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.
| Original language | English |
|---|---|
| Pages (from-to) | 183-188 |
| Number of pages | 6 |
| Journal | Biotechnology Letters |
| Volume | 28 |
| Issue number | 3 |
| DOIs | |
| State | Published - Feb 2006 |
| Externally published | Yes |
Keywords
- Affinity chromatography
- Monoclonal antibody
- Thioredoxin
- Western blotting