|Calculated MW||24.4 kDa (219 aa, 25-222 aa + His Tag)|
|Other Names||Superoxide dismutase [Mn], mitochondrial, IPOB, MNSOD, MVCD6.|
|Sequence||MGSSHHHHHH SSGLVPRGSH MKHSLPDLPY DYGALEPHIN AQIMQLHHSK HHAAYVNNLN VTEEKYQEAL AKGDVTAQIA LQPALKFNGG GHINHSIFWT NLSPNGGGEP KGELLEAIKR DFGSFDKFKE KLTAASVGVQ GSGWGWLGFN KERGHLQIAA CPNQDPLQGT TGLIPLLGID VWEHAYYLQY KNVRPDYLKA IWNVINWENV TERYMACKK|
|Storage||-80°C; 0.5 mg/ml solution in 20 mM Tris-HCl (pH 8.0) containing 20% glycerol.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
SOD2 is part of the iron/manganese superoxide dismutase family. It encodes a mitochondrial protein that forms a homotetramer and binds one manganese ion per subunit. SOD2 binds to the superoxide byproducts of oxidative phosphorylation and converts them to hydrogen peroxide and diatomic oxygen. Mutations in SOD2 gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer. SOD2 destroys radicals which are usually produced within the cells and which are toxic to biological systems.
Wispe J.R.,et al.Biochim. Biophys. Acta 994:30-36(1989).
Beck Y.,et al.Nucleic Acids Res. 15:9076-9076(1987).
Heckl K.,et al.Nucleic Acids Res. 16:6224-6224(1988).
Ho Y.-S.,et al.FEBS Lett. 229:256-260(1988).
Church S.L.,et al.Biochim. Biophys. Acta 1087:250-252(1990).
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