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SOD (Mn) Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IP |
|---|---|
| Primary Accession | P04179 |
| Other Accession | NP_000627.2 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Chicken, Bovine, Xenopus, Dog, Sheep, Guinea Pig |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Human SOD (Mn) Polyclonal |
| Target/Specificity | Detects ~25kDa. |
| Other Names | Manganese SOD Antibody, IPO B Antibody, Mn SOD Antibody, SOD2 Antibody |
| Immunogen | Human Mn SOD |
| Purification | Protein A Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 0.2 µg/ml of SPC-118 was sufficient for detection of Mn SOD in 20 µg of rat brain tissue extract by colorimetric immunoblot analysis using Goat anti-mouse IgG:AP as the secondary antibody. |
| Cellular Localization | Mitochondrion | Mitochondrion Matrix |
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Provided below are standard protocols that you may find useful for product applications.
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 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 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 (7). 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. Furukawa Y., O’Halloran T. (2006). Antioxidants & Redo Signaling. Vol 8, No 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. Kurobe N., et al. (1990) Biomedical Research. 11: 187-194
7. Wispe J.R., et al. (1989) BBA. 994: 30-36.
8. Xiao-Hong Liu., et al. (1993) Brain Research. 625: 29-37.
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