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Thioredoxin reductase (TR) is a dimeric NADPH-dependent FAD containing enzyme that catalyzes the reduction of the active site disulfide of thioredoxin and other substrates. Additionally we are shipping Thioredoxin Reductase 2 Antibodies (58) and Thioredoxin Reductase 2 Kits (3) and many more products for this protein.
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A meta-analysis of the top SNPs identified three new associated loci in primary open angle glaucoma--TXNRD2, ATXN2 (show ATXN2 Proteins), and FOXC1 (show FOXC1 Proteins)
The TXNRD2 rs 1548357 polymorphism might be a genetic risk factor for Myocardial infarction in subjects with T2 Diabetes mellitus of Slovenian origin.
Data suggest TXNRD1 (show TXNRD1 Proteins) and TXRNRD2 function at the top of a redox pyramid that governs the oxidation state of peroxiredoxins and other protein factors, thereby dictating a hierarchy of phenotypic responses to oxidative insults.
Absence of TXNRD2 in humans leads to glucocorticoid deficiency.
Single Nucleotide Polymorphisms in the genes GPX1 (show GPX1 Proteins) (rs1050450, rs1800668 and rs3811699), TrxR2 (rs5748469), and DIO2 (show DIO2 Proteins) (rs225014) may not be significantly associated with Kashin-Beck disease in a Tibetan population.
Development of subcutaneous fibrosis can be associated with genetic variation in the mitochondrial enzyme TXNRD2, critically involved in removal of ROS (show ROS1 Proteins), and maintenance of the intracellular redox balance.
Data suggest that dietary factor (selenium supplementation) up-regulates endogenous antioxidant systems and protects trophoblasts from oxidative stress; selenium upregulates GPX1 (glutathione peroxidase 1 (show GPX1 Proteins)) and thioredoxin (show TXN Proteins) reductases (TXNRD1 (show TXNRD1 Proteins); TXNRD2).
A role of GPx2 (show GPX2 Proteins), TrxR2 and TrxR3 (show TXNRD3 Proteins) in proliferation, apoptosis and, therefore, also during cancer development.
No obvious correlation can be found between rs5748469 polymorphisms in TrxR2 gene and the susceptibility to Kashin-Beck disease.
study reveals significant differences between TrxR1 (show TXNRD1 Proteins) and TrxR2 in substrate specificity and metal compound inhibition in vitro and in cells
Suggest role for Txnrd2 in sustaining heart function during aging and suggest that Txnrd2 may be a modifier of heart failure.
Regulatory link was discovered between mitochondrial Txnrd and the JNK (show MAPK8 Proteins)-PHD2 (show EGLN1 Proteins)-Hif-1alpha (show HIF1A Proteins) axis, which highlights how the loss of Txnrd2 and the resulting altered mitochondrial redox balance impairs tumor growth as well as tumor-related angiogenesis.
The SirT1 (show SIRT1 Proteins) regulates the expression of several antioxidant genes in bovine aortic endothelial cells, including Mn superoxide dismutase (show SOD2 Proteins), catalase (show CAT Proteins), peroxiredoxins 3 and 5, thioredoxin 2 (show TXN2 Proteins), thioredoxin reductase 2, and uncoupling protein 2 (show UCP2 Proteins).
Data indicate that mammalian thioredoxin reductase (H-TrxR) reduces hypothiocyanous acid (HOSCN).
Txnrd2 exerts a crucial function during postischemic reperfusion via thiol regeneration.
Energization of mitochondria increases the antioxidant potential of the TrxR2/Trx2 (show TXN2 Proteins) system and that inhibition of TrxR2 results in increased H(2)O(2) emission.
Genomic organization and identification of a novel alternative splicing variant of mouse mitochondrial TrxR2 gene
Neither Trx2 (show TXN2 Proteins) nor TrxR2 gain of function modified the redox regulation of mitochondria-dependent apoptosis in cos-7 cells, Hela cells and Mouse Neuro2a cells.
Cardiac tissue-restricted ablation of thioredoxin reductase 2 results in fatal dilated cardiomyopathy
Thioredoxin reductase (TR) is a dimeric NADPH-dependent FAD containing enzyme that catalyzes the reduction of the active site disulfide of thioredoxin and other substrates. TR is a member of a family of pyridine nucleotide-disulfide oxidoreductases and is a key enzyme in the regulation of the intracellular redox environment. Three thioredoxin reductase genes have been found that encode selenocysteine containing proteins. This gene partially overlaps the COMT gene on chromosome 22.
, thioredoxin reductase
, selenoprotein Z
, thioredoxin reductase 2, mitochondrial
, thioredoxin reductase 3
, thioredoxin reductase TR3
, thioredoxin reductase beta
, TR beta