Superoxide Dismutase 1 (SOD1) (human) ELISA Kit (10x96T)

Catalog number: YIF-LF-EK0103
Brand: AbFrontier
Packing: 10 x 96 wells
Price: On Request
Expected delivery time: 7 days
Quantity:

Product specifications for - Superoxide Dismutase 1 (SOD1) (human) ELISA Kit (10x96T)

Overview: 
Product group: Assays
Category: ELISA / EIA
Application: ELISA
Species: Human
Properties: 
Assay Sensitivity: 12.5 pg/ml
Assay Detection Range: 12.5 pg/ml - 800 pg/ml
Datasheet: Datasheet
  Research Use Only
UNSPSC: 41116158
Storage instructions: 2-¦C to 8-¦C
Scientific information: 
Scientific info: Sandwich ELISA. Sensitivity: 12.5 pg/ml. 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). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit. 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. SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. 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. - 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.
Safety information: 
Hazard information: Non-hazardous
Additional information: 
Synonyms: YIF-LF-EK0103; AbFrontier