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T7915

Sigma-Aldrich

Thioredoxin Reductase from Escherichia coli

ammonium sulfate suspension, >25 units/mg protein (Bradford)

Synonyme(s) :

NADPH:oxidized thioredoxin oxidoreductase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.32

Source biologique

Escherichia coli

Niveau de qualité

Forme

ammonium sulfate suspension

Activité spécifique

>25 units/mg protein (Bradford)

Poids mol.

70 kDa

Technique(s)

activity assay: suitable

Numéro d'accès UniProt

Température de stockage

2-8°C

Informations sur le gène

Escherichia coli K12 ... trxB(949054)

Description générale

Research area: Cell Signaling
Thioredoxin reductases (TrxRs) belongs to family of selenium-containing pyridine nucleotide-disulphide oxidoreductases.

Application

Thioredoxin Reductase from Escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of Cys-based thiol peroxidases.Thioredoxin Reductase from Escherichia coli has been used:
  • for determining the enzymatic activity of His6-Ahp1p.
  • to assay C. elegans TRXR using the TXN-dependent activity assay.
  • to investigate the biological reducing systems for organic hydroperoxide resistance R gene (OhrR).
  • for enzymatic targeting of auranofin to test its antimicrobial properties.
  • in thioredoxin reductase activity and peroxiredoxin assay.
  • to study the synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes.
Thioredoxin reductase from Escherichia coli has been used in thioredoxin reductase activity and peroxiredoxin assay.
It has also been used to study the synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes.

Actions biochimiques/physiologiques

An FAD-containing enzyme involved in the transfer of hydrogen from E. coli thioredoxin to other proteins thus providing a powerful disulfide reductase system.
Thioredoxin reductase is a FAD containing enzyme, which transfers the reducing equivalent from NADPH to the disulphide bond of the enzyme by using FAD moiety within the Cys-Ala-Thr-Cys sequence. It can also reduce Trx-S2 to Trx-(SH)2 by using NADPH.
Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide.

Définition de l'unité

One unit will cause an increase in absorbance of 1.0 at 412 nm (when measured in a coupled assay with E. coli thioredoxin and DTNB) per min per mL at pH 7.0 at 25 °C.

Forme physique

Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

Deletion of Thioredoxin Reductase and Effects of Selenite and Selenate Toxicity in Caenorhabditis elegans
Boehler CJ, et al.
PLoS ONE, 8(8), e71525-e71525 (2013)
Synergy between broccoli sprout extract and selenium in the upregulation of thioredoxin reductase in human hepatocytes
Li D, et al.
Food Chemistry, 110(1), 193-198 (2008)
NR1D1 Recruitment to Sites of DNA Damage Inhibits Repair and Is Associated with Chemosensitivity of Breast Cancer
Ka NL, et al.
Journal of Separation Science, 77(9), 2453?2463-2453?2463 (2017)
Purification and characterization of ferredoxin-NAD (P)+ reductase from the green sulfur bacterium Chlorobium tepidum
Seo D, et al.
Biochim. Biophys. Acta Gen. Subj., 1597(1), 123-132 (2002)
Valérie Prouzet-Mauléon et al.
The Journal of biological chemistry, 277(7), 4823-4830 (2001-11-24)
Yeasts lacking cytoplasmic superoxide dismutase (Cu,Zn-SOD) activity are permanently subjected to oxidative stress. We used two-dimensional PAGE to examine the proteome pattern of Saccharomyces cerevisiae strains lacking Cu,Zn-SOD. We found a new stable form of alkyl hydroperoxide reductase 1 (Ahp1)

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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