Characterization of an Anti-Thioredoxin Monoclonal Antibody

  • Wei Zhang
  • , Wang Zhang
  • , Yanchun Tang
  • , Jing Zhang
  • , Jian Ning Liu*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

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 languageEnglish
Pages (from-to)183-188
Number of pages6
JournalBiotechnology Letters
Volume28
Issue number3
DOIs
StatePublished - Feb 2006
Externally publishedYes

Keywords

  • Affinity chromatography
  • Monoclonal antibody
  • Thioredoxin
  • Western blotting

Fingerprint

Dive into the research topics of 'Characterization of an Anti-Thioredoxin Monoclonal Antibody'. Together they form a unique fingerprint.

Cite this