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Key Documents

S8160

Sigma-Aldrich

Superoxide Dismutase from bovine liver

lyophilized powder, ≥1500 units/mg protein

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

lyophilized powder

Activité spécifique

≥1500 units/mg protein

Poids mol.

32.5 kDa

Composition

Protein, ≥70% biuret

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

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Description générale

Research area: Cell signalingSuperoxide Dismutase (SOD), a low molecular weight protein that is found in all aerobic cells of microorganisms, plants, and animals. It exists as three distinct families such as manganese SOD, copper–zinc SOD, and extracellular SOD.

Application

Superoxide dismutase from bovine liver has been used in a study to determine that hypercholesterolemia increases endothelial superoxide anion production. Superoxide dismutase from bovine liver has also been used in a study to investigate diazo coupling, subunit interactions, and electrophoretic variants of bovine erythrocyte superoxide dismutase. It has also been used as a component of the assay buffer in thequantification of reactive oxygen species (ROS) by O2k fluorometry.

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

Lyophilized powder containing potassium phosphate buffer salts

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, type N95 (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

S D Yan et al.
The Journal of biological chemistry, 269(13), 9889-9897 (1994-04-01)
Attack by reactive oxygen intermediates, common to many kinds of cell/tissue injury, has been implicated in the development of diabetic and other vascular diseases. Such oxygen-free radicals can be generated by advanced glycation end products (AGEs), which are nonenzymatically glycated
Bovine erythrocyte superoxide dismutase: diazo coupling, subunit interactions, and electrophoretic variants.
D P Malinowski et al.
Biochemistry, 18(1), 237-244 (1979-01-09)
Y Ohara et al.
The Journal of clinical investigation, 91(6), 2546-2551 (1993-06-01)
Indirect evidence suggests accelerated degradation of endothelium-derived nitric oxide (ENDO) by superoxide anion (O2-) in hypercholesterolemic vessels (HV). To directly measure O2- production by normal vessels (NV) and HV, we used an assay for O2- based on the chemiluminescence (CL)
Luciana Cacciottola et al.
Fertility and sterility, 110(3), 534-544 (2018-07-02)
To characterize oxidative stress and metabolic activity in xenografted human ovarian tissue using microdialysis. Prospective experimental study. Gynecology research unit at a university hospital. Cryopreserved ovarian cortex from five women 27-35 years of age. Frozen-thawed human ovarian tissue fragments were xenografted
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

Protocoles

Enzymatic Assay of Superoxide Dismutase

Chromatograms

application for HPLC

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