SOD1 Rabbit anti-Human, Polyclonal, Invitrogen™

Description

Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD1 is found in all eukaryotic species as a homodimeric 32kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor

PA1-18276 detects Superoxide Dismutase 1 from human samples.PA1-18276 has been successfully used in immunohistochemistry (paraffin and frozen) and Western blot procedures.The PA1-18276 immunogen is a synthetic peptide corresponding to residues H(121) E K A D D L G K G G N E E S T K T G(139) of human superoxide dismutase (SOD1), conjugated to diphtheria toxin. After reconstitution keep aliquots at -20ºC for a higer stability, and at 4ºC with an appropriate antibacterial agent. Avoid freeze/thaw cycles. Glycerol (1:1) may be added for an additional stability.Reconstitute with 100 ul of distilled water.