Antigen: human Cu/Zn SOD · Host: rabbit · Application(s): WB, IP, EIA, and IHC · Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body.¹ 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.^2,3 In general, SODs play a major role in antioxidant defense mechanisms.⁴ 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 16 kDa each are linked by two cystines forming an intra-subunit disulphide bridge.¹ The second form, SOD2, is a manganese-containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. 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 30 kDa and it exists only in the extra-cellular space.⁵ SOD3 can also be distinguished by its heparin-binding capacity.⁶

1 Furukawa, Y., and O'Halloran, T.V. Posttranslational modifications in Cu,Zn^-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. Antioxid Redox Signal 8(5-6) 847-867 (2006).

2 Bannister, J.V., Bannister, W.H., and Rotilio, G. Aspects of the structure, function, and applications of superoxide dismutase. Crit Rev Biochem Mol Biol 22(2) 111-180 (1987).

3 Hassan, H.M. Biosynthesis and regulation of superoxide dismutases. Free Radic Biol Med 5(5-6) 377-385 (1988).

4 Gao, B., Flores, S.C., Leff, J.A., et al. Synthesis and anti-inflammatory activity of a chimeric recombinant superoxide dismutase: SOD2/3. Am J Physiol Lung Cell Mol Physiol 284 L917-L925 (2003).

5 Wispé, J.R., Clark, J.C., Burhans, M.S., et al. Synthesis and processing of the precursor for human mangano-superoxide dismutase. Biochim Biophys Acta 994(1) 30-36 (1989).

6 Adachi, T., Ohta, H., Yamada, H., et al. Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody. Clin Chim Acta 212(3) 89-102 (1992).

Wispé, J.R., Clark, J.C., Burhans, M.S., et al. Synthesis and processing of the precursor for human mangano-superoxide dismutase. Biochim Biophys Acta 994(1) 30-36 (1989).

Shinder, G.A., Lacourse, M., Minotti, S., et al. Mutant Cu/Zn^-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis. J Biol Chem 276(16) 12791-12796 (2001).

Bannister, J.V., Bannister, W.H., and Rotilio, G. Aspects of the structure, function, and applications of superoxide dismutase. Crit Rev Biochem Mol Biol 22(2) 111-180 (1987).

Adachi, T., Ohta, H., Yamada, H., et al. Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody. Clin Chim Acta 212(3) 89-102 (1992).

Gao, B., Flores, S.C., Leff, J.A., et al. Synthesis and anti-inflammatory activity of a chimeric recombinant superoxide dismutase: SOD2/3. Am J Physiol Lung Cell Mol Physiol 284 L917-L925 (2003).

Hassan, H.M. Biosynthesis and regulation of superoxide dismutases. Free Radic Biol Med 5(5-6) 377-385 (1988).

Furukawa, Y., and O'Halloran, T.V. Posttranslational modifications in Cu,Zn^-superoxide dismutase and mutations associated with amyotrophic lateral sclerosis. Antioxid Redox Signal 8(5-6) 847-867 (2006).

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