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Cat. Number

069849704658486

Chemical Name

Mn SOD (human) Polyclonal Antibody

References

Synonyms	Manganese Superoxide Dimutase
Formula Weight	25.0
Formulation	Affinity-purified antibody at 1 mg/ml in PBS, pH 7.0, containing 0.1% sodium azide and 50% glycerol
Stability	1 year
Storage	-20°C
Shipping	Wet ice in continental US; may vary elsewhere

Background Reading

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).

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).

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

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).

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Size	Global Purchasing
25 µL
100 µL

Description

Antigen: human Mn SOD · Host: rabbit · Application(s): WB, IP, and IHC · Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body.¹ It catalyzes the dismutation of the superoxide radical O₂- to O₂ and H₂O₂.^2,3 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.⁴ SOD3 can also be distinguished by its heparin-binding capacity.⁵

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 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).

5 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).

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