Cu/Zn Superoxide dismutase (Cu/Zn SOD) is an antioxidant enzyme that protects cells from oxidative stress by scavenging superoxide anions.{55250} It exists as a homodimer that is stabilized by a disulfide bond between the subunits. Each monomer is composed of a Greek key ?-barrel and an active site channel made up of a ?4/?5 loop, which interacts with the dimer interface and active site zinc, and an electrostatic loop, which facilitates superoxide entry into the copper-containing active site.{55251} Cu/Zn SOD is ubiquitously expressed and primarily localizes to the cytosol but has also been found in the nucleus, peroxisomes, lysosomes, and the intermembrane space of mitochondria.{65441,12502} It catalyzes the dismutation of superoxide to hydrogen peroxide and oxygen by alternating reduction and reoxidation of copper at the enzyme active site.{55250} Overexpression of SOD1 protects against increases in reactive oxygen species (ROS) and apoptosis in an in vitro model of renal ischemia induced by ATP depletion.{27265} In vivo, transgenic mice expressing the destabilized Cu/Zn SODG93A mutation exhibit impaired spinal cord mitochondrial respiration.{10639,64708} Mutations in SOD1 are associated with amyotrophic lateral sclerosis (ALS).{15491} Cayman’s Cu/Zn SOD Monoclonal Antibody can be used for flow cytometry (FC), immunoprecipitation (IP), and Western blot (WB) applications.