SOD2/Mn-SOD (human, recombinant)

Superoxide dismutase 2 (SOD2)/manganese SOD (Mn-SOD) is an antioxidant enzyme that protects cells from oxidative stress by scavenging superoxide anions. It exists as a homotetramer where each monomer is composed of an N-terminal alpha-hairpin domain and a C-terminal alpha/beta domain that contain Mn-binding catalytic active sites. SOD2 is expressed in the mitochondria and is localized to the mitochondrial matrix where it catalyzes the dismutation of superoxide to hydrogen peroxide and oxygen by alternating reduction and reoxidation of Mn at the enzyme active site. Genetic deletion of Sod2 in mice induces metabolic acidosis and lipid accumulation in the liver and skeletal muscle, and is perinatal lethal. Transgenic SOD2 overexpression reduces superoxide levels in the hippocampal CA1 region and extends the lifespan of aged mice. SOD2 expression is reduced in tumors from patients with hepatocellular carcinoma (HCC) and this decrease is associated with increased tumor number, metastasis, and reduced survival. SOD2 SNPs have been found in patients with non-Hodgkin's lymphoma, lung cancer, or colorectal cancer. Cayman's SOD2/Mn-SOD (human, recombinant) protein consists of 199 amino acids and has a calculated molecular weight of 22.3 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 25 kDa.Synonyms: IPOB, MVCD6, Superoxide Dismutase 2/Manganese SOD. Purity: >97% estimated by SDS-PAGE. Source: Recombinant human SOD2/Mn-SOD expressed in E. coli. Amino Acids: 25-222. MW: 22.3 kDa. Formulation: (Request formulation change), Lyophilized from sterile PBS, pH 7.4, 5% trehalose, 5% mannitol, and 0.01% Tween 80.