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S4636

Sigma-Aldrich

Superoxide Dismutase from horseradish

lyophilized powder, 1,000-4,000 units/mg protein

Synonym(s):

SOD, Superoxide: superoxide oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204

form

lyophilized powder

specific activity

1,000-4,000 units/mg protein

composition

Protein, ≥70% biuret

storage temp.

−20°C

General description

Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. They provide protection against damaging reactions with the superoxide radical anion (O2-) by catalyzing its disproportionation into oxygen and hydrogen peroxide.

Application

Superoxide dismutase from horseradish has been used in a study to assess the correlation between CuZn superoxide dismutase and glutathione reductase, and environmental and xenobiotic stress tolerance in maize inbreds. Superoxide dismutase from horseradish has also been used in a study to investigate chemiluminometric enzyme sensors for flow-injection analysis.

Biochem/physiol Actions

Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. Plays a critical role in the defense of cells against the toxic effects of oxygen radicals. Competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice.

Unit Definition

One unit will inhibit reduction of cytochrome c by 50% in a coupled system with xanthine oxidase at pH 7.8 at 25 °C in a 3.0 mL reaction volume. Xanthine oxidase concentration should produce an initial ΔA550 of 0.025 ± 0.005 per min.

Physical form

Lyophilized powder containing potassium phosphate buffer salts

Analysis Note

For assay method, see McCord, J.M. and Fridovich, I., J. Biol. Chem., 244, 6049 (1969).

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Chemiluminometric enzyme sensors for flow-injection analysis
Spohn, U., et al.
Analytica Chimica Acta, 303, 109-120 (1995)
Correlation between CuZn superoxidedismutase and glutathione reductase, and environmental and xenobiotic stress tolerance in maize inbreds
Malan, C., et al.
Plant Science, 69, 157-166 (1990)
Characterisation by EPR spectroscopy of the co-ordination environment of copper in superoxide dismutase from horseradish (Armoracia rusticana Gaertn.)
Palivan, C., et al.
Proceedings of the Royal Society of Edinburgh. Section B: Biology, 102B, 273-277 (1994)
Ou-Yang Chao et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 68(1-2), 60-69 (2013-05-11)
We report cDNA cloning, expression, purification, and characterization of a novel Cu/ Zn superoxide dismutase (SOD) from Jatropha curcas leaves. The full-length cDNA of this SOD contained a 496-bp open-reading frame (ORF) encoding 162 amino acid residues. The recombinant plasmid
Raymond S W Tsang et al.
Canadian journal of microbiology, 59(5), 362-364 (2013-05-08)
Haemophilus influenzae serotype a (Hia) is an important pathogen since the introduction of vaccines for control of disease due to serotype b strains. Using a sodC-based polymerase chain reaction, Hia can be divided into 2 phylogenetic divisions, each with their

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