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- W1981567781 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." @default.
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- W1981567781 date "2009-10-01" @default.
- W1981567781 modified "2023-09-27" @default.
- W1981567781 title "Purification process development for HER1 extracellular domain as a potential therapeutic vaccine" @default.
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- W1981567781 doi "https://doi.org/10.1016/j.jchromb.2009.07.041" @default.
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