T9698
Thioredoxin Reductase from rat liver
buffered aqueous glycerol solution, ≥100 units/mg protein (Bradford)
Synonym(s):
NADPH:Oxidised Thioredoxin Oxidoreductase, Thioredoxin: NADP+ Oxidoreductase
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About This Item
CAS Number:
UNSPSC Code:
12352200
NACRES:
NA.32
MDL number:
Form:
buffered aqueous glycerol solution
Assay:
≥90% (GE)
Biological source:
rat liver
Mol wt:
55—67 kDa
biological source
rat liver
assay
≥90% (GE)
form
buffered aqueous glycerol solution
specific activity
≥100 units/mg protein (Bradford)
mol wt
55—67 kDa
technique(s)
activity assay: suitable
impurities
Glutathione reductase
solubility
water: soluble
suitability
suitable for molecular biology
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Quality Level
Gene Information
rat ... Txnrd1(58819)
General description
Research area: Cell signaling
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 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.
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.
Physical form
Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol.
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.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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Luciano Oehninger et al.
Dalton transactions (Cambridge, England : 2003), 42(5), 1657-1666 (2012-11-15)
Metal complexes with N-heterocyclic carbene (NHC) ligands have been widely used in catalytic chemistry and are now increasingly considered for the development of new chemical tools and metal based drugs. Ruthenium complexes of the type (p-cymene)(NHC)RuCl(2) interacted with biologically relevant
Kely Navakoski de Oliveira et al.
ChemMedChem, 8(2), 256-264 (2013-01-03)
Thioredoxin reductase (TrxR) is overexpressed in cancer cells and is therefore a putative cancer target. Inhibition of this enzyme is considered an important strategy for the development of new chemotherapeutic agents with a specific mechanism of action. Organotin compounds have
Aristi P Fernandes et al.
PloS one, 7(11), e50727-e50727 (2012-12-12)
Naturally occurring selenium compounds like selenite and selenodiglutathione are metabolized to selenide in plants and animals. This highly reactive form of selenium can undergo methylation and form monomethylated and multimethylated species. These redox active selenium metabolites are of particular biological
Arun Kumar Selvam et al.
Antioxidants (Basel, Switzerland), 9(2) (2020-02-09)
Kynurenine aminotransferase 1 (KYAT1 or CCBL1) plays a major role in Se-methylselenocysteine (MSC) metabolism. It is a bi-functional enzyme that catalyzes transamination and beta-elimination activity with a single substrate. KYAT1 produces methylselenol (CH3SeH) via β-elimination activities with MSC as a
L Zhong et al.
The Journal of biological chemistry, 275(24), 18121-18128 (2000-06-13)
Mammalian thioredoxin reductases (TrxR) are dimers homologous to glutathione reductase with a selenocysteine (SeCys) residue in the conserved C-terminal sequence -Gly-Cys-SeCys-Gly. We removed the selenocysteine insertion sequence in the rat gene, and we changed the SeCys(498) encoded by TGA to
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