HT Superoxide Dismutase Assay Kit

High Throughput
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Citations (2)

HT Superoxide Dismutase Assay Kit Summary

The HT Superoxide Dismutase Assay Kit is a 96-well microplate-based assay that is designed for the high throughput analysis of Superoxide Dismutase (SOD) activity in mammalian tissue and cell lysates. SODs are metalloenzymes that catalyze the dismutation of the superoxide radical (O2•-) into hydrogen peroxide (H2O2) and molecular oxygen (O2), providing an important defense against oxidative damage. In the HT Superoxide Dismutase Assay Kit, superoxide ions are generated from the conversion of xanthine and O2 to uric acid and H2O2 by Xanthine Oxidase (XOD). The superoxide anion then coverts the tetrazolium salt WST-1 to the colored product WST-1 formazan. Absorbance is then measured at 450 nm using a standard microplate reader. Addition of SOD to this reaction reduces superoxide ion levels, thereby lowering the rate of WST-1 formazan formation. SOD activity in the experimental sample is measured as the percent inhibition of the rate of WST-1 formazan formation.

Kit Contents

  • SOD
  • SOD Reaction Buffer
  • Xanthine Oxidase
  • Xanthine Solution
  • Triton® X-100
  • WST-1 Reagent
  • Five 96-well plates for 480 tests

SOD Inhibition Assay Mechanism

XOD and SOD Antagonism in the Generation of Formazan Dye. The conversion of xanthine and O2 to uric acid and H2O2by XOD generates superoxide radicals. The superoxide anions reduce a tetrazolium salt (nitroblue tetrazolium [NBT] or WST-1) to a colored formazan product (NBT-diformazan or WST-1 formazan) that absorbs light. SOD scavenges superoxide anions, thereby reducing the rate of formazan dye formation.

Triton is a registered trademark of Dow Chemical Corporation.

Product Datasheets

Preparation and Storage

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
The product requires storage at -20 to -70 °C, 2 - 8 °C, and room temperature.  Consult the product insert for specific storage temperatures. Do not use past expiration date.

Background: SOD (Superoxide Dismutase)

Superoxide Dismutases, originally identified as Indophenoloxidases (IPOs), are enzymes that catalyze the conversion of naturally-occuring but harmful superoxide radicals into molecular oxygen and hydrogen peroxide. Three mammalian isozymes of SOD have been identified and are functionally related but have very modest sequence homology. SODs are typically soluble secreted or cytosolic proteins, but are also found in the mitochondria and extracellular matrix.

Any of three metals, manganese, iron, or copper, may be used in the active site of SOD and are indicative of cellular localization.MnSOD (SOD2) is found in the mitochondria of both prokaryotes and ukaryotes, whereas the cytosol of eukaryotes and prokaryotic organisms contains Cu/ZnSOD (SOD1) and FeSOD, respectively.

There have been several mutations identified in the Cu/ZnSOD (SOD1) gene in amyotrophic lateral sclerosis (ALS) patients, possibly suggesting a role for free radicals in this disease process. The mechanism of motor neuron degeneration that occurs in ALS, however, is unclear at this time. Several hypotheses have been explored for the role of mutant SOD1 and convincing evidence for the involvement of apoptosis has been presented, as well.

Long Name
Superoxide Dismutase
Alternate Names

Citations for HT Superoxide Dismutase Assay Kit

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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  1. The Specific Inhibition of SOD1 Selectively Promotes Apoptosis of Cancer Cells via Regulation of the ROS Signaling Network
    Authors: X Li, Y Chen, J Zhao, J Shi, M Wang, S Qiu, Y Hu, Y Xu, Y Cui, C Liu, C Liu
    Oxid Med Cell Longev, 2019;2019(0):9706792.  2019
  2. Actions of Inonotus obliquus against Hyperuricemia through XOD and Bioactives Screened by Molecular Modeling
    Authors: T Yong, S Chen, D Liang, D Zuo, X Diao, C Deng, Y Wu, H Hu, Y Xie, D Chen
    Int J Mol Sci, 2018;19(10):.  2018


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