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Purification process development for HER1 extracellular domain as a potential therapeutic vaccine

2009; Elsevier BV; Volume: 877; Issue: 27 Linguagem: Inglês

10.1016/j.jchromb.2009.07.041

1873-376X

Dania León, Yadira Prieto, Eutímio Gustavo Fernández Núñez, N. Viveros Perez, José Montero, Julio Palacios, Dubhe Bulté, Kathya r. De La Luz, Vladimir Peña, Williams Ferro, Belinda Sánchez Pérez, Rodolfo Valdés, Adolfo Castillo,

vaccines and immunoinformatics approaches

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.