Thioredoxin Reductase from Escherichia coli

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

NADPH:oxidized thioredoxin oxidoreductase
CAS Number:
Enzyme Commission number:
MDL number:

biological source

Escherichia coli

Quality Level


ammonium sulfate suspension

specific activity

>25 units/mg protein (Bradford)

mol wt

70 kDa


activity assay: suitable

UniProt accession no.

storage temp.


Gene Information

Escherichia coli K12 ... trxB(949054)


Thioredoxin Reductase from Escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of Cys-based thiol peroxidases. The product was used for determining the enzymatic activity of His6-Ahp1p.
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.


250 μg in poly bottle

Biochem/physiol Actions

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.
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 (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.

Unit Definition

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.

Physical form

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


NONH for all modes of transport

WGK Germany


Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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)
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)...
Luciano Oehninger et al.
Dalton transactions (Cambridge, England : 2003), 42(5), 1657-1666 (2012-11-15)
Metal complexes with N-heterocyclic carbene (NHC) ligands have been widely used in catalytic chemistry and are now increasingly considered for the development of new chemical tools and metal based drugs. Ruthenium complexes of the type (p-cymene)(NHC)RuCl(2) interacted with biologically relevant...
Kely Navakoski de Oliveira et al.
ChemMedChem, 8(2), 256-264 (2013-01-03)
Thioredoxin reductase (TrxR) is overexpressed in cancer cells and is therefore a putative cancer target. Inhibition of this enzyme is considered an important strategy for the development of new chemotherapeutic agents with a specific mechanism of action. Organotin compounds have...
Instructions for working with enzymes supplied as ammonium sulfate suspensions
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