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Characterization of an Anti-Thioredoxin Monoclonal Antibody

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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 0.40×109 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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Correspondence to Jian-Ning Liu.

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These authors contributed equally to the work.

Received 21 September 2005; Revisions requested 7 October 2005; Revisions received 10 November 2005; Accepted 11 November 2005

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Zhang, W., Zhang, W., Tang, Y. et al. Characterization of an Anti-Thioredoxin Monoclonal Antibody. Biotechnol Lett 28, 183–188 (2006). https://doi.org/10.1007/s10529-005-5333-6

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  • DOI: https://doi.org/10.1007/s10529-005-5333-6

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