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SOD3 encodes a member of the superoxide dismutase (SOD) protein family. Additionally we are shipping SOD3 Kits (66) and SOD3 Proteins (16) and many more products for this protein.
Showing 10 out of 237 products:
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
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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, IHC (fro) - ABIN3044113
Wu, Ming, Zhang, Wu, Wu, Yao: Edaravone rescues the lung by inhibiting lipid peroxidation and pro-inflammatory cytokines in a rat model. in Chinese medical journal 2014
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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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Human Polyclonal SOD3 Primary Antibody for IHC - ABIN5692939
Li, Xiao, Li, Li, Zeng, Liu, Liang, Li, Chu, Yang: Hydrogen sulfide reduced renal tissue fibrosis by regulating autophagy in diabetic rats. in Molecular medicine reports 2018
SOD3 might be a novel player in thyroid tumor stroma.
SOD3 protects mesenchymal stem cells against the negative effects of serum deprivation via modulation of AMP-activated protein kinase (show PRKAA2 Antibodies)/sirtulin 1, extracellular signalregulated kinase activation, and promoted Forkhead box O3a (show FOXO3 Antibodies) trafficking to the nucleus.
Copper chaperone Atox-1 (show ATOX1 Antibodies) is involved in the induction of SOD3 in a monocyte cell line.
the presence of terminal sialic acids in the N-glycans of EC-SOD enhanced both the secretion and furin (show FURIN Antibodies)-mediated C-terminal cleavage of EC-SOD. These results provide new insights into how the posttranslational modifications of EC-SOD control its functions.
Studies suggest that both SOD3 and SOD2 (show SOD2 Antibodies) superoxide dismutases are regulated by oxidative stress and redox-dependent signaling mechanisms.
SOD3 reduced HIF prolyl hydroxylase domain protein activity, which increased hypoxia-inducible factor-2alpha (HIF-2alpha (show EPAS1 Antibodies)) stability and enhanced its binding to a specific vascular endothelial cadherin (show CDH5 Antibodies) promoter region.
EC-SOD released from activated neutrophils affects the redox conditions of the extracellular space and may offer protection against highly reactive oxygen species such as hydroxyl radicals otherwise generated as a result of respiratory burst activity of activated neutrophils.
The results of the present study demonstrate that TET1 (show TET1 Antibodies) might function as one of the key molecules in SOD3 expression through its 5mC hydroxylation in A549 cells.
The SOD3 enzyme plays a role in cardiovascular disease.
SOD3 expression in human idiopathic pulmonary arterial hypertension is in part regulated by histone deacetylation.
Enhanced expression of EcSOD in skeletal muscle profoundly protects against multiple organ dysfunction syndrome by inhibiting endothelial activation and inflammatory cell adhesion.
Epigenetic regulation of EC-SOD expression in aging lung fibroblasts is exerted via histone acetylation.
Results indicate that medium molecular weight heparinyl phenylalanine (MHF) and medium molecular weight heparinyl leucine (MHL) show a radical scavenging ability by increasing the extracellular superoxide dismutase (EC-SOD) activity and MHF may be a candidate for clinical use.
the redistribution of SOD3 as a result of the R213G single-nucleotide polymorphism protects mice from bleomycin-induced fibrosis and secondary pulmonary hypertension by improved resolution of alveolar inflammation.
These data reveal that ecSOD activity modulates neutrophil recruitment and function in a cell-extrinsic fashion, highlighting the importance of the enzyme in protecting tissues from oxidative damage.
wound healing impairments in ageing are associated with increased levels of ROS (show ROS1 Antibodies), decreased SOD3 expression and impaired extracellular oxidative stress regulation
FXR (show NR1H4 Antibodies) may regulate SOD3 expression to suppress reactive oxygen species production, resulting in decreasing JNK (show MAPK8 Antibodies) activity.
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.
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)