S9697
Superoxide Dismutase bovine
recombinant, expressed in E. coli, lyophilized powder, ≥2500 units/mg protein, ≥90% (SDS-PAGE)
Synonyme(s) :
Superoxide Dismutase 1 bovine, cytocuprein, erythrocuprein, hemocuprein, CU/ZN-SOD, SOD, SOD1, Superoxide: superoxide oxidoreductase
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About This Item
Produits recommandés
Source biologique
bovine
Niveau de qualité
Produit recombinant
expressed in E. coli
Pureté
≥90% (SDS-PAGE)
Forme
lyophilized powder
Activité spécifique
≥2500 units/mg protein
Conditions de stockage
(Tightly closed)
Technique(s)
inhibition assay: suitable
Couleur
white
pH optimal
7.8 (25 °C)
Plage de pH
7.6-10.5
pl
4.95
Remarque sur la séquence
MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK
Numéro d'accès UniProt
Température de stockage
−20°C
Description générale
Research area: Cell Signaling
SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. There are three forms of SOD differentiated by the metal ions in the active site. These are Cu+2/Zn+2, Mn+2, and Fe+2 SOD. In vertebrates, Cu/Zn-SOD is found in the cytoplasm, chloroplast, and may be in extracellular space, while Mn-SOD is found in the mitochondrial matrix space and peroxisome. Fe-SOD is found in the chloroplast of prokaryotes and some higher plants.
SOD from bovine erythrocytes was the first SOD to be found in mammalian tissues. There are three forms of SOD differentiated by the metal ions in the active site. These are Cu+2/Zn+2, Mn+2, and Fe+2 SOD. In vertebrates, Cu/Zn-SOD is found in the cytoplasm, chloroplast, and may be in extracellular space, while Mn-SOD is found in the mitochondrial matrix space and peroxisome. Fe-SOD is found in the chloroplast of prokaryotes and some higher plants.
Application
Superoxide Dismutase bovine has been used:
- to construct a calibration curve for the evaluation of superoxide dismutase (SOD) enzyme activities
- in a study to investigate where lipoproteins may affect the L-arginine-nitric oxide pathway
- in a study to investigate the mass spectral evidence for carbonate-anion-radical-induced posttranslational modification of tryptophan to kynurenine in human Cu, Zn superoxide dismutase
Actions biochimiques/physiologiques
Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. This reaction in turn activates redox-sensitive kinases and inactivates specific phosphatases to regulate redox-sensitive signaling pathway, including hypertrophy, proliferation, and migration. SOD serves as a potent antioxidant and protects the cells against the toxic effects of oxygen radicals. SOD may also suppress apoptosis by competing with nitric oxide (NO) for superoxide anion, which reacts with NO to form peroxynitrite, an inducer of apoptosis.
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.
Notes préparatoires
Produced using animal component-free materials.
Reconstitution
Reconstitute in 10 mM potassium phosphate, pH 7.4.
Remarque sur l'analyse
Extinction coefficient: EmM= 10.3 (258 nM)
SOD has no significant absorbance peak at 280 nM because of the absence of tryptophan.
SOD has no significant absorbance peak at 280 nM because of the absence of tryptophan.
Autres remarques
Inhibitors: cyanide, OH- (competitive), hydrogen peroxide
Anticorps
Produit(s) apparenté(s)
Réf. du produit
Description
Tarif
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
Certificats d'analyse (COA)
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