Recombinant Human SOD1/Cu-Zn SOD His (N-Term) Protein

This lyophilized preparation is stable for 12 months from date of receipt at -20 to -70 degrees C, preferably desiccated. Upon reconstitution, the preparation can be stored for 1 month at 2-8 degrees C under sterile conditions, and for 3 months at -20 degrees C to -70 degrees C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Stock solutions should be aliquoted and stored at < -20 degrees C. Further dilutions should be made in appropriate buffered solutions

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/SOD1), mitochondrial manganese SOD (Mn SOD/SOD2) and extracellular Cu, Zn SOD (EC SOD/SOD3). 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 chaperon 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. Superoxide dismutase recognizes copper/zinc superoxide dismutase (SOD). Superoxide dismutases are ubiquitous metalloproteins that destroy oxygen-mediated free radicals, that are normally produced within the cells, which are toxic to biological systems. There are three forms of superoxide dismutase, including the Fe, mitochondrial (Mn) and the copper/zinc binding (Cu/Zn) form. The Cu/Zn form of SOD is utilised by most eukaryotic organisms. SOD Cu/Zn prevents oxygen-mediated free radical damage by catalysing the dismutation of the toxic superoxide radical to molecular oxygen and hydrogen peroxide.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Array NBP2-34942

• SOD1/Cu-Zn SOD Antibodies
• SOD1/Cu-Zn SOD Antibody Pair
• SOD1/Cu-Zn SOD ELISA Kits
• SOD1/Cu-Zn SOD Lysate
• SOD1/Cu-Zn SOD Proteins