Superoxide Dismutase 3, Extracellular (SOD3) antibody

Details for Product No. ABIN361741
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Antigen
Synonyms SOD3, LOC780439, fb05f10, si:dkey-117m1.6, sod3, wu:fb05f10, EC-SOD, AI314465, ECSODPT, ECSOD, SODA.4
Reactivity
Human, Rat (Rattus), Mouse (Murine)
(74), (29), (19), (12), (12), (12)
Host
Mouse
(52), (33), (2), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(7), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Western Blotting (WB), ELISA, Immunohistochemistry (IHC)
(75), (51), (36), (25), (15), (10), (8), (7), (4), (3), (3), (1)
Pubmed 7 references available
Quantity 25 μg
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Catalog No. ABIN361741
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Immunogen Human EC SOD purified from aortas
Clone 4GG11G6
Isotype IgG1 kappa
Specificity Detects EC SOD at approx. 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
Alternative Name SOD (EC)
Background Synonyms:
EC-SOD, MGC20077, EC 1.15.1.1, SOD3
Superoxide dismutase (SOD) is an endogenously produced intracellular enzyme present in almost every cell in the body. 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. In general, SODs play a major role in antioxidant defense mechanisms.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. 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. SOD3 can also be distinguished by its heparin-binding capacity.
Gene ID 6649
NCBI Accession NP_003093
UniProt P08294
Research Area Oxidative Stress
Application Notes Recommended Dilution: 1:1000 (WB), 1:100 (IHC and ICC)
Restrictions For Research Use only
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
anti-Superoxide Dismutase 3, Extracellular (SOD3) antibody EC-SOD, (4GG11G6, human cartilage)
anti-Superoxide Dismutase 3, Extracellular (SOD3) antibody (2) EC SOD (4GG11G6), Human cartilage, ICC Left control, middle young, right cartilage with osterarthritis
Background publications 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).

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).

General in:

Wispue, 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).

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

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).

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