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SOD3 Mouse anti-Guinea Pig, Human, Mouse, Rat, Clone: 4GG11G6, Invitrogen™

Mouse Monoclonal Antibody

Manufacturer:  Invitrogen MA527661

Catalog No. PIMA527661


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Description

Description

Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
Specifications

Specifications

SOD3
Monoclonal
1 mg/ml
PBS with 50% glycerol and 0.09% sodium azide; pH 7.4
O09164, P08294, Q08420
EC SOD, EC-SOD, Extracellular superoxide dismutase [Cu Zn], Extracellular superoxide dismutase [Cu-Zn], Extracellular superoxide dismutase, Extracellular superoxide dismutase precursor, MGC20077, SOD 3, SOD3, SODE_HUMAN, Superoxide dismutase 3 extracellular
Mouse
IgG1, kappa
100 μg
-20°C
Primary
100718762, 20657, 25352, 6649
ELISA, Immunocytochemistry, Immunofluorescence, Immunohistochemistry, Western Blot
4GG11G6
Unconjugated
SOD3
Liquid
SOD3
Human extracellular SOD purified from aortas
Protein G
RUO
Antibody
Monoclonal
Guinea Pig, Human, Mouse, Rat
Documents
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