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Cu/Zn SOD polyclonal antibody (biotin conjugate)

ADI-SOD-100B-0050 50 µg 209.00 USD
ADI-SOD-100B-0200 200 µg 428.00 USD
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Product Specification

Alternative Name:Superoxide Dismutase (Cu-Zn), Superoxide dismutase 1, SOD1
Immunogen:Native human Cu/Zn SOD.
UniProt ID:P00441
Species reactivity:Human, Mouse, Rat
Applications:IF, IHC (PS), IP, WB
Recommended Dilutions/Conditions:Western Blot (1:1,000, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Application Notes:Detects a band of ~23kDa (human) or ~19kDa (mouse and rat) by Western blot.
Purity Detail:Protein A-affinity purified.
Formulation:Liquid. In PBS containing 50% glycerol and 0.09% sodium azide.
Handling:Avoid freeze/thaw cycles.
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
Scientific Background:Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells: extracellular SOD (EC SOD, SOD-3); copper and zinc-containing SOD (Cu/Zn SOD, SOD-1); and manganese-containing SOD (Mn SOD, SOD-2). The Cu/Zn form binds Cu and Zn ions and exists as a soluble 32kDa homodimer in the cytosol. Mutations in the SOD-1 gene accounts for approximately 20% of amyelotrophic lateral sclerosis (ALS) or ‘Lou Gehrig disease,’ a neurodegenerative disorder characterized by the death of motor neurons in the brain, brainstem, and spinal cord that results in fatal paralysis.
Western Blot Analysis of Cu/Zn SOD: Lane 1:MWM Lane 2: Rat liver tissue lysate, Lane 3: Mouse liver tissue lysate, Lane 4: HeLa, (cell lysate) (Prod No. ADI-LYC-HL100), Lane 5: Brain (mouse), (tissue extract) (Prod No. ADI-LYT-MB100), Lane 6: Brain (rat), (tissue extract) (Prod No. ADI-LYT-RB100).
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General Literature References

Effect of exposure to benzo[a]pyrene on SODs, CYP1A1/1A2- and CYP2E1 immunopositive proteins in the blood clam Scapharca inaequivalvis: M. Monari, et al.; Mar. Environ. Res. 63, 200 (2007), Abstract;
Mutant Cu/Zn-superoxide dismutase proteins have altered solubility and interact with heat shock/stress proteins in models of amyotrophic lateral sclerosis: G.A. Shinder, et al.; J. Biol. Chem. 276, 12791 (2001), Abstract;
Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase: H.X. Deng, et al.; Science 261, 1047 (1993), Abstract;
Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis: D.R. Rosen, et al.; Nat Med. 362, 59 (1993), Abstract;
---: N. Kurobe, et al.; Biom. Res. 11, 187 (1990),
Sensitive enzyme immunoassay for human Mn superoxide dismutase: N. Kurobe, et al.; Clin. Chim. Acta 192, 171 (1990), Abstract;

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HeLa, (cell lysate) 

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ADI-LYC-HL100-F 200 µg 111.00 USD
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Brain (mouse), (tissue extract) 

Mouse brain extract., WB | Print as PDF
ADI-LYT-MB100-F 200 µg 111.00 USD
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Brain (rat), (tissue extract) 

Rat brain extract, WB | Print as PDF
ADI-LYT-RB100-F 200 µg 111.00 USD
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