Purolite, An Ecolab Company, Bio-Expo Live June 2026: Downstream Bioprocessing

Modern monoclonal antibodies, bispecifics, and Fc-fusion proteins often face their biggest purification challenges at the capture step. Traditional protein A chromatography relies on low-pH elution that can destabilize acid-sensitive molecules, trigger aggregation, and increase the impurity load carried into polishing. A more effective strategy begins with affinity resins engineered for high-capacity binding and milder, higher-pH elution. Preventing aggregate formation early can improve product stability while also increasing clearance of host cell proteins, residual nucleic acids, and viral contaminants during capture. Stronger impurity removal at the start of the process reduces pressure on downstream polishing and can open the door to simpler, more economical two-step purification approaches.

Explore the comparative clearance data to see how an elution strategy can improve platform performance.