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S8409

Sigma-Aldrich

Superoxide Dismutase from bovine liver

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

Synonyme(s) :

SOD, Superoxide: superoxide oxidoreductase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Forme

ammonium sulfate suspension

Niveau de qualité

Activité spécifique

2,000-6,000 units/mg protein (biuret)

Poids mol.

32.5 kDa

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

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Description générale

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

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

Remarque sur l'analyse

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

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Perturbed redox signaling exacerbates a mitochondrial myopathy
Dogan SA, et al.
Cell Metabolism, 28(5), 764-775 (2018)
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)
L G Chi et al.
Circulation research, 64(4), 665-675 (1989-04-01)
Available data demonstrate that oxygen free radicals and derived reactive species of oxygen are produced during myocardial ischemia as well as upon reperfusion of the ischemic tissue. The present study was designed to determine if polyethylene glycol-conjugated superoxide dismutase (PEG-SOD)
Naoya Ichimaru et al.
Biochemistry, 47(40), 10816-10826 (2008-09-11)
The mode of action of Deltalac-acetogenins, strong inhibitors of bovine heart mitochondrial complex I, is different from that of traditional inhibitors such as rotenone and piericidin A [Murai, M., et al. (2007) Biochemistry 46 , 6409-6416]. As further exploration of

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