Product Name :
Thioredoxin Reductase 1, SelCys498Cys, Human
Product Type :
Protein
Lot No :
TDE 06
Storage :
Shipped at 4°C. Store at -20°C. After reconstitution, store at -80°C and avoid frequent freeze and thaw.
Composition :
Lyophilized from 20mM HEPES, pH 7.0, 1mM EDTA
Source :
Purified from E.coli expressing the human Thioredoxin Reductase 1 gene (1-498aa, with additional 3 amino acids-GSH at N-term)
Molecular Weight :
55 kDa
Endotoxin activity :
Not tested
Form :
Lyophilized
Purity :
> 95% by SDS-PAGE
Expression system :
E.coli
Tag :
None
Origin :
Human
Background :
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).
Background reference :
1) Mustacich, D. and Powis,G. (2000) Biochem J. 15. 346 Pt 1:1-8.
Research area :
ROS Signaling 
Database link - SwissProt no.
P10599

The test was performed by customers with their own sample.