Superoxide Dismutase 1, Soluble (SOD1) antibody

Details for Product No. ABIN967513
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(366), (187), (185), (94), (32), (29), (28), (24), (22), (22), (20), (19), (17), (17), (17), (17), (5), (4), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
(358), (80), (24), (12), (9), (1), (1)
Clonality (Clone)
Monoclonal ()
(31), (29), (17), (11), (10), (10), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (7), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB)
(413), (262), (154), (125), (89), (85), (55), (31), (29), (14), (10), (5), (4), (3), (3), (2), (2), (2), (2), (1), (1)
Pubmed 4 references available
Quantity 0.1 mg
Shipping to United States ( )
Brand BD Pharmingen™
Immunogen Recombinant Human CuZnSOD GST Fusion Protein
Clone G215-1
Isotype IgG2a
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Purification The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name SOD (SOD1 Antibody Abstract)
Background The superoxide free radical O2.- is an intermediate form of molecular oxygen that is produced as a natural by-product of respiration and other biological processes Free radicals like O2.- can lead to the formation of additional reactive oxygen species that, in turn, can cause oxidative damage to DNA, protein, and lipid. The superoxide dismutases provide a defense against the damaging effects of O2.- by converting it to O2 + H2O2 (hydrogen peroxide). Hydrogen peroxide is then normally converted to water by either glutathione peroxidase or catalase. SODs are divided up into three types, and thought to evolve from two independent evolutionary lines: The copper- and zinc-containing SOD, CuZnSOD, is expressed in the cytosol of eukaryotic cells, the manganese-containing SOD, MnSOD, is present in bacteria, in the matrix of bacteria, and in mitochondria, and the iron-containing SOD, FeSOD, is found primarily in bacteria and is also expressed in some plants. All of the SODs catalyze the dismutation of O2.- at approximately the same rates. CuZnSOD lacks amino acid sequence homology with MnSOD and FeSOD, suggesting that it evolved independently from the FeSOD/MnSOD family of enzymes. Mutations have been described in the gene encoding CuZnSOD (SOD1) which reduce the activity and halflife of the enzyme. However, the role of these mutations in pathogenesis remains to be elucidated. Clone G215-1 recognizes human CuZnSOD. The antibody was originally characterized by western blot analysis of cells from transgenic mice expressing human CuZnSOD. Recombinant full-length human CuZnSOD GST fusion protein was used as immunogen.
Synonyms: CuZnSOD Copper/Zinc-Binding Superoxide Dismutase
Molecular Weight 32 kDa
Application Notes Applications include western blot analysis (1-2 µg/ml) of over-expressed human CuZnSOD. CuZnSOD is a homodimeric enzyme with a molecular weight of ~32 kDa. The two subunits associate noncovalently and are also stabilized by an intrachain disulfide bond. The molecular weight of each subunit is ~16 kDa.
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/mL
Buffer Aqueous buffered solution containing ≤0.09 % sodium azide.
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Storage Comment Store undiluted at 4°C.
Supplier Images
Western Blotting (WB) image for anti-Superoxide Dismutase 1, Soluble (SOD1) antibody (ABIN967513) Western blot analysis of SOD. SOD recombinant protein (25 U/lane) was probed with ant...
Image no. 2 for anti-Superoxide Dismutase 1, Soluble (SOD1) antibody (ABIN967513) anti-Superoxide Dismutase 1, Soluble (SOD1) antibody (Image 2)
Product cited in: Reaume, Elliott, Hoffman et al.: "Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury." in: Nature genetics, Vol. 13, Issue 1, pp. 43-7, 1996 (PubMed).

Rosen, Siddique, Patterson et al.: "Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis." in: Nature, Vol. 362, Issue 6415, pp. 59-62, 1993 (PubMed).

Rabizadeh, Gralla, Borchelt et al.: "Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 92, Issue 7, pp. 3024-8, 1995 (PubMed).

Fridovich: "Superoxide dismutases." in: Advances in enzymology and related areas of molecular biology, Vol. 58, pp. 61-97, 1986 (PubMed).

Catalog No. ABIN967513
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