The human recombinant form of TXNRD1, specifically the 161-649 amino acid (a.a.) segment, is produced in Escherichia coli and is fused with a 21 amino acid His tag at the N-terminus . This recombinant protein is a single, non-glycosylated polypeptide chain containing 510 amino acids and has a molecular mass of approximately 55.9 kDa . The protein is purified using proprietary chromatographic techniques to ensure high purity and functionality .
TXNRD1 plays a pivotal role in reducing thioredoxins and other substrates, which is essential for various cellular processes, including DNA synthesis, repair, and defense against oxidative stress . The enzyme catalyzes the reduction of thioredoxin by transferring electrons from NADPH to the active site disulfide of thioredoxin, thereby maintaining it in a reduced state .
The thioredoxin system, including TXNRD1, is vital for cellular redox homeostasis and protection against oxidative damage. It is involved in numerous physiological processes such as cell growth, apoptosis, and immune response . Dysregulation of TXNRD1 activity has been implicated in various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases .
Due to its critical role in cellular redox regulation, TXNRD1 is a target for therapeutic interventions. Inhibitors of TXNRD1 are being explored as potential treatments for cancer, AIDS, and other autoimmune diseases . Additionally, recombinant TXNRD1 is used in laboratory research to study its function and to develop new therapeutic strategies .
The recombinant TXNRD1 protein is typically stored at 4°C for short-term use and at -20°C for long-term storage. It is recommended to add a carrier protein, such as 0.1% HSA or BSA, to prevent degradation during storage . The protein should be handled carefully to avoid multiple freeze-thaw cycles, which can affect its stability and activity .