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Increase mAb purity with salt-tolerant cation exchanger

Introduction

Ion exchange chromatography is often used as an intermediate purification step in monoclonal antibody (mAb) purification for the removal of protein aggregates, host cell proteins (HCP), and leached protein A ligand. Industry trends are focusing on the development of continuous downstream processing. Typically scientists in biopharmaceutical settings use cation exchange (CEX) and anion exchange (AEX) chromatography steps in series to further polish a purified mAb after the protein A capturing step. In this study, we focus on the development of a post protein A CEX step for the removal of aggregates, host cell proteins and leached protein A to improve the purity of the mAb eluate in a single polishing step.

A strong cation exchange resin, TOYOPEARL Sulfate-650F, is used in this study. It is a novel resin with the following benefits: strong capture of mAb aggregates, high salt-tolerance, wide working pH range, and high dynamic binding capacity. The protocol used with this resin has a minimal pH adjustment of the purified mAb eluate after the protein A step.

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