Recombinant Human TXNRD1 protein is a Human Full Length protein, in the 2 to 499 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, FuncS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes 1. May be used as auto-antibodies detection reagent, which will react with sera of some auto-immuno-diseases and cancer patients. 2. May be used for in vitro human TXNRD1 mediated oxidative stress regulation study. 3. May be used for TXNRD1 protein-protein interaction assay. 4. May be used as specific substrate protein for kinase, and ubiquitin (Sumo pathway) related enzyme functional screening assays. 5. As antigen for specific antibody production. |
Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437). Isoform 1. Induces actin and tubulin polymerization, leading to formation of cell membrane protrusions. Isoform 4. Enhances the transcriptional activity of estrogen receptors ESR1 and ESR2. Isoform 5. Enhances the transcriptional activity of the estrogen receptor ESR2 only (PubMed:15199063). Mediates cell death induced by a combination of interferon-beta and retinoic acid (PubMed:9774665).
GRIM12, KDRF, TXNRD1, TR, Gene associated with retinoic and interferon-induced mortality 12 protein, KM-102-derived reductase-like factor, Peroxidase TXNRD1, Thioredoxin reductase TR1, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein
Recombinant Human TXNRD1 protein is a Human Full Length protein, in the 2 to 499 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 0.32% Tris HCl
refolded and chromatographically purified.
Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form (PubMed:8577704). Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis (Probable). Also has reductase activity on hydrogen peroxide (H2O2) (PubMed:10849437).
Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
Isoform 5
Thioredoxin reductase 1 (TXNRD1) also known as TRXR1 is a selenoprotein that plays an important role in maintaining cellular redox balance by catalyzing the reduction of thioredoxin (TRX). It possesses a molecular mass of approximately 55 kDa. TXNRD1 can be found in many tissues displaying a stronger presence in the liver kidney and pancreas indicating its significance in these organs. The enzyme contains a selenocysteine residue at its active site which is essential for its enzymatic activity.
TXNRD1 functions as an integral part of the thioredoxin system which includes thioredoxin and NADPH. It maintains the redox homeostasis in cells by regenerating oxidized thioredoxin. This action allows thioredoxin to in turn reduce disulfide bonds in various substrate proteins. Furthermore TXNRD1 participates in regulating cellular processes such as DNA synthesis and repair signal transduction and antioxidant defense. It does not work alone but collaborates with various redox-active components to achieve its roles.
TXNRD1 participates in the antioxidant defense and redox signaling pathways. Within the antioxidant defense pathway TXNRD1 along with thioredoxin provides resistance to oxidative stress. In the redox signaling pathway the protein interacts with NF-κB signaling processes impacting cell inflammation and apoptosis. These pathways are vital for cellular health and are connected through thioredoxin emphasizing the interconnected nature of TXNRD1-related processes.
TXNRD1 has associations with cancer and neurodegenerative diseases. Elevated levels of TXNRD1 have been observed in various cancers including lung and hepatocellular carcinoma suggesting a role in tumor growth and survival through redox regulation. Additionally TXNRD1 is linked to neurodegenerative diseases such as Alzheimer's where oxidative stress plays a contributory role. In these conditions TXNRD1 interacts closely with other redox proteins like glutathione reductase highlighting its potential as a therapeutic target.
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