Thioredoxin Reductase from rat liver
SIGMA/T9698 - buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford)
Synonym: NADPH:Oxidised Thioredoxin Oxidoreductase; Thioredoxin: NADP+ Oxidoreductase
CAS Number: 9074-14-0
MDL Number: MFCD00678149
Product Type: Chemical
Unit Definition The assay of thioredoxin reductase (TrxR) uses 5,5’-dithiobis(2-nitrobenzoic acid) (DTNB) as a substrate. TNB (5’-thionitrobenzoic acid) has a strong yellow color, which can be measured at 412 nm- one unit will cause the increase of A412 of 1.0 per minute at pH 7.0 at 25 °C (when measured in a non-coupled assay containing DTNB alone as the substrate).
| assay | ≥90% (GE) |
| biological source | rat liver |
| form | buffered aqueous glycerol solution |
| impurities | Glutathione reductase |
| mol wt | 55—67 kDa |
| Quality Level | 200  |
| shipped in | dry ice |
| solubility | water: soluble |
| specific activity | ≥100 units/mg protein (Bradford) |
| storage temp. | −20°C |
| suitability | suitable for molecular biology |
| technique(s) | activity assay: suitable |
| UniProt accession no. | O89049  |
| Application: | Thioredoxin Reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid by utilizing reducing capacity of human erythrocytes. The product can also be used for studying the activation mechanism of transglutaminase 2 (TG2) in the extracellular matrix by using Thioredoxin. |
| Biochem/physiol Actions: | Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized thioredoxin (Trx). |
| Biochem/physiol Actions: | Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized 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 non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxide. |
| Biochem/physiol Actions: | Thioredoxin reductase from mammalian sources contains a selenocysteine residue that is essential for the activity of the enzyme. It is one of the antioxidant enzymes present in the mammalian cell together with catalase, glutathione peroxidase and superoxide dismutase, and helps in removal of reactive oxygen species (ROS) from the cell. An example is the removal of excess nitric oxide (NO) by the formation of a complex with glutathione forming the S-nitroso-glutathione adduct (GS-NO). This can be cleaved directly by thioredoxin reductase. Hydrogen peroxide, another deleterious oxidant in the cell, is also reduced directly by mammalian TrxR. |
| Biochem/physiol Actions: | Thioredoxin Reductase is a ubiquitous enzyme that catalyzes the active site disulfide of thioredoxin by NADPH. The product also reduces ubiquinone and regenerates ubiquinol, a powerful antioxidant. |
| General description: | Research area: Cell signaling |
| Other Notes: | One unit will cause an increase in absorbance of 1.0 at 412 nm (when measured in a non-coupled assay containing DTNB [Sigma No. D8130] alone as substrate) per minute at pH 7.0 at 25 °C. |
| Packaging: | 50 μg in glass bottle |
| Physical form: | Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| Purity | ≥90% (GE) |
| activity | specific activity: ≥100 units/mg protein (Bradford) |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 1.8.1.9 ( BRENDA | IUBMB ) |
| UNSPSC | 12352200 |