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S5395

Sigma-Aldrich

Superoxide Dismutase from bovine erythrocytes

BioReagent, ≥3,000 units/mg protein, lyophilized powder, suitable for cell culture

Synonyme(s) :

SOD, Superoxide: superoxide oxidoreductase

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About This Item

Numéro CAS:
9054-89-1
Numéro de classification (Commission des enzymes):
1.15.1.1 (BRENDA, IUBMB)
Numéro CE :
232-943-0
Numéro MDL:
MFCD00132404
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.75

Source biologique

bovine erythrocytes

Gamme de produits

BioReagent

Forme

lyophilized powder

Activité spécifique

≥3,000 units/mg protein

Poids mol.

32.5 kDa

Conditionnement

pkg of 15000 units

Technique(s)

cell culture | mammalian: suitable

pH

7.6-10.5

Conditions d'expédition

dry ice

Température de stockage

−20°C

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Description générale

Superoxide Dismutase from bovine erythrocytes is a metalloprotein which disproportionates superoxide anion radicals. It is a 31.5 kDa copper binding protein and displays a conserved domain and fold. It is a homodimer with one copper and zinc ion per subunit and has antiparallel “greek-key” β barrel fold.

Application

Superoxide Dismutase (SOD) from bovine erythrocytes has been used:
  • for measuring the superoxide radical using the electron paramagnetic resonance spin in human brain microvascular endothelial cells
  • for measuring superoxide production in cytochrome C assay in peripheral blood mononuclear cells
  • as a standard in characterization of hen egg SOD using Fourier-transform infrared spectroscopy (FTIR) and matrix-assisted laser desorption/ionization (MALDI) analysis

Actions biochimiques/physiologiques

Superoxide Dismutase from bovine erythrocytes catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. It serves as an antioxidant and 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.

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.

Remarque sur l'analyse

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

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

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)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Chunxia Xiao et al.
PloS one, 7(1), e30343-e30343 (2012-01-25)
The C57BLKS/J db/db (db/db) mouse is a widely used type 2 diabetic animal model, and this model develops early inner retinal neuronal dysfunction beginning at 24 weeks. The neural mechanisms that mediate early stage retinal dysfunction in this model are
Zoe Loomis et al.
PloS one, 12(2), e0171219-e0171219 (2017-02-06)
It is now well established that both inherited and acquired forms of hemolytic disease can promote pulmonary vascular disease consequent of free hemoglobin (Hb) induced NO scavenging, elevations in reactive oxygen species and lipid peroxidation. It has recently been reported
Partial biochemical characterization of Cu, Zn-superoxide dismutase extracted from eggs of hens (Gallus gallus domesticus)
Wawrzykowski J and Kankofer M
Food Chemistry, 227, 390-396 (2017)
human cystic fibrosis macrophages have defective calcium-dependent protein kinase C activation of the NADPH oxidase, an effect augmented by Burkholderia cenocepacia
Assani K, et al.
Journal of immunology (Baltimore, Md. : 1950), 198(5), 1985-1994 (2017)
Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15
Hough MA and Hasnain SS
Structure, 11(8), 937-946 (2003)
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Protocoles

Enzymatic Assay of Superoxide Dismutase

Enzymatic Assay of Superoxide Dismutase

HPLC Analysis of Superoxide Dismutase on Discovery® BIO PolyMA-WAX

Separation of Superoxide dismutase

Chromatograms

application for HPLC

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