TXNRD1
TXNRD1 (thioredoxin reductase 1, also known as TXNR, GRIM-12, Trxr1 and TXNR1) is a selenocysteine-containing flavoenzyme of the thioredoxin system. It reduces thioredoxins and other substrates and plays a key role in redox homoeostasis. Browse Assay Genie's current range of TXNRD1 research reagents below, or read on for the biology behind the target.
TXNRD1 is a member of the thioredoxin (Trx) system and belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. Thioredoxin reductases are selenocysteine-containing flavoenzymes that reduce thioredoxins, as well as other substrates, and play a key role in redox homoeostasis. TXNRD1 functions as a homodimer containing FAD, with selenocysteine (Sec) at the active site. UniProt also annotates roles beyond redox control: the protein enhances the transcriptional activity of the oestrogen receptor ESR2 only, and it mediates cell death induced by a combination of interferon-beta and retinoic acid.
The TXNRD1 gene encodes the ubiquitously expressed, cytosolic form of thioredoxin reductase; the protein is found in the cytoplasm and the nucleus. Three thioredoxin reductase isozymes are found in mammals, and TXNRD2 is a related family member. Sec is encoded by a UGA codon that normally signals translation termination. The 3' UTRs of selenoprotein mRNAs contain a conserved stem-loop structure, the Sec insertion sequence (SECIS) element, which is necessary for recognition of UGA as a Sec codon rather than a stop signal. This makes TXNRD1 a useful example in selenoprotein biology.
Alternative splicing, primarily at the 5' end, produces transcript variants that encode the same or different isoforms, including a glutaredoxin-containing isoform predominantly expressed in testis. HGNC places TXNRD1 in the selenoprotein, glutaredoxin domain containing, flavoprotein and thioredoxin reductase family gene groups. The alias GRIM-12 reflects its link to interferon-beta and retinoic acid induced cell death. Mouse and rat both carry a Txnrd1 ortholog.
As a core component of the thioredoxin system, TXNRD1 reduces thioredoxins and other substrates and is central to redox homoeostasis.
TXNRD1 relies on selenocysteine at its active site, encoded by UGA and recognised through the SECIS element in the mRNA 3' UTR.
TXNRD1 (GRIM-12) mediates cell death induced by a combination of interferon-beta and retinoic acid.
TXNRD1 enhances the transcriptional activity of the oestrogen receptor ESR2 only, linking a redox enzyme to hormone receptor function.
TXNRD1 is a selenocysteine-containing FAD flavoenzyme that reduces thioredoxins and other substrates, contributing to redox homoeostasis. UniProt also records that it enhances ESR2 transcriptional activity and mediates cell death induced by interferon-beta combined with retinoic acid.
TXNRD1 is also called TXNR, GRIM-12, Trxr1 and TXNR1, and the protein is named thioredoxin reductase 1, cytoplasmic. Alternative splicing, mainly at the 5' end, yields variants encoding the same or different isoforms, including a glutaredoxin-containing isoform predominantly expressed in testis.
Mouse and rat both have a Txnrd1 ortholog, so rodent models are available for study; check the datasheet of any product for its validated reactivity. Mammals have three thioredoxin reductase isozymes, and TXNRD1 is the ubiquitously expressed cytosolic form, distinct from the mitochondrial TXNRD2.
Other thioredoxin reductase family members and redox-related targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q16881; product specifications from Assay Genie datasheets.