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100 µl

Ref. YIF-LF-MA0015
ABFRONTIER

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Neuf 321.00 H.T.
en stock

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Détails Produit

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). Plays a central role as a glucosyl donor in cellular metabolic pathways.

Alternate Names/Synonyms: TR; TXNRD1; GRIM12; GRIM-12; EC=1.8.1.9; Thioredoxin Reductase TR1; Thioredoxin Reductase 1; Cytoplasmic; KM-102-derived Reductase-like Factor; Gene Associated with Retinoic and IFN-induced Mortality 12 Protein

Product Type: Monoclonal Antibody

Clone: 19A1

Isotype: Mouse IgG1 kappa

Immunogen: Recombinant human protein purified from E. coli.

Applications: ELISA, IP, WB

Species Crossreactivity: Human

Formulation: Liquid. HEPES with 0.15M NaCl, 0.01% BSA, 0.03% sodium azide, and 50% glycerol.

Short Term Storage: +4°C

Long Term Storage: -20°C

Shipping: BLUE ICE

Use & Stability: Stable for at least 1 year after receipt when stored at -20°C.

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Literature References: 1) Mustacich, D. and Powis,G. (2000) Biochem J. 15. 346 Pt 1:1-8. (General)