Abcam, ab65354, Superoxide Dismutase Activity Assay Kit (Colorimetric)

Size: 100Test / 2000Test
Superoxide Dismutase (SOD) Activity Assay Kit (Colorimetric) ab65354 is a simple 30 min assay for superoxide dismutase (SOD) activity. Readout on any colorimetric (450 nm) microplate reader. - Results in just 30 min - Ease of use: highly rated by customers - Trusted by the scientific community: cited in >290 publications - Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Key facts
Detection method:Colorimetric,
Sample types:Plasma, Tissue Extracts, Cell culture media, Serum, Other biological fluids, Cell Lysate,
Assay type:Enzyme activity,
Assay time:30m,
Assay Platform:Microplate reader

Product details:
Superoxide Dismutase Activity Assay Kit (Colorimetric) ab65354 is a simple and rapid assay for superoxide dismutase (SOD) activity.
In the SOD assay protocol:
- superoxide anions are produced by the action of xanthine oxidase
- SOD catalyzes the dismutation of the superoxide anion into hydrogen peroxide and O
- superoxide anions act on WST-1 to produce a water-soluble formazan dye which can be detected by the increase in absorbance at 450 nm
The greater the activity of SOD in the sample, the less formazan dye is produced.
Superoxide dismutase assay protocol summary:
- add samples to wells
- add WST-1 working solution and enzyme working solution and incubate for 20 min at 37°C
- analyze with microplate reader
Superoxide dismutase (SOD) is one of the most important antioxidative enzymes. It catalyzes the dismutation of the superoxide anion into hydrogen peroxide and molecular oxygen. **Related products** Review the to learn about more assays for oxidative stress.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information-Please refer to protocols

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Superoxide dismutase also called SOD functions as an antioxidant enzyme that converts superoxide radicals into oxygen and hydrogen peroxide. It plays a critical role in reducing oxidative stress in cells. The enzyme exists in several isoforms including SOD1 SOD2 and SOD3 each with different cellular localizations and cofactors. SOD1 or cytosolic copper-zinc superoxide dismutase has a mass of approximately 32 kDa and is found in the cytoplasm. SOD2 known as manganese superoxide dismutase is mitochondrial and shares similar antioxidant functions. SOD3 is extracellular and has a distinct expression pattern mostly found in tissues like lungs and blood vessels.
Biological function summary
SOD enzymes protect cells by dismutating reactive superoxide radicals preventing cellular damage and apoptosis. These enzymes although not forming large protein complexes have critical interactions with cellular systems maintaining redox balance. Superoxide radicals if not regulated can lead to lipid peroxidation DNA damage and protein oxidation disrupting normal cellular processes. Superoxide dismutases thereby hold a defensive position in maintaining physiological homeostasis.
Pathways
Superoxide dismutase enzymes especially within the reactive oxygen species (ROS) signaling pathway contribute to cellular defense mechanisms. In the antioxidant defense pathway SOD enzymes act alongside catalase and glutathione peroxidase. They modulate oxidative stress levels that play a signal transduction role in processes like cell proliferation and apoptosis. This activity links them with proteins like catalase which further catabolize hydrogen peroxide into water and oxygen completing the detoxification process initiated by SOD.
Superoxide dismutases are associated with neurodegenerative diseases and cancer. Mutations in SOD1 have links to amyotrophic lateral sclerosis (ALS) where misfolded proteins lead to motor neuron degeneration. SOD activity levels altered oxidative stress responses and faulty mitochondrial functions connect with Alzheimer's disease. The disease associations also include seemingly related proteins like TDP-43 in ALS pointing towards a wider network of dysfunction in oxidative stress pathways.