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anti-Superoxide Dismutase 1, pAb

YIF-LF-PA0013 100 µl INQ
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Additional Information

Product Data
Synonyms SOD1; hSod1; EC=1.15.1.1; Superoxide Dismutase 1; Superoxide Dismutase [Cu-Zn]
Properties
Immunogen/Antigen Recombinant human protein purified from E. coli.
Application Western Blot (1:2,000)
Immunoprecipitation (1 μl)
IHC-P
Crossreactivity Human, Mouse, Rat
Purity Detail Protein A purified.
Concentration 0.5 mg/ml
Formulation 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.
Origin Manufactured by AbFrontier
Product Type Polyclonal Antibody
Shipping and Handling
Shipping BLUE ICE
Short Term Storage +4°C
Long Term Storage -20°C
Use/Stability Stable for at least 1 year after receipt when stored at -20°C.

Product Description

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. Destroys radicals which are normally produced within the cells and which are toxic to biological systems.

Product 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)
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