Thioredoxin Reductase from Escherichia coli
SIGMA/T7915 - ammonium sulfate suspension, >25 units/mg protein (Bradford)
Synonym: NADPH:oxidized thioredoxin oxidoreductase
CAS Number: 9074-14-0
MDL Number: MFCD00678149
Product Type: Chemical
The reduction of ribonucleotides, which is essential for DNA synthesis in E. coli is carried out by the enzyme ribonucleotide diphosphate reductase (E.C. 1.17.4.1).1 This reduction reaction is coupled in vitro to the oxidation of NADPH via the small protein thioredoxin (TRX) and thioredoxin reductase.
| biological source | Escherichia coli |
| form | ammonium sulfate suspension |
| mol wt | 70 kDa |
| Quality Level | 200  |
| specific activity | >25 units/mg protein (Bradford) |
| storage temp. | 2-8°C |
| technique(s) | activity assay: suitable |
| UniProt accession no. | P0A9P4  |
| Application: | 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. |
| 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. • 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. |
| Biochem/physiol Actions: | An FAD-containing enzyme involved in the transfer of hydrogen from E. coli thioredoxin to other proteins thus providing a powerful disulfide reductase system. |
| Biochem/physiol Actions: | 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. |
| 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. |
| General description: | Research area: Cell Signaling Thioredoxin reductases (TrxRs) belongs to family of selenium-containing pyridine nucleotide-disulphide oxidoreductases. |
| Other Notes: | 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. |
| Packaging: | 250 μg in poly bottle |
| Physical form: | Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: >25 units/mg protein (Bradford) |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 1.8.1.9 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |