|Reactivity||Human Mouse Rat|
|Tested applications||WB IHC|
|Recommended Dilution||WB 1:500 - 1:2000
IHC 1:50 - 1:200|
|Observed MW||Refer to Figures|
|Immunogen||Recombinant protein of human SOD1|
|Storage Buffer||Store at -20℃. Avoid freeze / thaw cycles.
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.|
SOD1, Cu/Zn superoxide dismutase, is a major antioxidant enzyme that catalyzes the conversion of superoxide anion to hydrogen peroxide and molecular oxygen (1). SOD1 is ubiquitously expressed and is localized in the cytosol, nucleus and mitochondrial intermembrane space. The SOD1 gene locus is on chromosome 21 in a region affected in Down Syndrome (2). In addition, over 100 distinct SOD1 inherited mutations have been identified in the familial form of amyotrophic lateral sclerosis (ALS), a progressive degenerative disease of motor neurons (3-5). Despite the fact that SOD1 helps to eliminate toxic reactive species, its mutations in ALS have been described as gain-of-function (5). The mechanism by which mutant SOD1 induces the neurodegeneration observed in ALS is still unclear. Mutant SOD1 proteins become misfolded and consequently oligomerize into high molecular weight species that aggregate and end up in proteinaceous inclusions (5).
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