SOD is located intracellular (SOD-1; cytosolic, SOD-2; mitochondrial matrix) and extracellular (SOD-3), and catalyzes the dismutation of superoxide anion to H2O2.SOD3, or EC-SOD, is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. SOD-3 is a Mn-containing tetrameric protein with a subunit Mr of 24-35 kDa. The activity of EC-SOD is dependent on its ability to form a tetramer of 135 kDa.
Description | SOD is located intracellular (SOD-1; cytosolic, SOD-2; mitochondrial matrix) and extracellular (SOD-3), and catalyzes the dismutation of superoxide anion to H2O2.SOD3, or EC-SOD, is the most recently characterized SOD, exists as a copper and zinc-containing tetramer, and is synthesized containing a signal peptide that directs this enzyme exclusively to extracellular spaces. SOD-3 is a Mn-containing tetrameric protein with a subunit Mr of 24-35 kDa. The activity of EC-SOD is dependent on its ability to form a tetramer of 135 kDa. |
Tested Applications | WB: 1:1000; IF: 1:100-1:300; IHC:1:50-1:200 |
Species Reactivity | Human, Mouse, Rat |
Host Species/Isotype | Rabbit/IgG |
Molecular Weight | 25-33 kDa |
GenBank | BC014418 |
Uniprot | P08294 |
Concentration | 410 μg/ml |
Form | Liquid |
Storage Instruction | 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at -20°C. Do Not Aliquot. |
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