Yeast Thioredoxin 1 (DAG4448)

Yeast Thioredoxin 1, recombinant protein from E. coli

Product Overview
Yeast Thioredoxin 1
Nature
Recombinant
Tag/Conjugate
Unconjugated
Procedure
1mM EDTA
Concentration
1.0 mg/ml
Buffer
20mM Tris, pH 7.5/10mM NaCl/1mM EDTA
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Thioredoxins (Trx) are small, multi-functional proteins with oxidoreductase activity and are ubiquitous in essentially all living cells. Trx contains a redox-active disulfide/dithiol group within the conserved Cys-Gly-Pro-Cys active site. The two cysteine residues in the conserved active centers can be oxidized to form intramolecular disulfide bonds. Reduction of the active site disulfide in oxidized Trx is catalyzed by Trx reductase with NADPH as the electron donor. The reduced Trx is a hydrogen donor for ribonucleotide reductase, the essential enzyme for DNA synthesis, and a potent general protein disulfide reductase with numerous functions in growth and redox regulations. Specific protein disulfide targets for reduction by Trx include protein disulfide –isomerase (PDI) and a number of transcription factors such as p53, NFkB and AP-1 (T1–151). Trx is also capable of removing H2O2, particularly when it is coupled with either methionine sulfoxide reductase or several isoforms of peroxiredoxins.
Keywords
TXN; thioredoxin; TRX; ADF; Surface associated sulphydryl protein; TXN protein; ATL derived factor; ATL-derived factor; DKFZp686B1993; MGC61975; SASP; Surface-associated sulphydryl protein; THIO_HUMAN; Thioredoxin; TRDX;

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References


Flavonoid VI-16 protects against DSS-induced colitis by inhibiting Txnip-dependent NLRP3 inflammasome activation in macrophages via reducing oxidative stress

MUCOSAL IMMUNOLOGY

Authors: Zhao, Yue; Guo, Qinglong; Zhu, Qin; Tan, Renxiang; Bai, Dongsheng; Bu, Xiumin; Lin, Binyan; Zhao, Kai; Pan, Chuyue; Chen, Haiyan; Lu, Na

Emerging evidence suggests that NLRP3 inflammasome was associated with various kinds of immunological diseases including colitis. However, there are few drugs targeting inflammasomes in the treatment of colitis. Several flavonoids have been found to affect the inflammasome pathway, but the mechanism is still confusing. Here we report that VI-16, a synthetic flavonoid compound, exerts potent anti-inflammatory effects on macrophages in DSS-induced colitis mice, which intervened in the activation of NLRP3 inflammasome without affecting intestinal epithelial cells. However, the protection of VI-16 against DSS-induced colitis was dependent on NLRP3 expression in hematopoietic cells. Furthermore, this inhibitory effect of VI-16 was found to be at least partially achieved by decreasing the mitochondria) ROS generation without affecting autophagy. Further studies confirm that VI-16 inhibits the binding of Txnip to NLRP3 by reducing oxidative stress and ultimately inhibits NLRP3 inflammasome. This demonstrates the ability of VI-16 to inhibit the NLRP3 inflammasome activation and its potential use in the treatment of inflammatory bowel disease.

Glucocorticoid Upregulates Thioredoxin-interacting Protein in Cultured Neuronal Cells

NEUROSCIENCE

Authors: Bharti, Veni; Tan, Hua; Chow, Desiree; Wang, Yiran; Nagakannan, Pandian; Eftekharpour, Eftekhar; Wang, Jun-Feng

Previous studies have shown that chronic stress and chronic stress hormone treatment induce oxidative damage in rodents. Thioredoxin (Trx) is a small redox protein that plays an important role in regulation of oxidative protein cysteine modification. A Trx reduced state is maintained by thioredoxin reductase (TrxR), and the thioredoxin-interacting protein (Txnip) is an endogenous inhibitor of Trx. The purpose of this study was to investigate the effects of chronic treatment with stress hormone corticosterone on Trx, TrxR and Txnip in cultured neuronal cells. Using immunoblotting analysis we found that although chronic corticosterone treatment had no effect on Trx and TrxR protein levels, this treatment significantly increased Txnip protein levels. Using immunocytochemistry we also found that chronic corticosterone treatment increased Txnip in both nucleus and cytosol, while glucocorticoid receptor inhibitor RU486 can block corticosterone-increased Txnip protein levels. Using biotin switch, dimedone conjugation and CRISPR/Cas9 methods we found that chronic corticosterone treatment increased protein nitrosylation and sulfenylation, while knocking out Txnip blocked corticosterone-induced protein nitrosylation and sulfenylation. Since Trx can reduce cysteine oxidative protein modification such as nitrosylation and sulfenylation, our findings suggest that chronic corticosterone treatment may upregulate Txnip by targeting glucocorticoid receptor, subsequently inhibiting Trx activity and enhancing oxidative protein cysteine modification, which contributes to corticosterone-caused oxidative damage. (C) 2018 IBRO. Published by Elsevier Ltd. All rights reserved.

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