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Product Description: The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxido-reductases. All the mammalian TrxRs are homologous to glutathione reductase with respect to primary structure including the conserved redox catalytic site (-Cys-Val-Asn-Val-Gly-Cys-) but distinctively with a C-terminal extension containing a catalytically active penultimate selenocysteine (SeCys) residue in the conserved sequence(-Gly-Cys-SeCys-Gly). TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. Electrons are transferred from NADPH via FAD and the active-site disulfide to C-terminal SeCys-containing redox center, which then reduces the substrate like thioredoxin. The members of TrxR family are 55 58 kilodalton in molecular size and composed of three isoforms including cytosolic TrxR1, mitochondrial TrxR2, and TrxR3, known as Trx and GSSG reductase (TGR). TrxR plays a key role in protection of cells against oxidative stress and redox-regulatory mechanism of transcription factors and various biological phenomena (1).
Alternate Names/Synonyms: TR; TXNRD1; GRIM12; GRIM-12; EC=1.8.1.9; Thioredoxin Reductase TR1; KM-102-derived Reductase-like Factor; Thioredoxin Reductase 1; Cytoplasmic; Gene Associated with Retinoic and IFN-induced Mortality 12 Protein
Product type: Protein
Source / Host: E. coli
Species Crossreactivity: Human
Purity: >95% (SDS-PAGE)
Formulation: Lyophilized from 20mM HEPES, pH 7.0, 1mM EDTA.
Handling Advice: Avoid freeze/thaw cycles.
Short Term Storage: +4°C
Long Term Storage: -20°C
Shipping: BLUE ICE
Use & Stability: After reconstitution, store at -80°C.
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