Thioredoxin Reductase 2 SelCys523Cys (human) (rec.)
|Synonyms||SelZ; TXNRD2; TR-β; KIAA1652; EC=220.127.116.11; Selenoprotein Z; Thioredoxin Reductase TR3; Thioredoxin Reductase 2, Mitochondrial|
Enzymatic Activity has not been tested.
|Formulation||Liquid in 20mM HEPES, pH 7.4, 10% Glycerol.|
|Other Product Data||
Click here for Original Manufacturer Product Datasheet
|Declaration||Manufactured by AbFrontier|
|Shipping and Handling|
|Short Term Storage||-20°C|
|Long Term Storage||-80°C|
|Handling Advice||Avoid freeze/thaw cycles.|
|Product Specification Sheet|
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).
1) Mustacich, D. and Powis,G. (2000) Biochem J. 15. 346 Pt 1:1-8. (General)