Superoxide Dismutases (SODs), originally identified as Indophenoloxidases (IPOs), are enzymes that catalyze the conversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Superoxide Dismutases 2, SOD2, also known as Manganese (Mn) SOD, mitochondrial SOD and IPO-B, is an intramitochondrial 22 kDa homotetramer. Each SOD2 monomer binds one Mn2+ ion. Three isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SOD2 shares only 23 and 17% sequence identity with SOD1 and SOD3, respectively.
Image: Western blot detection of SOD2. Recombinant human SOD1, SOD2, and SOD3 (1 ng) and lysates from human MCF-7, mouse NIH-3T3 and rat L6 cells were resolved by SDS-PAGE, transferred to Immobilon-P membrane and immunoblotted with 0.5 μg/mL mouse anti-SOD2 as described in Protocol on Datasheet. A 10 second exposure to film is shown.
SOD2 is, however, well conserved from species to species and shares 90% and 87% homology with mouse and rat SOD2. Oxidative stress has been implicated in many diseases and the chief source of reactive oxygen species within the cell is the mitochondrion. SOD2 is a free radical scavenging enzyme that protects against damage from superoxide produced as a byproduct of oxidative phosphorylation. SOD2 is required for normal biologic function of tissues by maintaining the integrity of mitochondrial enzymes susceptible to inactivation by superoxide. Mutations in this gene have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer.
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