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TR1 (human) ELISA Kit (10x96T)
Product Details | |
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Synonyms | TR; TXNRD1; GRIM12; GRIM-12; EC=1.8.1.9; Thioredoxin Reductase TR1; KM-102-derived Reductase-like Factor; Thioredoxin Reductase 1; Cytoplasmic; Gene Associated with Retinoic and IFN-induced Mortality 12 Protein |
Product Type | Kit |
Properties | |
Application Set | Compound Screening |
Crossreactivity | Human |
Quantity |
10x96 wells |
Sensitivity | 0.39 ng/ml |
Range | 0.39 ng/ml - 25 ng/ml |
Sample Type |
Buffers Cell Lysate Plasma Serum |
Assay Type | Sandwich |
Other Product Data |
Click here for Original Manufacturer Product Datasheet |
Declaration | Manufactured by AbFrontier |
Shipping and Handling | |
Shipping | BLUE ICE |
Short Term Storage | +4°C |
Long Term Storage | +4°C |
Handling Advice |
Any unused reconstituted standard should be discarded or frozen at -80℃. Standard can be frozen and thawed one time only without loss of immunoreactivity. |
Documents | |
Manual |
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MSDS | Inquire |
Product Specification Sheet | |
Datasheet |
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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.