|Application ||WB, IP|
|Isotype||Mouse IgG 1|
|Calculated MW||15936 Da|
|Positive Control||IP analysis : HeLa cell lysates|
|Application & Usage||Western blot: 1 µg/ml, IP: 1-2 µg.|
|Other Names||Superoxide dismutase, SOD1, SOD, ALS, ALS1, IPOA.|
|Formulation||100 µl of antibody in HEPES with 0.15 M NaCl, 0.01 % BSA, 0.03 % sodium azide, and 50 % glycerol|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Superoxide Dismutase 1 (SOD-1) Antibody (72B1) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Destroys radicals which are normally produced within the cells and which are toxic to biological systems.|
|Cellular Location||Cytoplasm. Nucleus. Note=Predominantly cytoplasmic; the pathogenic variants ALS1 Arg-86 and Ala-94 gradually aggregates and accumulates in mitochondria|
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Provided below are standard protocols that you may find useful for product applications.
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). SOD1 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. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. 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. SOD1 destroys radicals which are normally produced within the cells and which are toxic to biological systems.
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