Recombinant Proteins
Product List
TXNL4A Human
Thioredoxin-Like 4A Human Recombinant
TXNL4A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
TXNL4B Human
Thioredoxin-Like 4B Human Recombinant
TXNL4B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (1-149 a.a) and having a molecular mass of 21.1kDa.
TXNL4B is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Introduction
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 .
