TR1 (human) ELISA Kit (10x96T)
|Synonyms||TR; TXNRD1; GRIM12; GRIM-12; EC=184.108.40.206; Thioredoxin Reductase TR1; KM-102-derived Reductase-like Factor; Thioredoxin Reductase 1; Cytoplasmic; Gene Associated with Retinoic and IFN-induced Mortality 12 Protein|
|Application Set||Compound Screening|
|Range||0.39 ng/ml - 25 ng/ml|
|Other Product Data||
Click here for Original Manufacturer Product Datasheet
|Declaration||Manufactured by AbFrontier|
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||+4°C|
Any unused reconstituted standard should be discarded or frozen at -80℃.
Standard can be frozen and thawed one time only without loss of immunoreactivity.
|Product Specification Sheet|
The mammalian thioredoxin reductases (TrxRs) are a family of selenocysteine-containing pyridine nucleotide-disulfide oxidoreductases. 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). Isoform 1 may possess glutaredoxin activity as well as thioredoxin reductase activity and induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4 enhances the transcriptional activity of estrogen receptors α and β while isoform 5 enhances the transcriptional activity of the β receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-β and retinoic acid.