Rabbit anti-Cu/Zn SOD - SPC-115D
|Product Name ||SOD (Cu/Zn) Antibody|
|Catalog # ||SPC-115D|
|Package size ||100ug|
|Alternate Product Sizes ||SPC-115C|
|Datasheet ||SPC 115 Copper Zine Superoxide Dismutase (Cu Zn SOD) Oxidative Stress|
|Description ||Anti-Cu/Zn SOD|
|Research Area ||Oxidative Stress|
|Alternative Names ||Superoxide dismutase1, ALS1, IPOA, SOD1, SOD2, SODC|
|Clone Number ||N/A|
|Host Species ||Rabbit|
|Immunogen ||Rat Cu/Zn SOD|
|Applications ||WB, IP, EIA, IHC|
|Species Reactivity ||Human, Rat, Mouse, Bovine|
|Accession Number ||NP_058746.1|
|Gene ID ||24786|
|Background Info ||Detects a ~23kDa (human) and 19kDa (other species) proteins corresponding to the molecular mass of Cu/Zn superoxide dismutase (SOD) on SDS PAGE immunoblots.|
|Recommended Dilutions ||0.5 µg/ml was sufficient for detection of Cu/Zn SOD in 20 µg of rat brain tissue extract|
|Form ||Affinity (antigen) Purified|
|Storage Buffer ||PBS pH7.0, 50% glycerol, 0.09% sodium azide|
|Certificate of Analysis ||0.5 μg/mL of SPC-115 was sufficient for detection of Cu/Zn SOD in 20μg of rat brain tissue extract by colorimetric immunoblot analysis using Goat anti-rabbit IgG:AP as the secondary antibody.|
|Storage Temp ||-20 °C|
|Shipping Temp ||Blue Ice or 4 °C|
Western blot analysis of Cu/Zn SOD, rat, in a human cell line mix using a 1:1000 dilution of SPC-115.
|Research 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 O2Ë‰ 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.
|Cited References ||1. Wang, F., Kumagai-Braesch, M., Herrington M.K., Larsson, J. and Permert, J. (2009). Increased lipid metabolism and cell turnover of MiaPaCa2 cells induced by high-fat diet in an orthotopic system. Metabolism. 58 (8), 1131-1136. doi: 10.1016/j.metabol.2009.03.027.|
2. Leung, P.T.Y., Wang, Y., Mak, S.S.T. and Leung, K. M.Y. (2011). Differential proteomic responses in hepatopancreas and adductor muscles of the green-lipped mussel Perna viridis to stresses induced by cadmium and hydrogen peroxide. Aquatic Toxicology. 105 (1-2), 49-61. doi:10.1016/j.aquatox.2011.05.010
3. Hung, G. et al. (2012). Green tea extract supplementation ameliorates CCl4-induced hepatic oxidative stress, fibrosis, and acute-phase protein expression in rat. Journal of the Formosan Medical Association. 111 (10), 550-559. doi:10.1016/j.jfma.2011.06.026