T9698
Thioredoxin Reductase from rat liver
buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford)
Sinónimos:
NADPH:Oxidised Thioredoxin Oxidoreductase, Thioredoxin: NADP+ Oxidoreductase
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50 μG
US$ 653,00
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50 μG
US$ 653,00
About This Item
Número de CAS:
Número MDL:
Código UNSPSC:
12352200
NACRES:
NA.32
Productos recomendados
origen biológico
rat liver
Nivel de calidad
Ensayo
≥90% (GE)
Formulario
buffered aqueous glycerol solution
actividad específica
≥100 units/mg protein (Bradford)
mol peso
55—67 kDa
técnicas
activity assay: suitable
impurezas
Glutathione reductase
solubilidad
water: soluble
idoneidad
suitable for molecular biology
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
Información sobre el gen
rat ... Txnrd1(58819)
Descripción general
Research area: Cell signaling
Aplicación
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.[1] The product can also be used for studying the activation mechanism of transglutaminase 2 (TG2) in the extracellular matrix by using Thioredoxin.[2]
Acciones bioquímicas o fisiológicas
Thioredoxin Reductase is a ubiquitous enzyme that catalyzes the active site disulfide of thioredoxin by NADPH.[3] The product also reduces ubiquinone and regenerates ubiquinol, a powerful antioxidant.[4]
Thioredoxin reductase (TrxR) is a NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidized thioredoxin (Trx).
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.
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.
Definición de unidad
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.
Forma física
Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol.
Código de clase de almacenamiento
12 - Non Combustible Liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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X Peng et al.
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The low-molecular-weight compound APR-246 (PRIMA-1(MET)) restores wild-type conformation and function to mutant p53, and triggers apoptosis in tumor cells. We show here that APR-246 also targets the selenoprotein thioredoxin reductase 1 (TrxR1), a key regulator of cellular redox balance. APR-246
James M May et al.
Clinical biochemistry, 40(15), 1135-1142 (2007-08-04)
The reducing capacity of erythrocytes has been used clinically as to estimate resistance to oxidant stress. In this work we targeted the antioxidant capacity of pyridine nucleotide disulfide reductases of these cells by measuring their ability to reduce the disulfide
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Nucleic acids research, 41(21), 9800-9811 (2013-08-29)
Selenoprotein expression in Escherichia coli redefines specific single UGA codons from translational termination to selenocysteine (Sec) insertion. This process requires the presence of a Sec Insertion Sequence (SECIS) in the mRNA, which forms a secondary structure that binds a unique
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BioFactors (Oxford, England), 18(1-4), 45-50 (2003-12-30)
Ubiquinol is a powerful antioxidant, which is oxidized in action and needs to be replaced or regenerated to be capable of a sustained effort. This article summarises current knowledge of extramitochondrial reduction of ubiquinone by three flavoenzymes, i.e. lipoamide dehydrogenase
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The Journal of biological chemistry, 288(16), 11312-11324 (2013-03-13)
S-nitrosothiols (SNOs), formed by nitric oxide (NO)-mediated S-nitrosylation, and hydrogen peroxide (H2O2), a prominent reactive oxygen species, are implicated in diverse physiological and pathological processes. Recent research has shown that the cellular action and metabolism of SNOs and H2O2 involve
Artículos
Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.
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