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Updated: Aug 5, 2026
09:54
Laboratory Scale Production and Purification of a Therapeutic Antibody
Published on: January 24, 2017
Engineering recombinant antibodies for immunotherapy
1Cambridge Centre for Protein Engineering, MRC Centre, United Kingdom.
Cell Biophysics
|August 1, 1995
Summary
High-affinity recombinant antibody fragments are generated using phage display and antibody libraries. Effective transformation into immunotherapeutic agents requires specific engineering, purification, and functionalization strategies for clinical use.
Area of Science:
- Biotechnology
- Immunology
- Molecular Biology
Background:
- Recombinant antibody fragments offer high-affinity antigen binding.
- Current methods yield fragments needing further processing for clinical use.
Purpose of the Study:
- To outline procedures for transforming recombinant antibodies into immunotherapeutic agents.
- To discuss key features for effective antibody functionalization.
Main Methods:
- Phage display methodologies for antibody library construction.
- Engineering techniques to enhance antibody binding affinity.
- Purification and functionalization strategies for recombinant antibodies.
Main Results:
- Successful generation of high-affinity antibody fragments.
- Identification of critical steps for therapeutic antibody development.
Conclusions:
- Recombinant antibody fragments can be effectively developed into immunotherapeutics.
- Specific engineering, purification, and functionalization are crucial for clinical application.
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