Purification Workflow For The Production of Highly Pure Recombinant Proteins

By Louisa Vang and Xuemei He

A three-column workflow has been developed for the purification of a histidine-tagged recombinant protein from E. coli extract. The macroporous Ni2+-charged Nuvia IMAC Resin provides efficient capture of the target protein molecules with excellent selectivity, binding capacity, and recovery. The subsequent mixed-mode chromatography steps, performed with Nuvia™ cPrime™ Resin followed by CHT™ Ceramic Hydroxyapatite Media, eliminate leached Ni2+ ions and offer further clearance of residual impurities from host cells.