S9636

Superoxide Dismutase from human erythrocytes

essentially salt-free, lyophilized powder, ≥2,500 units/mg protein

• Synonyme(s) : SOD, Superoxide: superoxide oxidoreductase
• 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.54

Propriétés

• Source biologique: human erythrocytes
• Niveau de qualité: 400
• Pureté: >80% protein (biuret)
• Forme: essentially salt-free, lyophilized powder
• Activité spécifique: ≥2,500 units/mg protein
• Poids mol.: 32.0 kDa
• Composition: Protein, ≥80% biuret
• Fabricant/nom de marque: Sigma-Aldrich
• Technique(s): activity assay: suitable
• Couleur: white to off-white
• Plage de pH: 7.6—10.5
• pH: 7.8
• Adéquation: suitable for molecular biology
• Numéro d'accès UniProt: P00441; P04179; P08294
• Application(s): life science and biopharma
• Température de stockage: −20°C
• Informations sur le gène: human ... SOD1(6647) , SOD2(6648) , SOD3(6649)

Description

Description générale

Superoxide dismutases (SOD) are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals and micro-organisms. Three forms of SOD exist, based on the metal ions in the active site. These are Cu²⁺/Zn²⁺, Mn²⁺ and Fe²⁺ containing SOD. In vertebrate organisms, Cu/Zn-SOD is located in the cytoplasm as well as the mitochondrial intermembrane space, whereas Mn-SOD is located at the mitochondrial matrix space in prokaryotes. Fe-SOD is also found in prokaryotes and higher plants. Human erythrocyte SOD is a non-covalently bound homodimeric protein with two 16.3 kDa subunits containing 153 amino acids. Each dimer consists of two Cu²⁺ atoms and two Zn²⁺ atoms.

Application

Superoxide Dismutase from human erythrocytes has been used:

• to test its effect on human neutrophils in reactive oxygen species (ROS) measurement studies involving Pseudomonas aeruginosa infection
• as an antioxidant to test its effect on ROS generation induced by atmospheric-pressure plasma jet (APPJ) in red blood cell (RBC) homogenates using optical spectroscopy studies
• to test its attenuating effect on hemoglobin (Hb)-induced nuclear factor-kappa B (NF- κB) and hypoxia-inducible factor (HIF) activity in human dermal microvascular endothelial cells (HMECs-1)
• as a reference antioxidant protein to examine its expression in human intestinal Caco-2 cells following treatment with dietary flavonoids
• in combination with catalase to promote cell differentiation in vitro

Actions biochimiques/physiologiques

Mutations in the SOD1 gene are implicated in Amyotrophic lateral sclerosis (ALS).

Catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. 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).

Informations sur la sécurité

• Pictogrammes: 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)