A 96-well sandwich ELISA for measuring the expression of mitochondrial superoxide dismutase (SOD2) in human, mouse and rat samples.

Aerobic organisms have several mechanisms to protect against oxidation, particularly from harmful reactive oxygen species (ROS). The principle cellular anti-oxidants are the superoxide dismutase family (SOD, E.C. 1.15.1.1). These enzymes dismutate superoxide into hydrogen peroxide which is further detoxified by other cellular defenses such as glutathione peroxidase and catalase. Superoxide and its products have been implicated in a wide range of diseases including cancer, inflammation, neurodegenerative diseases, diabetes and aging itself.

The SOD family has 3 members, two of which are Cu-Zn type - the extracellular SOD3 and the cytoplasmic SOD1. The other member is the mitochondrial Mn type SOD2.

The mitochondrial Mn-SOD2 is a homotetramer of subunit mass 23 kDa in the mitochondrial matrix. SOD2 has been shown to be essential since knockout mice die shortly after birth. SOD2 levels may be down-regulated in tumor cells and recent observations show that over expression of SOD2 in tumor cells may suppress cell division and cancer growth (Oberley, Biomedecine & Pharmacotherapy, 2005, 59, p143-8).