TXNRD1 Human
Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.
Description
TXNRD1 Human Recombinant produced in E.Coli is a single, non-glycosylated,
polypeptide chain containing 508 amino acids (161-647 a.a.) and having a molecular mass of 55.7 kDa. TXNRD1 protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.
Product Specs
Thioredoxin reductase 1 cytoplasmic, TR, GRIM-12, Gene associated with retinoic and IFN-induced mortality 12 protein, KM-102-derived reductase-like factor, Thioredoxin reductase TR1, TXNRD1, GRIM12, KDRF, TR1, TXNR, TRXR1, MGC9145.
MGSSHHHHHH SSGLVPRGSH MYDYDLIIIG GGSGGLAAAK EAAQYGKKVM VLDFVTPTPL GTRWGLGGTC VNVGCIPKKL MHQAALLGQALQDSRNYGWK VEETVKHDWD RMIEAVQNHI GSLNWGYRVA LREKKVVYEN AYGQFIGPHR IKATNNKGKE KIYSAERFLI ATGERPRYLGIPGDKEYCIS SDDLFSLPYC PGKTLVVGAS YVALECAGFL AGIGLDVTVM VRSILLRGFD QDMANKIGEH MEEHGIKFIR QFVPIKVEQIEAGTPGRLRV VAQSTNSEEI IEGEYNTVML AIGRDACTRK IGLETVGVKI NEKTGKIPVT DEEQTNVPYI YAIGDILEDK VELTPVAIQAGRLLAQRLYA GSTVKCDYEN VPTTVFTPLE YGACGLSEEK AVEKFGEENI EVYHSYFWPL EWTIPSRDNN KCYAKIICNT KDNERVVGFH VLGPNAGEVT QGFAAALKCG LTKKQLDSTI GIHPVCAEVF TTLSVTKRSG ASILQAGC.
Product Science Overview
Thioredoxin Reductase 1 is a homodimeric enzyme, meaning it consists of two identical subunits. Each subunit contains a flavin adenine dinucleotide (FAD) prosthetic group and a selenocysteine residue at the active site. The enzyme catalyzes the reduction of thioredoxin, a small redox protein, using NADPH as an electron donor. The reaction can be summarized as follows:
This reduction process is essential for various cellular processes, including DNA synthesis, repair, and defense against oxidative stress .
Thioredoxin Reductase 1 is involved in several critical biological functions:
- Redox Regulation: It helps maintain the redox balance within cells by reducing oxidized thioredoxin, which in turn reduces other proteins through cysteine thiol-disulfide exchange.
- Antioxidant Defense: By reducing thioredoxin, TXNRD1 indirectly contributes to the detoxification of reactive oxygen species (ROS), protecting cells from oxidative damage.
- Cell Growth and Survival: The enzyme is involved in regulating cell proliferation and apoptosis. It has been shown to influence the activity of various transcription factors and signaling pathways.
- Selenium Metabolism: As a selenoprotein, TXNRD1 plays a role in selenium metabolism, which is vital for the proper function of several other selenoproteins .
Recombinant Human Thioredoxin Reductase 1 is produced using Escherichia coli (E. coli) expression systems. The recombinant protein typically includes an N-terminal His-tag to facilitate purification. The amino acid sequence of the recombinant protein corresponds to the amino acids 161-647 of the native human enzyme .
The recombinant form retains the enzymatic activity of the native protein, making it useful for various research applications, including studies on redox biology, drug development, and understanding the enzyme’s role in disease processes .
Recombinant Thioredoxin Reductase 1 is widely used in biochemical and biomedical research. Some of its applications include:
- Studying Redox Mechanisms: Researchers use the recombinant enzyme to investigate the mechanisms of redox regulation and the role of thioredoxin in cellular processes.
- Drug Screening: The enzyme is used in high-throughput screening assays to identify potential inhibitors or activators that could be developed into therapeutic agents.
- Disease Research: Given its involvement in cancer, cardiovascular diseases, and neurodegenerative disorders, TXNRD1 is a target of interest in understanding the molecular basis of these diseases and developing targeted therapies .
