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Updated: Jun 20, 2026

Laboratory Scale Production and Purification of a Therapeutic Antibody
Published on: January 24, 2017
Purification process development for HER1 extracellular domain as a potential therapeutic vaccine
Dania León1, Yadira Prieto, Eutimio G Fernández
1Process Development Department, Center for Molecular Immunology, 216th Street to 15th, P.O. Box 16040, Havana 11600, Cuba.
Abstract:
HER1 is a tumor associated antigen emerging as an attractive target for cancer therapy. In the present study we demonstrated for first time that HER1 extracellular domain can be purified by a downstream process at pilot scale based on immunoaffinity chromatography from bioreactor supernatant of HEK 293 transfectomes. Filtered supernatant was applied to CNBr-activated Sepharose CL-4B with monoclonal antibody anti-human EGF immobilized, followed by three additional chromatographic polishing steps. HER1 extracellular domain was obtained with high purity (>95%), low DNA content, and biological activity.
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