Thioredoxin Mouse Recombinant
TXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (1-105 a.a.) and having a molecular mass of 14.1kDa. TXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Escherichia Coli.
Sterile filtered colorless solution.
Thioredoxin E.Coli Recombinant
Thioredoxin Human Recombinant
Thioredoxin Human Recombinant, His Tag
Thioredoxin Recombinant, His Tag
Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.
Thioredoxin-2 Human Recombinant
Thioredoxin-2 Yeast Recombinant
Thioredoxin-2 Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 12.6kDa.
Thioredoxin Domain Containing 12 Human Recombinant
Thioredoxin Domain Containing 17 Human Recombinant
Thioredoxin-Like 1 Human Recombinant
Thioredoxin is a class of small redox proteins found in nearly all known organisms. These proteins play a crucial role in many biological processes, including redox signaling. In humans, thioredoxins are encoded by the TXN and TXN2 genes . Thioredoxin proteins are characterized by a conserved active site containing two cysteine residues in a CXXC motif, which are essential for their redox activity .
Thioredoxins are ubiquitously expressed in various tissues and are essential for life in mammals . They are involved in maintaining redox homeostasis, cell proliferation, and DNA synthesis . Thioredoxin-1 (Trx-1) is found in the cytoplasm and nucleus, while Thioredoxin-2 (Trx-2) is located in the mitochondria . These proteins are also present in plants, where they regulate functions such as photosynthesis, growth, and development .
The primary function of thioredoxin is the reduction of oxidized cysteine residues and the cleavage of disulfide bonds . Thioredoxins act as electron donors to peroxidases and ribonucleotide reductase . They play a significant role in immune responses and pathogen recognition by modulating the expression of defense-related genes . In plants, thioredoxins contribute to defense responses against pathogens by regulating the expression of pathogenesis-related genes .
Thioredoxins interact with a broad range of proteins through a redox mechanism based on the reversible oxidation of cysteine thiol groups to disulfides . This interaction involves the transfer of two electrons and two protons, resulting in the covalent interconversion of a disulfide and a dithiol . Thioredoxins are maintained in their reduced state by the enzyme thioredoxin reductase, which uses NADPH as a co-substrate . This system is crucial for maintaining cellular redox homeostasis and protecting cells from oxidative damage .
The expression and activity of thioredoxins are regulated by various mechanisms, including transcriptional regulation and post-translational modifications . Thioredoxin expression can be induced by oxidative stress, UV irradiation, and inflammatory cytokines . Post-translational modifications, such as phosphorylation and acetylation, also play a role in modulating thioredoxin activity .
Thioredoxins have significant applications in biomedical research, diagnostic tools, and therapeutic strategies . They are used as biomarkers for oxidative stress and inflammation . In cancer therapy, targeting the thioredoxin system has shown promise in inhibiting tumor growth and enhancing the efficacy of chemotherapeutic agents . Additionally, thioredoxins are being explored as potential therapeutic agents for treating diseases associated with oxidative stress .
Thioredoxins play a vital role throughout the life cycle, from development to aging and disease . During development, they are essential for cell proliferation and differentiation . In aging, thioredoxins help mitigate oxidative damage and maintain cellular function . In diseases such as cancer and chronic obstructive pulmonary disease (COPD), thioredoxins contribute to disease progression by regulating redox homeostasis and inflammation .