Target: SOD3
Conjugate: ATTO 488
Product Type: Monoclonal
Clone Number: 4GG11G6
Immunogen: Human extracellular SOD purified from aortas
Swiss-Prot: P08294
Purification: Protein G Purified
Storage Buffer: PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Detects extracellular SOD ~35kDa.
Cellular Localization: Extracellular Space
Scientific Background: Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2ˉ to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4).There are three 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 cysteines forming an intra-subunit disulphide bridge (3). 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 (6). SOD3 can also be distinguished by its heparin-binding capacity (1).
References: 1. Adachi T., et al. (1992) Clin Chim Acta. 212: 89-102.2. Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111-180.3. FurukawaY., and O'Halloran T. (2006) Antioxidants & Redo Signaling. 8(5): 6.4. Gao B., et al. (2003) Am J Physiol Lung Cell Mol Physiol 284: L917-L925.5. Hassan H.M. (1988) Free Radical Biol. Med. 5: 377-385.6. Wispe J.R., et al. (1989) BBA. 994: 30-36.7. Regan, E. et al. (2005) Arthritis & Rheumatism 52(11): 3479–3491
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
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