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SOD3 encodes a member of the superoxide dismutase (SOD) protein family. Additionally we are shipping SOD3 Antibodies (241) and SOD3 Kits (65) and many more products for this protein.
Showing 10 out of 16 products:
Human SOD3 Protein expressed in Wheat germ - ABIN1320950
Fujiwara, Duscher, Rustad, Kosaraju, Rodrigues, Whittam, Januszyk, Maan, Gurtner: Extracellular superoxide dismutase deficiency impairs wound healing in advanced age by reducing neovascularization and fibroblast function. in Experimental dermatology 2016
Copper chaperone Atox-1 (show ATOX1 Proteins) 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 Proteins)-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 Proteins) 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 Proteins)) stability and enhanced its binding to a specific vascular endothelial cadherin (show CDH5 Proteins) 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 Proteins) 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 (show SQSTM1 Proteins) cell damage.
Study shows that patients with the Ala40Thr polymorphism in EC-SOD are at a higher risk of developing type 2 diabetes mellitus.
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 Proteins), decreased SOD3 expression and impaired extracellular oxidative stress regulation
FXR (show NR1H4 Proteins) may regulate SOD3 expression to suppress reactive oxygen species production, resulting in decreasing JNK (show MAPK8 Proteins) 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 Proteins) 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 (show HMOX1 Proteins) 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)