The state of protein-derived self-associated, aggregated, and fragmented impurities in therapeutics are critical quality attributes (CQAs) and are widely monitored using non-denaturing size-exclusion chromatography (SEC).
A surge in the development and commercialization of monoclonal antibody (mAb)-based ther-apeutics has driven the requirement for accurate and reproducible analytical methods for pro-tein characterization. Monoclonal antibodies are popular biologic drug candidates, but are sus-ceptible to a myriad of modifications during manufacture and complex degradation pathways during purification and storage, often leading to distinct charge variants that require character-ization and quantification. Ion‑exchange liquid chromatography (IEX) is a well-accepted and widely used technique to separate various mAb charge variant species for the sake of charac-terization and profiling. With the most recent advances in analytical technologies, IEX can be used to help ensure the selection of stable and efficacious mAb drug candidates, from discov-ery through manufacturing.