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MilliporeSigma™ anti-Cu/Zn-SOD, Polyclonal
Rabbit Polyclonal Antibody
Supplier: MilliporeSigma™ 07403I
Description
Specifically detects Cu/Zn-SOD Clone: in Human, Mouse, Rat samples, and it is validated for Immunohistochemistry, Western Blotting
Superoxide dismutase [Cu-Zn] (EC 1.15.1.1; UniProt P00441; also known as Cu/Zn superoxide dismutase, Epididymis secretory protein Li 44, hSod1, Indophenoloxidase A, Superoxide dismutase 1) is encoded by the SOD1 (also known as ALS1) gene (Gene ID 6647) in human. Superoxide dismutases (SOD) provide important cellular antioxidant defense against oxidative damage by catalyzing the dismutation (or partitioning) of the superoxide (O2-) radical into either molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide dismutases are divided into three families based on the metal cofactor. The Cu/Zn type binds both copper and zinc, the Fe and Mn types bind either iron or manganese, and the Ni type binds nickel. Three forms of SOD are present in mammals, the cytosolic SOD1, the mitochondrial SOD2, and the extracellular SOD3. SOD1 exists in dimeric form, whereas the SOD2 and SOD3 are tetrameric. SOD1 and SOD3 Cu/Zn type, whereas SOD2 is Mn type. Mutations in SOD1 gene have been linked to 20% of amyotrophic lateral sclerosis (ALS), also known as Lou Gehrig disease.Specifications
Cu/Zn-SOD | |
Polyclonal | |
Purified rabbit polyclonal antibody in buffer containing 0.1M Tris-Glycine (pH 7.4), 150mM NaCl with 0.05% sodium azide. | |
SOD1 | |
KLH-conjugated linear peptide corresponding to a C-terminal sequence of human Cu/Zn-SOD. | |
100 μg | |
Neuroscience | |
NP_000445 | |
2°C to 8°C for one year |
Immunohistochemistry, Western Blot | |
Unconjugated | |
P00441 | |
Rabbit | |
Affinity Purified | |
RUO | |
Primary | |
Human, Mouse, Rat |
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