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Purified Mouse Anti-Human SOD
Purified Mouse Anti-Human SOD

Western blot analysis of SOD. SOD recombinant protein (25 U/lane) was probed with anti-SOD (clone G215-1) at concentrations of 1.0, 0.5, and 0.25 µg/ml. SOD is identified as a band of 16 kDa (subunit).

Western blot analysis of SOD. SOD recombinant protein (25 U/lane) was probed with anti-SOD (clone G215-1) at concentrations of 1.0, 0.5, and 0.25 µg/ml. SOD is identified as a band of 16 kDa (subunit).

Product Details
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BD Pharmingen™
CuZnSOD Copper/Zinc-Binding Superoxide Dismutase
Human (QC Testing)
Mouse IgG2a
Recombinant Human CuZnSOD GST Fusion Protein
Western blot (Routinely Tested)
32 kDa
0.5 mg/ml
Aqueous buffered solution containing ≤0.09% sodium azide.

Preparation And Storage

The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography. Store undiluted at 4°C.

Recommended Assay Procedures

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.

Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Please refer to 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.
556360 Rev. 6
Antibody Details
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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.

556360 Rev. 6
Format Details
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Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
556360 Rev.6
Citations & References
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Development References (4)

  1. Fridovich I. Superoxide dismutases. Adv Enzymol Relat Areas Mol Biol. 1986; (58):61-97. (Biology). View Reference
  2. Rabizadeh S, Gralla EB, Borchelt DR. Mutations associated with amyotrophic lateral sclerosis convert superoxide dismutase from an antiapoptotic gene to a proapoptotic gene: studies in yeast and neural cells. Proc Natl Acad Sci U S A. 1995; 92(7):3024-3028. (Biology). View Reference
  3. Reaume AG, Elliott JL, Hoffman EK. Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet. 1996; 13(1):43-47. (Biology). View Reference
  4. Rosen DR, Siddique T, Patterson D. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature. 1993; 362(6415):59-62. (Biology). View Reference
View All (4) View Less
556360 Rev. 6

Please refer to Support Documents for Quality Certificates

Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described

Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.