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Superoxide Dismutase 3, Extracellular (SOD3) antibody

Details for Product No. ABIN361741, Supplier: Log in to see
Guinea Pig, Human, Mouse (Murine), Rat (Rattus)
Clonality (Clone)
Monoclonal ()
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
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Immunogen Human extracellular SOD purified from aortas
Clone 4GG11G6
Specificity Detects extracellular SOD ~35 kDa.
Sensitivity 1 µg/mL of SMC-167 was sufficient for detection of EC-SOD in 20 µg of human cartilage lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
Purification Protein G Purified
Background Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body (3). It works by catalyzing the dismutation of the superoxide radical O2ˉ to O2 and H2O2, which are then metabolized to H2O and O2 by catalase and glutathione peroxidase (2, 5). In general, SODs play a major role in antioxidant defense mechanisms (4). There are three types of SOD in mammalian cells. One form (SOD1) contains Cu and Zn ions as a homodimer and exists in the cytoplasm. The two subunits of 16 kDa each are linked by two cysteines forming an intra-subunit disulphide bridge (3). The second form (SOD2) is a manganese containing enzyme and resides in the mitochondrial matrix. It is a homotetramer of 80 kDa. The third form (SOD3 or EC-SOD) is like SOD1 in that it contains Cu and Zn ions, however it is distinct in that it is a homotetramer, with a mass of 30 kDA and it exists only in the extra-cellular space (6). SOD3 can also be distinguished by its heparin-binding capacity (1).
Cellular Localization: Extracellular Space
Gene ID 6649
NCBI Accession NP_003093
UniProt P08294
Application Notes Recommended Dilution: WB (1:1000), IHC (1:100), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-Superoxide Dismutase 3, Extracellular (SOD3) antibody (ABIN361741) EC-SOD, (4GG11G6, human cartilage)
 image for anti-Superoxide Dismutase 3, Extracellular (SOD3) antibody (ABIN361741) EC SOD (4GG11G6), Human cartilage, ICC Left control, middle young, right cartilage wi...
Product cited in: Konior, Klemenska, Brudek et al.: "Seasonal superoxide overproduction and endothelial activation in guinea-pig heart; seasonal oxidative stress in rats and humans." in: Journal of molecular and cellular cardiology, Vol. 50, Issue 4, pp. 686-94, 2011 (PubMed).

Tollefson, Oberley-Deegan, Butterfield et al.: "Endogenous enzymes (NOX and ECSOD) regulate smoke-induced oxidative stress." in: Free radical biology & medicine, Vol. 49, Issue 12, pp. 1937-46, 2010 (PubMed).

Background publications Regan, Flannelly, Bowler et al.: "Extracellular superoxide dismutase and oxidant damage in osteoarthritis." in: Arthritis and rheumatism, Vol. 52, Issue 11, pp. 3479-91, 2005 (PubMed).

Gao, Flores, Leff et al.: "Synthesis and anti-inflammatory activity of a chimeric recombinant superoxide dismutase: SOD2/3." in: American journal of physiology. Lung cellular and molecular physiology, Vol. 284, Issue 6, pp. L917-25, 2003 (PubMed).

Bannister, Bannister, Rotilio: "Aspects of the structure, function, and applications of superoxide dismutase." in: CRC critical reviews in biochemistry, Vol. 22, Issue 2, pp. 111-80, 1988 (PubMed).

Hassan: "Biosynthesis and regulation of superoxide dismutases." in: Free radical biology & medicine, Vol. 5, Issue 5-6, pp. 377-85, 1989 (PubMed).

Wispé, Clark, Burhans et al.: "Synthesis and processing of the precursor for human mangano-superoxide dismutase." in: Biochimica et biophysica acta, Vol. 994, Issue 1, pp. 30-6, 1989 (PubMed).

Adachi, Ohta, Yamada et al.: "Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody." in: Clinica chimica acta; international journal of clinical chemistry, Vol. 212, Issue 3, pp. 89-102, 1993 (PubMed).

Johnson, Drugan, Miller et al.: "38" in: , Vol. 1363, Issue Nucleic acids research, pp. 28-39, 1991