DHA) concentrations

Ascorbate oxidase, from Cucurbita sp., may be used to study oxidative stress and heat stress response and tolerance. Ascorbate oxidase, from Sigma, has been used in ascorbic acid assays to study the heat stress response of Arabidopsis .

Biochem/physiol Actions

Ascorbate oxidase (AO) participates in cell growth by regulating reduction/oxidation (redox) of the apoplast. This enzyme can synthesize the oxidative molecule dehydroascorbate acid (DHA) in the apoplast. It is also involved in cell elongation and enlargement development.
Ascorbate oxidase converts ascorbic acid to dehydroascorbic acid. It is highly specific for L-ascorbic acid and a few analogs. Ascorbate oxidase exists as a dimer and has a molecular weight of approximately 140 kDa.

Unit Definition

One unit will oxidize 1.0 μmole of L-ascorbate to dehydroascorbate per min at pH 5.6 at 25 °C.

Physical form

Lyophilized powder containing buffers and sucrose as stabilizer.

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

A0157-BULK:
A0157-1KU-PW:
A0157-100UN-PW:
A0157-250UN:
A0157-100UN:
A0157-1KU:
A0157-VAR:
A0157-250UN-PW:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Manuel A Matamoros et al.
Journal of experimental botany, 61(1), 87-97 (2009-10-14)
In plant cells, antioxidants keep reactive oxygen species at low concentrations, avoiding oxidative damage while allowing them to play crucial functions in signal transduction. However, little is known about the role of antioxidants during fruit maturation, especially in legumes. Snap
Cotton ascorbate oxidase promotes cell growth in cultured tobacco bright yellow-2 cells through generation of apoplast oxidation
Li R, et al.
International Journal of Molecular Sciences, 18(7), 1346-1346 (2017)
Ethylene response factor 6 is a regulator of reactive oxygen species signaling in Arabidopsis
Sewelam N, et al.
PLoS ONE, 8(8), e70289-e70289 (2013)
Cécile Garchery et al.
Plant, cell & environment, 36(1), 159-175 (2012-06-26)
The regulation of carbon allocation between photosynthetic source leaves and sink tissues in response to stress is an important factor controlling plant yield. Ascorbate oxidase is an apoplastic enzyme, which controls the redox state of the apoplastic ascorbate pool. RNA
A Messerschmidt et al.
Journal of molecular biology, 224(1), 179-205 (1992-03-05)
The crystal structure of the fully oxidized form of ascorbate oxidase (EC 1.10.3.3) from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution, using an energy-restrained least-squares refinement procedure. The refined model, which includes 8764 protein
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