Thioredoxin Reductase Yeast (E.coli)

Introduction to the Molecule

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 enultimate 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.

Source

E. coli

Storage, Stability/Shelf Life

Yeast thioredoxin reductase is supplied with a vial of storage buffer (20mM HEPES, pH 7.5/ 1mM EDTA). Store at –80°C.

By molecule:

• Thioredoxin reductase