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Updated: Aug 11, 2026

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Characterization of an anti-thioredoxin monoclonal antibody
Wei Zhang1, Wang Zhang, Yanchun Tang
1Institute of Molecular Medicine, Nanjing University, Nanjing, 210093, China.
Abstract:
An anti-E. coli thioredoxin monoclonal antibody, IMM-3C6, which showed high specificity to thioredoxin as assessed by indirect ELISA, was generated using hybridoma technology. The affinity constant of IMM-3C6 to thioredoxin was 0.40 x 10(9) M: (-1) and its sensitivity to thioredoxin fusion protein in dot blotting was 50 ng. In sandwich ELISA, it detected thioredoxin fusion protein between 16 and 150 ng/ml. By using IMM-3C6 as the ligand, thioredoxin fusion protein was successfully purified by affinity chromatography. IMM-3C6 was confirmed to be a useful tool for immunoassay and purification of thioredoxin fusion proteins.
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