The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Specific activity : 25.6 U/mg.
One unit will cause the oxidation of 1µmole of NADPH per minute by deltaA412/0.0136 x 2.
Yeast thioredoxin reductase is a flavoprotein with a molecular weight of approx. 35,000 and consist of two subunits, each containing one molecule of FAD and catayzes the NADPH-dependent reduction of thioredoxin.
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Preparation and Storage
Stability and Storage
Shipped at 4°C. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Gene associated with retinoic and IFN-induced mortality 12 protein
Gene associated with retinoic and interferon-induced mortality 12 protein
Gene associated with retinoid IFN induced mortality 12 protein
KM 102 derived reductase like factor
KM-102-derived reductase-like factor
Thioredoxin reductase 1
Thioredoxin reductase 1 cytoplasmic
Thioredoxin reductase GRIM 12
Thioredoxin reductase TR1
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 alpha and beta while isoform 5 enhances the transcriptional activity of the beta receptor only. Isoform 5 also mediates cell death induced by a combination of interferon-beta and retinoic acid.
Isoform 1 is expressed predominantly in Leydig cells (at protein level). Also expressed in ovary, spleen, heart, liver, kidney and pancreas and in a number of cancer cell lines. Isoform 4 is widely expressed with highest levels in kidney, testis, uterus, ovary, prostate, placenta and fetal liver.
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. Contains 1 glutaredoxin domain.
The N-terminal glutaredoxin domain found in isoform 1 does not contain the C-P-Y-C redox-active motif normally found in glutaredoxins and has been found to be inactive in classical glutaredoxin assays.
The N-terminus of isoform 5 is blocked. ISGylated.