Specific to human extracellular SOD (SOD3). Under reducing conditions the SOD3 antibody shows a major band at approximately 30kDa which is the approximate molecular weight of the SOD3 monomer and two faint minor bands at approximately 50 and 70 kDa. The SOD3 molecule is a homotetramer (4 monomers) with a combined molecular weight of around a 130 Kda. The two faint bands are probably dimers and triplicates of the monomer. This pattern is common with many tetramers (such as cellular glutathione peroxidase) as there is incomplete reduction with DTT.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/200 - 1/2000.
Use at an assay dependent concentration.
1/1000 - 1/4000. Detects a band of approximately 31 kDa (predicted molecular weight: 26 kDa).
Protect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Expressed in blood vessels, heart, lung, kidney and placenta. Major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid.
Belongs to the Cu-Zn superoxide dismutase family.
Secreted > extracellular space. 99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium.
Shrestha P et al. Cloning, Purification, and Characterization of Recombinant Human Extracellular Superoxide Dismutase in SF9 Insect Cells. Mol Cells39:242-9 (2016).
Read more (PubMed: 26912083) »
Cunningham MW et al. Pregnant rats treated with a high-fat/prooxidant Western diet with ANG II and TNF-a are resistant to elevations in blood pressure and renal oxidative stress. Am J Physiol Regul Integr Comp Physiol308:R945-56 (2015).
Read more (PubMed: 25810384) »