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The ratio of thioredoxin/Keap1 (show KEAP1 Proteins) protein level may be useful for suggesting distant metastasis in colorectal cancer.
Overexpression of NOS3 (show NANOS3 Proteins) increased the levels and activities of proteins of the redoxin systems, Trx1 (show MLL Proteins), Grx1 (show GRX1 Proteins), TrxR1 (show TXNRD1 Proteins) and TxnIP (show TXNIP Proteins), and the levels of signaling proteins (Akt1 (show AKT1 Proteins), pAkt1(-)Ser473, MapK (show MAPK1 Proteins), pMapK, Stat3 (show STAT3 Proteins), Fas (show FAS Proteins)).
Increased serum thioredoxin concentrations are highly associated with trauma severity
Plasma-TRX on day 1 was significantly increased in patients who later developed (show VAC14 Proteins) post-injury sepsis. In a logistic regression analysis including TRX, C-reactive protein, injury severity, massive transfusion, and admission blood pressure, TRX was the only variable independently associated with post-injury sepsis
High TRX1 (show MLL Proteins) expression is associated with myocardial infarction.
Data show that suberoylanilide hydroxamic acid (SAHA) induced apoptosis via the down-regulation thioredoxin1 (Trx1 (show MLL Proteins)), which was regulated by microRNA miR (show MLXIP Proteins)-129-5p.
Analysis of 25 independent cohorts with 5910 patients showed that Trx1 (show MLL Proteins) and TrxR1 (show TXNRD1 Proteins) were both associated with a poor patient prognosis in terms of overall survival, distant metastasis free survival and disease free survival.
these findings demonstrate that Trx1 is a critical regulator of necroptosis that suppresses cell death by maintaining MLKL in a reduced inactive state.
Study shows that TRX1 (show MLL Proteins) and APEX1 (show APEX1 Proteins) expressions are up regulated in new Multiple Sclerosis (MS) patients compared to controls and might be implicated in pathogenesis of the disease.
CD40 (show CD40 Proteins) activation resulted in down-regulation of Thioredoxin (Trx)-1 to permit ASK1 (show MAP3K5 Proteins) activation and apoptosis. Although soluble receptor (show IFNAR1 Proteins) agonist alone could not induce death, combinatorial treatment incorporating soluble CD40 (show CD40 Proteins) agonist and pharmacological inhibition of Trx-1 (show MLL Proteins) was functionally equivalent to the signal triggered by mCD40L
A novel mouse model for the identification of thioredoxin-1 protein interactions has been created.
Serum thioredoxin reductase (show PRDX2 Proteins) is highly increased in mice with hepatocellular carcinoma and its activity is restrained by several mechanisms, in particular, by the serum QSOX1 (show QSOX1 Proteins).
Nuclear overexpression of Trx1 restored Nrf2 (show NFE2L2 Proteins) activity and attenuated alcohol-induced acute lung injury.
Trx1 enhances blood perfusion and increases angiogenic protein expression in a rodent hind limb ischemia model.
GSR (show GSR Proteins) is not essential for the maintenance of antioxidant defenses in mouse cochlea; the thioredoxin/thioredoxin reductase (show PRDX2 Proteins) system can probably operate as a functional backup for GSR (show GSR Proteins).
These results strongly suggest that Trx1 ameliorates the myocardial effects of I/R by improving the free radical-mediated damage in cardiac and mitochondrial function, opening the possibility of new therapeutic strategies in coronary artery disease.
findings support the potential pathophysiological relevance of TRX in celiac disease and establish the Cys (show DNAJC5 Proteins)(370)-Cys (show DNAJC5 Proteins)(371) disulfide bond of TG2 (show TGM2 Proteins) as one of clearest examples of an allosteric disulfide bond in mammals.
Thioredoxin-mediated deglutathionylation of eNOS (show NOS3 Proteins) in the coronary artery in vivo protected against reperfusion injury, even in the presence of normal levels of glutathione.
Acute stimuli of epinephrine induced Trx-1 expression through activating CREB (show CREB1 Proteins).
results suggest that PostC prevents Trx-1 degradation, decreasing oxidative stress and allowing the activation of Akt and GSK3beta to exert its cardioprotective effect
In pigs, however not significant, there was a continuing increase in plasma-TRX after femur fracture and sequential hemorrhage despite near normalisation of cardiac index and lactate levels.
single-marker and haplotype analyses revealed significant effects of TXNIP (show TXNIP Proteins) on hot carcass weight, test daily gain, and lifetime daily gain
Crystallization and X-ray crystallographic analysis of recombinant Trx1 has been reported.
Thioredoxin-h5 (TRXh5) reverses SNO modifications by acting as a selective protein-SNO reductase.
Data indicate that thioredoxin h proteins are not required to prevent the spontaneous activation of S-locus receptor kinase (SRK (show ZAP70 Proteins)) in the stigma.
Redox regulation of AtCPK21 by Trx-h1 in Arabidopsis thaliana in response to external stimuli is important for appropriate cellular responses.
in LOV1's absence, victorin inhibits TRX-h5, resulting in compromised defense but not disease by C. victoriae; in LOV1's presence, victorin binding to TRX-h5 activates LOV1 and elicits a resistance-like response that confers disease susceptibility
Structral model of thioredoxin h1 from Arabidopsis thaliana in the oxidized state displays the conserved thioredoxin fold.
Data show that thioredoxin h5 (ATTRX5), but not ATTRX3, is highly induced in sensitive Arabidopsis following victorin treatment.
regulation of NPR1 is through the opposing action of S-nitrosoglutathione and thioredoxins; findings suggest a link between pathogen-triggered redox changes and gene regulation in plant immunity
The protein encoded by this gene acts as a homodimer and is involved in many redox reactions. The encoded protein is active in the reversible S-nitrosylation of cysteines in certain proteins, which is part of the response to intracellular nitric oxide. This protein is found in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene.
, ATL-derived factor
, TXN delta 3
, surface-associated sulphydryl protein
, thioredoxin delta 3
, thioredoxin-like protein