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SOD3 encodes a member of the superoxide dismutase (SOD) protein family.
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Human SOD3 Kit ELISA pour Sandwich ELISA - ABIN858369
Yang, Li, Zhang, Lin, Zhang, Zhang, Yu, Liu, Li, Zhang, Lv, Xie, Lu, Wu, Teng, Lu, He, Mo: Serum quantitative proteomic analysis reveals potential zinc-associated biomarkers for nonbacterial prostatitis. dans The Prostate 2015
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Human SOD3 Kit ELISA pour Sandwich ELISA - ABIN2685500
Fukai, Folz, Landmesser, Harrison: Extracellular superoxide dismutase and cardiovascular disease. dans Cardiovascular research 2002
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Human SOD3 Kit ELISA pour Sandwich ELISA - ABIN415162
Arce-Varas, Abate, Prandelli, Martínez, Cuetos, Menéndez, Marziano, Cabrera-García, Fernández-Sánchez, Novelli, Memo, Uberti: Comparison of Extracellular and Intracellular Blood Compartments Highlights Redox Alterations in Alzheimer's and Mild Cognitive Impairment Patients. dans Current Alzheimer research 2016
Rat (Rattus) SOD3 Kit ELISA pour Sandwich ELISA - ABIN416451
Yin, Jiang, Huang, Gong, You, Yang, Chen, Chen, Yuan, Li, Hu, Zhao, Peng: Burn Serum IncreasesStaphylococcus aureusBiofilm Formation via Oxidative Stress. dans Frontiers in microbiology 2017
Studies suggest that both SOD3 and SOD2 (Montrer SOD2 Kits ELISA) 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 (Montrer EPAS1 Kits ELISA)) stability and enhanced its binding to a specific vascular endothelial cadherin (Montrer CDH5 Kits ELISA) 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 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.
These data provide new insights into the functional actions of SOD3 on oxidative stress-induced (Montrer SQSTM1 Kits ELISA) 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 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.
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 (Montrer ROS1 Kits ELISA), decreased SOD3 expression and impaired extracellular oxidative stress regulation
FXR (Montrer NR1H4 Kits ELISA) may regulate SOD3 expression to suppress reactive oxygen species production, resulting in decreasing JNK (Montrer MAPK8 Kits ELISA) 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 (Montrer NOS3 Kits ELISA) activity, further compromising pulmonary vascular function.
Our results suggest that EC-SOD plays a dynamic role in the inflammatory response mounted by activated macrophages.
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 (Montrer HMOX1 Kits ELISA) 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)