Skip to Content
Merck
All Photos(1)

Documents

S8409

Sigma-Aldrich

Superoxide Dismutase from bovine liver

ammonium sulfate suspension, 2,000-6,000 units/mg protein (biuret)

Synonym(s):

SOD, Superoxide: superoxide oxidoreductase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

ammonium sulfate suspension

specific activity

2,000-6,000 units/mg protein (biuret)

mol wt

32.5 kDa

UniProt accession no.

storage temp.

2-8°C

Gene Information

Looking for similar products? Visit Product Comparison Guide

General description

Research area: Cell Signaling

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 bovine liver has been used:


  • for measuring mitochondrial hydrogen peroxide production in skeletal muscle
  • as a positive control in Cu(II) binding stability assay
  • as a positive control in superoxide dismutase assay
  • in a study to assess the inactivation of endothelial-derived relaxing factor by oxidized lipoproteins.
  • in a study to investigate the role of hydrogen peroxide in the cytotoxicity of the xanthine/xanthine oxidase system.

Biochem/physiol Actions

Superoxide Dismutase catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It plays a critical role in the defense of cells against the toxic effects of oxygen radicals. It 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

Suspension in 3.8 M (NH4)2SO4, pH 7.0

Analysis Note

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

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Perturbed redox signaling exacerbates a mitochondrial myopathy
Dogan SA, et al.
Cell Metabolism, 28(5), 764-775 (2018)
Molybdenum application enhances antioxidant enzyme activity and COR15a protein expression under cold stress in wheat
Al-Issawi M, et al.
Journal of Plant Interactions, 11(1), 5-10 (2016)
J H Chin et al.
The Journal of clinical investigation, 89(1), 10-18 (1992-01-01)
Endothelial cell derived relaxing factor (EDRF) mediated relaxation of blood vessels is impaired in vessels exposed to lipoproteins in vitro and in arteries of hyperlipidemic humans and animals. To investigate the mechanism by which lipoproteins impair the effects of EDRF
E M Link et al.
The Biochemical journal, 249(2), 391-399 (1988-01-15)
1. The survival of mammalian epithelial cells exposed in vitro to the xanthine/xanthine oxidase system in phosphate-buffered saline (PBS) or serum-containing medium (SCMEM) was investigated. 2. The cytotoxic effect observed depended on the composition of the medium in which the
Exploiting the vulnerable active site of a copper-only superoxide dismutase to disrupt fungal pathogenesis
Robinett NG, et al.
The Journal of Biological Chemistry, jbc-RA118 (2018)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service