Application
| WB, ICC |
|---|---|
| Primary Accession | P00441 |
| Other Accession | CAG46542 |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Clonality | Polyclonal |
| Description | Rabbit Anti-Human SOD1 (UbetaB) Polyclonal |
| Target/Specificity | Recognizes a conformation specific epitope where the beta barrel is unfolded. |
| Other Names | USOD Antibody, Superoxide dismutase 1 Antibody, SOD Antibody, SOD1 unfolded beta barrel region Antibody |
| Immunogen | N-terminal region of SOD1, unfolded beta barrel region |
| Purification | Protein A Purified |
| Storage | -20ºC |
| Storage Buffer | PBS, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 1 µg/ml of SPC-205 was sufficient for detection of the unfolded beta barrel of SOD1 by colorimetric dot blot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody. |
| Cellular Localization | Cytoplasm |
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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 (2). 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 (1,4). In general, SODs play a major role in antioxidant defense mechanisms (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 cysteines forming an intra-subunit disulphide bridge (2). Misfolding of SOD1 has been implicated in Amyotrophic lateral sclerosis (ALS). Therefore conformation specific antibodies such as Anti-SOD1 (UbetaB), which targets an unfolded region of the beta barrel of SOD1, are useful for determining the conformation of SOD1 in affected tissues (5). This antibody can be used in conjunction with Anti-SOD1 (EDI) (SPC-206D) which detects an exposed dimer interface (EDI) of SOD1.
References
1. Barrister J.V., et al. (1987). Crit. Rev. Biochem. 22:111-180.
2. Furukawa Y., and O’Halloran T. (2006) Antioxid Redox Signal. 8(5-6):847-67.
3. Gao B., et al. (2003) Am J Physiol Lung Cell Mol Physiol. 284:L917-L925.
4. Hassan H.M. (1988) Free Radical Biol. Med. 5:377-385.
5. Kerman A., et al. (2010) Acta Neuropathol. 119:335-344.