- Product Name :
- Superoxide Dismutase 4, Human
- Storage :
- Shipped at 4°C. Store at -20°C. After reconstitution, store at -80°C and avoid frequent freeze and thaw.
- Composition :
- Lyophilized from 20mM HEPES, pH 7.4
- Source :
- Purified from E.coli expressing the human Superoxide Dismutase 4 gene (1-274aa)
- Molecular Weight :
- 29 kDa
- Endotoxin activity :
- Not tested
- Purity :
- > 95% by SDS-PAGE
- Expression system :
- Background :
- Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu,Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
- Background reference :
- 1) Kuninaka, S. et al. (2000) Br. J. Cancer. 83, 928-934.
2) Strange, R. W. et al. (2003) J. Mol. Biol. 328, 877-891.
3) Weisiger, R. A., and Fridovich, I. (1973) J. Biol. Chem. 248, 3582-3592.
4) Enghild, J. J. et al. (1999) Biochem J. 317, 51-57.
- Research area :
- Database link - SwissProt no.
The test was performed by customers with their own sample.