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Superoxide Dismutase 1 (human) (rec.)
Product Details | |
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Synonyms | SOD1; hSod1; EC=1.15.1.1; Superoxide Dismutase 1; Superoxide Dismutase [Cu-Zn] |
Product Type | Protein |
Properties | |
Source/Host | E. coli |
Crossreactivity | Human |
Biological Activity |
Enzymatic Activity has not been tested. |
Purity | ≥95% (SDS-PAGE) |
Formulation | Lyophilized from 20mM HEPES, pH 7.4. |
Other Product Data |
Click here for Original Manufacturer Product Datasheet |
Declaration | Manufactured by AbFrontier |
Shipping and Handling | |
Shipping | BLUE ICE |
Short Term Storage | +4°C |
Long Term Storage | -20°C |
Handling Advice | Avoid freeze/thaw cycles. |
Use/Stability | After reconstitution, store at -80°C. |
Documents | |
MSDS | Inquire |
Product Specification Sheet | |
Datasheet |
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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.
1) Kuninaka, S. et al. (2000) Br. J. Cancer. 83, 928-934. (General)
2) Strange, R. W. et al. (2003) J. Mol. Biol. 328, 877-891. (General)
3) Weisiger, R. A., and Fridovich, I. (1973) J. Biol. Chem. 248, 3582-3592. (General)
4) Enghild, J. J. et al. (1999) Biochem J. 317, 51-57. (General)