Superoxide Dismutase from bovine erythrocytes
SIGMA/S5395 - BioReagent, ≥3,000 units/mg protein, suitable for cell culture, lyophilized powder
Synonym: SOD; Superoxide: superoxide oxidoreductase
CAS Number: 9054-89-1
EC Number: 232-943-0
MDL Number: MFCD00132404
Product Type: Chemical
SOD from bovine erythrocytes is a homodimeric non-covalently bound protein with two 16.3 kDa subunits of 151 amino acids. Each monomer has one intrachain disulfide and one free sulfhydryl, two copper atoms and two zinc atoms.
Multiple enzymatic scavengers are utilized by the cell to limit damage from reactive oxygen species. These scavengers include members of the superoxide dismutase (SOD) family, catalase, and glutathione peroxidase.
SOD catalyzes the conversion of superoxide radicals into hydrogen peroxide and molecular oxygen.
| biological source | bovine erythrocytes |
| form | lyophilized powder |
| mol wt | 32.5 kDa |
| packaging | pkg of 15000 units |
| pH | 7.6-10.5 |
| product line | BioReagent |
| Quality Level | 200  |
| shipped in | dry ice |
| specific activity | ≥3,000 units/mg protein |
| storage temp. | −20°C |
| technique(s) | cell culture | mammalian: suitable |
| Analysis Note: | For assay method, see McCord, J.M. and Fridovich,I., J. Biol. Chem., 244, 6049 (1969). |
| 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 |
| Biochem/physiol Actions: | 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. |
| General description: | 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. |
| Other Notes: | 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. |
| Packaging: | 15000 units in glass bottle |
| Packaging: | 30000, 75000 units in poly bottle |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 3 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥3,000 units/mg protein |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 1.15.1.1 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |