Superoxide Dismutase bovine
SIGMA/S9697 - recombinant, expressed in E. coli, lyophilized powder, ≥2500 units/mg protein, ≥90% (SDS-PAGE)
Synonym: Superoxide Dismutase 1 bovine; cytocuprein; erythrocuprein; hemocuprein; CU/ZN-SOD; SOD; SOD1; Superoxide: superoxide oxidoreductase
CAS Number: 9054-89-1
EC Number: 232-943-0
MDL Number: MFCD00132404
Product Type: Chemical
SOD catalyzes the conversion of superoxide radicals into hydrogen peroxide and molecular oxygen.
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.
SDS-PAGE Superoxide Dismutase bovine (Cat. No. S9697) was assessed on SDS-PAGE.
| assay | ≥90% (SDS-PAGE) |
| biological source | bovine |
| color | white |
| form | lyophilized powder |
| NCBI accession no. | NM_174615   |
| NP_777040 |
|
| optimum pH | 7.8 (25 °C) |
| pH range | 7.6-10.5 |
| pI | 4.95 |
| Quality Level | 200 |
| recombinant | expressed in E. coli |
| sequence note | MATKAVCVLKGDGPVQGTIHFEAKG |
| specific activity | ≥2500 units/mg protein |
| storage condition | (Tightly closed) |
| storage temp. | −20°C |
| technique(s) | inhibition assay: suitable |
| UniProt accession no. | A4URH1 |
| Analysis Note: | Extinction coefficient: EmM= 10.3 (258 nM) SOD has no significant absorbance peak at 280 nM because of the absence of tryptophan. |
| 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-i |
| Biochem/physiol Actions: | 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. |
| General description: | 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. |
| Other Notes: | Inhibitors: cyanide, OH- (competitive), hydrogen peroxide |
| 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, 300000 units in poly bottle |
| Preparation Note: | Produced using animal component-free materials. |
| Preparation Note: | Reconstitute in 10 mM potassium phosphate, pH 7.4. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 3 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | ≥90% (SDS-PAGE) |
| activity | specific activity: ≥2500 units/mg protein |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 1.15.1.1 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |