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Human Polyclonal TXNRD2 Primary Antibody für IHC, IHC (p) - ABIN4363625
Wirth, Conrad, Winterer, Wozny, Carlson, Roth, Schmitz, Bornkamm, Coppola, Tessarollo, Schomburg, Köhrle, Hatfield, Schweizer: Neuronal selenoprotein expression is required for interneuron development and prevents seizures and neurodegeneration. in FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2010
Show all 4 Pubmed References
Based on recent research, it has been reported that the modulation of the Trx/TrxR (zeige GSR Antikörper) system may be considered as a new target in the management of the metabolic syndrome, insulin (zeige INS Antikörper) resistance, and type 2 diabetes, as well as in the treatment of hypertension and atherosclerosis. In this review evidence about a possible role of this system as a marker of the metabolic syndrome is reported. [review]
TrxR2 was overexpressed in non-small-cell lung cancer cells; our results suggest that TrxR2 acts as an oncogenic gene in the context of lung cancer progression
p53R2 (zeige RRM2B Antikörper) acts as a positive regulator of TrxR2 activity in mitochondria both under normal physiological conditions and during the cellular response to DNA damage
TrxR2 deficiency-induced impaired proliferation and death of chondrocytes may be the pathological mechanism of the osteoarthropathy due to Selenium deficiency.
Evidence that the rs4485648 polymorphism of the TrxR2 gene might exert an independent effect on the development of Diabetic retinopathy.
Data suggest that TXNRD2 may represent a druggable target that could be deployed to reduce the development of fatal pulmonary metastases in patients with osteosarcoma (OS).
A meta-analysis of the top SNPs identified three new associated loci in primary open angle glaucoma--TXNRD2, ATXN2 (zeige ATXN2 Antikörper), and FOXC1 (zeige FOXC1 Antikörper)
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 (zeige TXNRD1 Antikörper) 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.
Maintenance of mitochondrial ROS (zeige ROS1 Antikörper) via Txnrd2 in endothelial cells is necessary for an intact vascular homeostasis and remodeling. Txnrd2 plays a vitally important role in balancing mitochondrial ROS (zeige ROS1 Antikörper) production in the endothelium.
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 (zeige MAPK8 Antikörper)-PHD2 (zeige EGLN1 Antikörper)-Hif-1alpha (zeige HIF1A Antikörper) 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 (zeige SIRT1 Antikörper) regulates the expression of several antioxidant genes in bovine aortic endothelial cells, including Mn superoxide dismutase (zeige SOD2 Antikörper), catalase (zeige CAT Antikörper), peroxiredoxins 3 and 5, thioredoxin 2 (zeige TXN2 Antikörper), thioredoxin reductase 2, and uncoupling protein 2 (zeige UCP2 Antikörper).
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 (zeige TXN2 Antikörper) 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 (zeige TXN2 Antikörper) nor TrxR2 gain of function modified the redox regulation of mitochondria-dependent apoptosis in cos-7 cells, Hela cells and Mouse Neuro2a cells.
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