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Temperature-induced expression of human-mouse chimeric Fab

H Zan1, M Yeh

  • 1Shanghai Institute of Cell Biology, Chinese Academy of Sciences, China.

Chinese Journal of Biotechnology
|January 1, 1997
PubMed
Summary

Researchers developed a new E. coli expression system for producing chimeric antibody fragments (Fabs). The system successfully generated functional anti-prostate specific antigen (PSA), anti-lysozyme (HEL), and anti-tetanus toxoid (TT) Fabs, demonstrating specific antigen binding.

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Area of Science:

  • Biotechnology
  • Molecular Biology
  • Immunology

Background:

  • Antibody fragments (Fabs) are crucial for targeted therapies and diagnostics.
  • Efficient production of functional chimeric Fabs in microbial systems remains a challenge.

Purpose of the Study:

  • To construct and validate a novel temperature-induced expression vector (pHZ01) utilizing the lambda PRPL promoter for efficient human-mouse chimeric Fab expression in E. coli.

Main Methods:

  • Construction of the pHZ01 expression vector with the lambda PRPL promoter.
  • Expression of three distinct chimeric Fabs: anti-prostate specific antigen (PSA), anti-lysozyme (HEL), and anti-tetanus toxoid (TT) in E. coli.
  • Assessment of antigen-binding activity of the soluble chimeric Fabs.

Main Results:

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  • Successful construction of the pHZ01 temperature-induced expression vector.
  • Efficient expression of soluble chimeric Fabs targeting PSA, HEL, and TT in E. coli.
  • Demonstrated specific antigen-binding activities for all expressed soluble chimeric Fabs.

Conclusions:

  • The pHZ01 vector system enables efficient production of functional human-mouse chimeric Fabs in E. coli.
  • This system provides a viable platform for generating specific antibody fragments for research and therapeutic applications.