anti-Superoxide Dismutase 1, mAb (72B1)

Product description: Monoclonal Antibody. Recognizes the Human protein. Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol. 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). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. 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. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. 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 radicals which are normally produced within the cells and which are toxic to biological systems.

Alternate Names/Synonyms: SOD1; hSod1; EC=1.15.1.1; Superoxide Dismutase 1; Superoxide Dismutase [Cu-Zn]

Product Type: Monoclonal Antibody

Clone: 72B1

Isotype: Mouse IgG1 kappa

Immunogen: Recombinant human protein purified from E. coli.

Applications: IP

Species Crossreactivity: Human

Formulation: Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.

Short Term Storage: +4°C

Long Term Storage: -20°C

Shipping: BLUE ICE

Use & Stability: Stable for at least 1 year after receipt when stored at -20°C.

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Literature References: 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)