Adipogen/anti-Superoxide Dismutase 2, mAb (2A1)/YIF-LF-MA0030/100 µl一抗
SOD2; EC=18.104.22.168; Superoxide Dismutase [Mn], Mitochondrial
Mouse IgG1 κ
Recombinant human protein purified from E. coli.
Western Blot (1:2,000)
Protein G purified.
Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.
Other Product Data
Click here for Original Manufacturer Product Datasheet
Our product description may differ slightly from the original manufacturers product datasheet.
Manufactured by AbFrontier
Shipping and Handling
Short Term Storage
Long Term Storage
Stable for at least 1 year after receipt when stored at -20°C.
Product Specification Sheet
Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide r
cal 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). SOD1 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). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 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. Destroys r
cals which are normally produced within the cells and which are toxic to
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)