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SOD3 encodes a member of the superoxide dismutase (SOD) protein family. Additionally we are shipping SOD3 Kits (42) and SOD3 Proteins (14) and many more products for this protein.
Showing 10 out of 162 products:
Guinea Pig Monoclonal SOD3 Primary Antibody for ICC, IF - ABIN361742
Gao, Flores, Leff, Bose, McCord: Synthesis and anti-inflammatory activity of a chimeric recombinant superoxide dismutase: SOD2/3. in American journal of physiology. Lung cellular and molecular physiology 2003
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Human Polyclonal SOD3 Primary Antibody for ICC, IF - ABIN2482056
Adachi, Ohta, Yamada, Futenma, Kato, Hirano: Quantitative analysis of extracellular-superoxide dismutase in serum and urine by ELISA with monoclonal antibody. in Clinica chimica acta; international journal of clinical chemistry 1993
Show all 5 references for ABIN2482056
Human Polyclonal SOD3 Primary Antibody for ICC, IF - ABIN2482052
Bannister, Bannister, Rotilio: Aspects of the structure, function, and applications of superoxide dismutase. in CRC critical reviews in biochemistry 1988
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Human Polyclonal SOD3 Primary Antibody for ICC, IF - ABIN2482054
Hassan: Biosynthesis and regulation of superoxide dismutases. in Free radical biology & medicine 1989
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Human Polyclonal SOD3 Primary Antibody for ICC, IF - ABIN2482055
Wispé, Clark, Burhans, Kropp, Korfhagen, Whitsett: Synthesis and processing of the precursor for human mangano-superoxide dismutase. in Biochimica et biophysica acta 1989
Show all 5 references for ABIN2482055
Human Monoclonal SOD3 Primary Antibody for ICC, IF - ABIN451713
Wang, Harrell, Iwanaga, Jedlicka, Ford: Vascular endothelial growth factor C promotes breast cancer progression via a novel antioxidant mechanism that involves regulation of superoxide dismutase 3. in Breast cancer research : BCR 2015
Show all 2 references for ABIN451713
Human Polyclonal SOD3 Primary Antibody for FACS, IHC (p) - ABIN390857
Stern, Chapman, Wijsman, Altherr, Rosen: Assignment of SOD3 to human chromosome band 4p15.3-->p15.1 with somatic cell and radiation hybrid mapping, linkage mapping, and fluorescent in-situ hybridization. in Cytogenetic and genome research 2003
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These data provide new insights into the functional actions of SOD3 on oxidative stress-induced (show SQSTM1 Antibodies) cell damage.
Study shows that patients with the Ala40Thr polymorphism in EC-SOD are at a higher risk of developing type 2 diabetes mellitus.
Increased expression of SOD3 ameliorates H2O2-induced oxidative damage in neuroblastoma (show ARHGEF16 Antibodies) cells by inhibiting the mitochondrial pathway.
Results describe the molecular cloning of both full length and truncated form of human SOD3 both expressed in Sf9 insect cells as monomers and dimer conformation, with enzymatic activity.
study suggests that carriers of adiponectin (show ADIPOQ Antibodies) gene promoter -11391G/A(AA) and EC-SOD (CG+GG) genotypes may have a high risk of nonalcoholic fatty liver disease (NAFLD (show TSC2 Antibodies)), and the gene genotypes can interact with H. Pylori infection in the pathogenesis of NAFLD (show TSC2 Antibodies)
FXR (show NR1H4 Antibodies) may regulate SOD3 expression to suppress reactive oxygen species production, resulting in decreasing JNK (show MAPK8 Antibodies) activity.
These results support the hypothesis that loss of extracellular SOD contributes to the invasive phenotype of pancreatic ductal adenocarcinoma
The T-allele of rs2284659 in the promoter of SOD3 was associated with better cardiovascular outcomes in diabetic patients.
SOD3 regulates the expression of multiple components of small G protein (show RAC2 Antibodies) GTPase (show RACGAP1 Antibodies) signal pathways.
Expression of extracellular superoxide dismutase (EC-SOD) and expression of the prooxidant gene NADPH oxidase 4 (show NOX4 Antibodies) was decreased significantly by trichostatin A.
wound healing impairments in ageing are associated with increased levels of ROS (show ROS1 Antibodies), decreased SOD3 expression and impaired extracellular oxidative stress regulation
Arginine 213 in the heparin-binding domain of SOD3 is critical for maintaining proper organ function through moderating the normal innate immune response, which would otherwise lead to chronic inflammation and degenerative diseases in aged mice.
the rs1799895 polymorphism in extracellular superoxide dismutase affects cardiopulmonary disease risk by altering protein distribution
the localized loss of pulmonary artery EC-SOD augments chronic hypoxic pulmonary hypertension. In addition to oxidative inactivation of nitric oxide, deletion of EC-SOD seems to reduce eNOS (show NOS3 Antibodies) activity, further compromising pulmonary vascular function.
Our results suggest that EC-SOD plays a dynamic role in the inflammatory response mounted by activated macrophages.
reduced SOD3 expression correlates with alveolar injury measures in the recovered neonatal hyperoxic lung
Data suggest that epigenetic silencing of EcSOD may contribute to mammary tumorigenesis and that restoring the extracellular superoxide scavenging activity could be an effective strategy for breast cancer treatment.
When Cys195 was introduced, both active EC-SOD and a novel inactive EC-SOD were generated, and the specific activity of the EC-SOD was significantly reduced by the mutation.
a decrease in ATP7A (show ATP7A Antibodies) protein expression contributes to impaired SOD3 activity, resulting in O2(*-) overproduction and endothelial dysfunction in blood vessels of type 1 diabetes mellitus.
expression profile of SOD3 in follicles: oocytes (high levels of SOD3); cumulus cells (high levels of SOD3); granulosa cells (some SOD3); follicular fluid (small follicles show increased amounts of SOD3 in comparison with large follicles)
in addition to binding heparin, EC-SOD specifically binds to type I collagen with a dissociation constant (K(d)) of 200 nm
Heme oxygenase-1 (show HMOX1 Antibodies) induction modulates hypoxic pulmonary vasoconstriction through upregulation of ecSOD/SOD3.
suggests a new physiological role for SOD3 as a Ras regulatory molecule in signal transduction
This gene encodes a member of the superoxide dismutase (SOD) protein family. SODs are antioxidant enzymes that catalyze the dismutation of two superoxide radicals into hydrogen peroxide and oxygen. The product of this gene is thought to protect the brain, lungs, and other tissues from oxidative stress. The protein is secreted into the extracellular space and forms a glycosylated homotetramer that is anchored to the extracellular matrix (ECM) and cell surfaces through an interaction with heparan sulfate proteoglycan and collagen. A fraction of the protein is cleaved near the C-terminus before secretion to generate circulating tetramers that do not interact with the ECM.
superoxide dismutase 3, extracellular
, extracellular superoxide dismutase
, Extracellular superoxide dismutase
, extracellular superoxide dismutase [Cu-Zn]
, Superoxide dimutase 3
, superoxide dismutase B
, superoxide dismutase [Mn] 3.1, mitochondrial
, superoxide dismutase-3 precursor (AA -32 to 203)