An Efficient Purification Platform for Recombinant Proteins

Mixed-mode chromatography matrices are designed to present multiple interaction modes to resolve target proteins and impurities, entities that are themselves complex multimodal molecules. Under specific purification conditions, one or more such interaction modes may be involved in the binding or repulsion between the target protein and the chromatography media. Therefore, the behavior of a protein during purification by mixed-mode chromatography is often not predictable on the basis of its pI or amino acid sequence. Here, we describe the use of a design of experiment (DOE) approach in the initial screening of chromatographic conditions for the purification of a diverse set of protein targets on Nuvia™ cPrime™ Hydrophobic Cation Exchange Media.