Monoclonal antibodies (mAbs) are currently the most important class of therapeutic proteins. Advances in upstream process technologies have led to tremendous improvement of mAb titers in mammalian cell culture. Increases in fermentation volume and the protein mass produced has made the timely processing of harvested material extremely challenging. This is further compounded by the elevated levels of process- and/or product-related impurities resulting from prolonged fermentation and substantially higher cell density in the expression culture. Chromatographic media with high capacity and improved chromatographic and operational performance offer the latest productivity tools to address downstream process challenges. We have employed two next generation ultra high-capacity ion exchangers, Nuvia™ S and Nuvia Q Resins, and Nuvia™ cPrime™ Hydrophobic Cation Exchange Resin, to effectively purify a monoclonal antibody from Chinese hamster ovary (CHO) cell culture harvest. The results demonstrate that this three-step nonaffinity workflow can effectively deliver highly purified monoclonal antibodies with minimal feed conditioning.