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Laboratory Scale Production and Purification of a Therapeutic Antibody
Published on: January 24, 2017
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Homogeneously modified immunoglobulin domains for therapeutic application
Tao Liu1, Juanjuan Du1, Xiaozhou Luo2
1California Institute for Biomedical Research (Calibr), 11119 N. Torrey Pines Road, La Jolla, CA 92037, United States.
Current Opinion in Chemical Biology
|June 29, 2015
Summary
Novel antibody modification technologies have revolutionized therapeutics. Antibody derivatives like antibody-drug conjugates offer enhanced profiles for treating cancer, autoimmune, and infectious diseases.
Area of Science:
- Biotechnology
- Immunology
- Pharmaceutical Sciences
Background:
- Therapeutic antibodies have seen significant advancements due to innovative modification technologies.
- While monoclonal antibodies are successful, antibody derivatives aim for improved therapeutic outcomes.
Purpose of the Study:
- To review recent developments in modifying immunoglobulin domains for therapeutic applications.
- To highlight the potential of engineered antibody derivatives in treating various diseases.
Main Methods:
- Review of genetic and chemical approaches for antibody domain modification.
- Analysis of methodologies producing homogeneous antibody therapeutics with enhanced functionalities.
Main Results:
- Innovative methods allow controllable modifications on immunoglobulin domains.
- Engineered antibody derivatives demonstrate enhanced therapeutic profiles and new functionalities.
Conclusions:
- Antibody-drug conjugates, bispecific antibodies, and antibody/Fc fusion proteins show great promise.
- These advanced therapeutics are valuable for treating cancer, autoimmune diseases, infectious diseases, and other disorders.
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