Key features and details
- Rabbit polyclonal to Superoxide Dismutase 3/EC-SOD
- Suitable for: IHC-Fr, IHC-P, WB
- Reacts with: Human
- Isotype: IgG
Product nameAnti-Superoxide Dismutase 3/EC-SOD antibody
See all Superoxide Dismutase 3/EC-SOD primary antibodies
DescriptionRabbit polyclonal to Superoxide Dismutase 3/EC-SOD
SpecificitySpecific 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.
Tested applicationsSuitable for: IHC-Fr, IHC-P, WBmore details
Species reactivityReacts with: Human
- IHC: cortex of Dementia patient with Lewy bodies WB: human lung lysate
Previously labelled as Superoxide Dismutase 3.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Storage bufferPreservative: 0.02% Thimerosal (merthiolate)
Constituent: Whole serum
Concentration information loading...
Our Abpromise guarantee covers the use of ab21974 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-Fr||1/200 - 1/2000.|
|IHC-P||Use at an assay dependent concentration.|
|WB||1/1000 - 1/4000. Detects a band of approximately 31 kDa (predicted molecular weight: 26 kDa).|
FunctionProtect the extracellular space from toxic effect of reactive oxygen intermediates by converting superoxide radicals into hydrogen peroxide and oxygen.
Tissue specificityExpressed in blood vessels, heart, lung, kidney and placenta. Major SOD isoenzyme in extracellular fluids such as plasma, lymph and synovial fluid.
Sequence similaritiesBelongs to the Cu-Zn superoxide dismutase family.
Cellular localizationSecreted > 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.
- Information by UniProt
- EC SOD antibody
- EC-SOD antibody
- Extracellular superoxide dismutase [Cu Zn] antibody
ab21974 (1/1000) staining of ciliated bronchiolar cells in human lung.
ab21974 (1/1000) staining of human kidney tubule cells.
All lanes : Anti-Superoxide Dismutase 3/EC-SOD antibody (ab21974) at 1/500 dilution
Lane 1 : Lung (Human) Tissue Lysate
Lane 2 : Human kidney tissue lysate - total protein (ab30203)
Lane 3 : Human placenta tissue lysate - total protein (ab29745)
Lysates/proteins at 10 µg per lane.
All lanes : Goat Anti-Rabbit IgG H&L (HRP) preadsorbed (ab97080) at 1/5000 dilution
Developed using the ECL technique.
Performed under reducing conditions.
Predicted band size: 26 kDa
Observed band size: 31 kDa why is the actual band size different from the predicted?
Additional bands at: 75 kDa. We are unsure as to the identity of these extra bands.
Exposure time: 30 seconds
Superoxide Dismutase 3 / EC-SOD contains a number of potential glycosylation sites (SwissProt) which may explain its migration at a higher molecular weight than predicted.
ab21974 has been referenced in 10 publications.
- Peng KT et al. Dysregulated expression of antioxidant enzymes in polyethylene particle-induced periprosthetic inflammation and osteolysis. PLoS One 13:e0202501 (2018). PubMed: 30125327
- Shrestha P et al. Cloning, Purification, and Characterization of Recombinant Human Extracellular Superoxide Dismutase in SF9 Insect Cells. Mol Cells 39:242-9 (2016). WB . 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 Physiol 308:R945-56 (2015). PubMed: 25810384
- Duscher D et al. Aging disrupts cell subpopulation dynamics and diminishes the function of mesenchymal stem cells. Sci Rep 4:7144 (2014). IHC-Fr ; Mouse . PubMed: 25413454
- Cunningham MW et al. Renal nitric oxide synthase and antioxidant preservation in cyp1a1-ren-2 transgenic rats with inducible malignant hypertension. Am J Hypertens 26:1242-9 (2013). PubMed: 23764378
- Quinn M et al. Suppression of the HPA axis during extrahepatic biliary obstruction induces cholangiocyte proliferation in the rat. Am J Physiol Gastrointest Liver Physiol 302:G182-93 (2012). PubMed: 21979757
- Moningka NC et al. Protective actions of nebivolol on chronic nitric oxide synthase inhibition-induced hypertension and chronic kidney disease in the rat: a comparison with angiotensin II receptor blockade. Nephrol Dial Transplant 27:913-20 (2012). PubMed: 21856762
- Moningka NC et al. Twelve weeks of treadmill exercise does not alter age-dependent chronic kidney disease in the Fisher 344 male rat. J Physiol 589:6129-38 (2011). WB ; Rat . PubMed: 21969451
- Mital R et al. Antioxidant network expression abrogates oxidative posttranslational modifications in mice. Am J Physiol Heart Circ Physiol 300:H1960-70 (2011). PubMed: 21335461
- Scott JL et al. Superoxide dismutase downregulation in osteoarthritis progression and end-stage disease. Ann Rheum Dis 69:1502-10 (2010). PubMed: 20511611