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100ug, 50ug
ProteoGenix
Recombinant Proteins
Mammalian cells
Elisa, WB
Thioredoxin reductase 1, cytoplasmic (TXNRD1) is a key enzyme involved in maintaining redox balance within mammalian cells. It is a member of the thioredoxin reductase family, which plays an important role in regulating cellular redox signaling pathways. TXNRD1 is a drug target for various diseases, as its dysregulation has been linked to numerous pathological conditions. In this article, we will discuss the structure, activity, and application of TXNRD1 in mammalian cells production.
TXNRD1 is a homodimeric enzyme composed of two identical subunits, each with a molecular weight of approximately 55 kDa. The crystal structure of TXNRD1 has been determined, revealing a unique fold consisting of three domains: the N-terminal domain, the central domain, and the C-terminal domain. The N-terminal domain contains the redox-active site, which consists of a selenocysteine residue and a cysteine residue. The central domain contains the FAD-binding site, while the C-terminal domain is involved in the dimerization of the enzyme.
The main function of TXNRD1 is to maintain the redox state of the cell by reducing oxidized thioredoxin back to its active form. This process is essential for the proper functioning of various redox-sensitive proteins involved in cell growth, differentiation, and apoptosis. TXNRD1 uses NADPH as a co-substrate to reduce thioredoxin, and in turn, NADPH is regenerated by the action of other enzymes such as glucose-6-phosphate dehydrogenase. This cycle of NADPH regeneration is crucial for maintaining the reducing environment of the cell.
TXNRD1 is involved in the production of mammalian cells through its role in regulating redox signaling pathways. The enzyme is essential for cell growth and proliferation, and its dysregulation has been linked to various diseases, including cancer. In cancer cells, TXNRD1 is overexpressed, leading to increased cell proliferation and resistance to chemotherapy. Therefore, targeting TXNRD1 has become a promising strategy for cancer treatment.
In addition to cancer, TXNRD1 has also been implicated in other diseases, such as cardiovascular disorders, neurodegenerative diseases, and inflammatory conditions. In these diseases, the dysregulation of TXNRD1 leads to oxidative stress, which can cause damage to cells and tissues. Hence, TXNRD1 is considered a potential drug target for these conditions.
Several inhibitors have been developed to target TXNRD1, which can potentially be used for the treatment of various diseases. These inhibitors act by binding to the redox-active site of the enzyme, thus blocking its activity. Some of the inhibitors also target the FAD-binding site, which is essential for the catalytic activity of TXNRD1. These inhibitors have shown promising results in preclinical studies, and clinical trials are currently underway to evaluate their efficacy and safety.
In summary, TXNRD1 is a key enzyme involved in maintaining redox balance in mammalian cells. Its dysregulation has been linked to various diseases, making it a potential drug target. The structure and activity of TXNRD1 have been extensively studied, and its role in mammalian cells production has been well established. Inhibitors targeting TXNRD1 have shown promising results and hold great potential for the treatment of various diseases. Further research on TXNRD1 and its inhibitors may lead to the development of novel therapies for a wide range of diseases.
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