Author/Authors :
Leَn، نويسنده , , Dania and Prieto، نويسنده , , Yadira and Fernلndez، نويسنده , , Eutimio G. and Pérez، نويسنده , , Noemي and Montero، نويسنده , , José A. and Palacios، نويسنده , , Julio and Bulté، نويسنده , , Dubhe and de la Luz، نويسنده , , Kathya R. and Peٌa، نويسنده , , Vladimir and Ferro، نويسنده , , Williams and Sلnchez، نويسنده , , Belinda and Valdés، نويسنده , , Rodolfo and Castillo، نويسنده , , Adol، نويسنده ,
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.
Keywords :
HER1 ECD , Protein Purification , monoclonal antibody , Immunoaffinity chromatography , HEK 293
