SOD2, Human, BioAssay(TM) ELISA Kit (Superoxide Dismutase Mn, Mitochondrial)

Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. : Cu/Zn SOD (SOD1) is localized in cytosol, Mn SOD (SOD2) in mitochondria, and ec SOD (SOD3) in extracellular space. SOD2, the primary antioxidant enzyme that scavenges superoxide radicals in mitochondria, is essential for the survival of aerobic life. It exists as a homotetramer with an individual subunit molecular weight of about 23kD. SOD2 has been shown to play a major role in promoting cellular differentiation and tumorigenesis and in protecting against hyperoxia-induced pulmonary toxicity. Recent studies have reported that Mn SOD activity is related to cancer, aging, progeria, asthma, and transplant rejection. The expression of SOD2 in many cancers shows elevated levels of AP2 transcription factor. SOD2 expression is regulated not only at the level of transcription, but also at the level of translation by an RNA-binding protein. Lack of SOD2 expression results in dilated ventricular cardiomyopathy, neonatal lethality, and neurodegeneration. Overexpression of SOD2 has been shown to protect against oxidative stress- induced cell death and tissue injury.\n\nIntended Use:\nHuman Superoxide Dismutase-2 (human SOD2) ELISA kit is to be used for the in vitro quantitative determination of human SOD2 in human serum, human plasma, cell lysate and buffered solution. The assay will recognize both native and recombinant human SOD2.\nThis kit has been configured for research use only and is not to be used in diagnostic procedures.\n\nSensitivity:\nThe minimal detectable dose of human SOD2 was calculated to be 78pg/ml, by subtracting two standard deviations from the mean of 10 zero standard replicates (ELISA buffer, S0) and intersecting this value with the standard curve obtained in the same calculation.\n\nSpecificity:\nThe following substances were tested and found to have no cross-reactivity: human SOD1, SOD3, SOD4, rat SOD2 and mouse SOD2.\n\nPrinciple:\nThe design of this assay is based on a sandwich Enzyme-Linked Immunosorbent Assay (ELISA). The microtiter plate provided in this kit has been pre-coated with a monoclonal antibody specific to human SOD2. Samples are pippetted into these wells. Nonbound SOD2 and other components of the sample should be removed by washing, then biotin-conjugated monoclonal antibody specific to SOD2 added. In order to quantitatively determine the amount of SOD2 present in the sample, Avidin conjugated to Horseradish Peroxidase (HRP) should be added to each microplate well. The final step, a TMB-substrate solution added to each well. Finally, a sulfuric acid solution is added and the resulting yellow colored product is measured at 450nm. Since the increases in absorbency is directly proportional to the amount of captured SOD2.\n\nKit Componants:\nMicroplate: 1x96 wells\nIncubation buffer: 1x30ml\nWashing buffer, (10x): 1x100ml\nStandard protein: 1 glass vial lyophilized\nStandard/sample dilution buffer: 1x25ml\nSecond antibody: 1 glass vial lyophilized\nAV-HRP, (100x): 1x150ul\nSecondary antibody/AV-HRP dilution buffer: 1x25ml\nSubstrate (TMB): 1x20ml\nStop solution: 1x20ml\n\nStorage and Stability:\nStore components at 4 degrees C. Stable for at least 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

S8060-02C

Size

96Tests

Applications

ELISA

References

1. Edward Luk et al manganese Activation of Superoxide Dismutase 2 in the Mitochondria of Saccharomyces cerevisiae. (2005) The Jounal of Biol. Chem. 280(24):22715-22720. 2. Macmillan-Crow LA et al Invited review: manganese superoxide dismutase in disease (2001) Free radic Res 34(4):325-336. 3. Igor N. Zelko et al Superoxide dismutase multigene family: a comparison of the CuZn- SOD (SOD1), Mn-SOD(SOD2), and EC-SOD(SOD3) gene structures, evolution, and expression (2002) Free Radical Biology & Medicine 33(3):337-349. 4. Ruby Leah B. et al The copper Chaperone CCS Directly Interacts with Copper/Zinc Superoxide Dismutase (1998) The Journal of Biological Chemistry 273(37):23625-23628. 5. Tim D. Oury et al Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimmers: a simplified, high-yield purification of extracellular superoxide dismutase (1996) Biochem .J .317:51-57. 6. Richard W. Strange et al The Structure of Holo and Metal-dificient Wild-type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis (2003) J. Mol. Biol. 328:877-891.