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Thioredoxin is a small, 12-kDa oxidoreductase protein that functions as a specific reductant for major allergenic proteins and plays an essential role in cellular redox regulation and antioxidant defense. Encoded by the TXN and TXN2 genes, it contains a dithiol-disulfide active site (CXXC motif) that enables it to reduce disulfide bonds in target proteins, thereby neutralizing food allergens and participating in redox signaling pathways. Thioredoxin is involved in numerous physiological processes including reduction of nucleotides to deoxyribonucleotides, detoxification from xenobiotics, oxidants, radicals, and regulation of transcription factors. It is also implicated in cancer biology; many tumor cells express high levels of thioredoxin which can contribute to drug resistance. Inhibition of the thioredoxin system has been explored as a therapeutic strategy for cancer[1][2][3][8].
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