Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body. It works by catalyzing the dismutation of the superoxide radical O2 to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase. In general, SODs play a major role in antioxidant defense mechanisms. There are two main types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16kD each are linked by two cysteines forming an intra-subunit disulphide bridge. The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80kD. The third form (SOD3 or EC- SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30kD and it exists only in the extracellular space. SOD3 can also be distinguished by its heparin-binding capacity. Protein, HIS-tagged, without transit, rat recombinant made in E. coli, GeneBank Accession Number: BC070913 Cellular Localization: Mitochondrion matrix Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilutions: Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing.. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
