Protein A affinity chromatography most often serves as the initial capture step in the downstream production of mAb biotherapeutics, and is often the most expensive component of this process. TOYOPEARL AF-rProtein A HC-650F affinity resin utilizes a recombinant, alkaline stable protein A ligand with increased dynamic binding capacity and excellent pressure-flow characteristics. A variety of column dimensions are used by scientists when scaling up protein purification procedures to optimize speed, yield, and recovery, which, in turn, causes the process to be as efficient and cost effective as possible. Here, we show that altering column dimensions to favor a shorter, wider column will maintain equal binding capacities when compared with a longer, narrower column of the same total volume, either when used at a constant, predetermined residence time or a constant linear velocity. This will allow for both ease of scale up and improved flow characteristics when transitioning from a research laboratory process to a full scale production process of biotherapeutics.

Comparison of binding capacity of TOYOPEARL AF-rProtein A HC-650F affinity resin at varying bed heights

249th National Meeting (2015)

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