摘要
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.
| 源语言 | 英语 |
|---|---|
| 页(从-至) | 183-188 |
| 页数 | 6 |
| 期刊 | Biotechnology Letters |
| 卷 | 28 |
| 期 | 3 |
| DOI | |
| 出版状态 | 已出版 - 2月 2006 |
| 已对外发布 | 是 |
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