| Identification | Back Directory | [Name]
RYNTR | [CAS]
9074-14-0 | [Synonyms]
RYNTR
EC 1.6.4.5
THIOREDOXIN REDUCTASE
Reductase, thioredoxin
thioredoxin-disulfide reductase
THIOREDOXIN REDUCTASE RAT LIVER
Native Rat Thioredoxin Reductase
THIOREDOXIN: NADP+ OXIDOREDUCTASE
THIOREDOXIN REDUCTASE, FROM E. COLI
thioredoxin reductase from rat liver
THIOREDOXIN REDUCTASE, YEAST, RECOMBINANT
NADPH:OXIDISED THIOREDOXIN OXIDOREDUCTASE
NADPH: OXIDIZED THIOREDOXIN OXIDOREDUCTASE
Thioredoxin Reductase from Escherichia coli
Native Escherichia coli Thioredoxin Reductase
Thioredoxin reductase, recombinant from Yeast
rNTR, NADPH: oxidized-thioredoxin oxidoreductase
THIOREDOXIN REDUCTASE, YEAST, RECOMBINANT, E COLI
Thioredoxin Reductase (NADPH) from Yeast, Recombinant
Thioredoxin Reductase from rat liver buffered aqueous glycerol solution, >=100 units/mg protein (Bradford) | [MDL Number]
MFCD00678149 |
| Chemical Properties | Back Directory | [storage temp. ]
2-8°C | [solubility ]
aqueous buffer, pH 7.0: soluble | [form ]
buffered aqueous glycerol solution | [color ]
Colorless to light yellow | [biological source]
r at liver | [Water Solubility ]
water: soluble | [Specific Activity]
≥5units/mg protein |
| Hazard Information | Back Directory | [Uses]
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). 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. |
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Sigma-Aldrich
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Energy Chemical
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Merck Millipore
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Merck KGaA
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