Superoxide Dismutase 4 (SOD4) (human) ELISA Kit
|Synonyms||CCS; Superoxide Dismutase Copper Chaperone; Copper Chaperone for Superoxide Dismutase|
|Application Set||Compound Screening|
|Other Product Data||
Click here for Original Manufacturer Product Datasheet
|Declaration||Manufactured by AbFrontier|
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||+4°C|
Any unused reconstituted standard should be discarded or frozen at -80℃.
Standard can be frozen and thawed one time only without loss of immunoreactivity.
|Product Specification Sheet|
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). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 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.