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Material Database:
Thioredoxin Reductase from rat liver
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| Producer |
SUPELCO by Sigma-Aldrich
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| Status |
Available |
| Material |
Liquid |
| Reference |
T9698 |
| Catalog (Web) |
http://www.sigmaaldrich.com/catalog/search/ProductDetail/S
IGMA/T9698 |
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Description
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buffered aqueous glycerol solution Synonym NADPH:Oxidised Thioredoxin Oxidoreductase
Thioredoxin: NADP+ Oxidoreductase
MDL number MFCD00678149 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.
Unit Definition 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. D 8130] alone as substrate) per minute at pH 7.0 at 25 °C. Physical form Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol
activity 100-300 units/mg protein (Bradford)
Shipped in dry ice
storage temp. −20°C
References: Holmgren, A., and Bjornstedt, M. Meth. Enzymol. 252, 199-208, (1995) Williams, C.H., et al. Eur. J. Biochem. 267, 6110-6117, (2000) Fujiwara, N., et al. Biochem. J. 340, 439-444, (1999)
Zhong, L., and Holmgren, A. J. Biol. Chem. 275, 18121, (2000)
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