Product Name :
Superoxide Dismutase 4, Human
Product Type :
Protein
Lot No :
PJN04
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
Form :
Lyophilized
Purity :
> 95% by SDS-PAGE
Expression system :
E.coli
Tag :
None
Origin :
Human
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 :
ROS Signaling 
Database link - SwissProt no.
O14618

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