Scientists in the field of process chromatography methods development are constantly on the lookout for better and more selective ways to remove aggregates and other process-related impurities from monoclonal antibody monomer. The data presented in the following paper demonstrate the capabilities of CaPure-HA to remove degradation products, dimer, and higher-order aggregates from the monomer of a protein A purified IgG1 monoclonal antibody.
Aggregate removal is a pivotal process step in the purification of monoclonal antibodies (mAbs). The removal of soluble, non-precipitated mAb aggregates is highly challenging due to their close physical and chemical similarity to the drug product itself. Ion exchange chromatography (IEC) has long been used as an effective means of removing process impurities from biological drug products. Cation exchange chromatography (CEX), in particular, has shown to be effective in separating mAb monomer from dimers and higher order aggregates. In this paper, the removal of mAb dimer and higher order aggregates from mAb monomer using TOYOPEARL GigaCap cation exchange resins is demonstrated.
The drive to reduce the manufacturing costs for biological therapeutics have increased the demands placed on downstream unit operations to the point where a single processing step is expected to accomplish a multitude of purification objectives. Where anion exchange resins have traditionally been used to remove DNA, endotoxin, and as a viral clearance step in the purification of monoclonal antibodies (mAbs), new ligand chemistries make it possible for anion exchange chromatography to do more. In the following paper, TOYOPEARL NH2-750F, a salt tolerant anion exchange resin from Tosoh Bioscience, is shown to be able to remove mAb dimer and higher order aggregates from mAb monomer.
This application note compares the amount of leached Protein A ligand that is present in purified monoclonal antibody, post elution, when using TOYOPEARL AF-rProtein A HC-650F, TOYOPEARL AF-rProtein A-650F, and another commercially available high capacity Protein A resin. Protein A ELISA tests specific to each resin evaluated show that the TOYOPEARL AF-rProtein A HC-650F is very stable and exhibits a markedly lower level of ligand leakage compared to the other resins tested.
The following paper compares the host cell protein (HCP) removal capabilities of TOYOPEARL AF-rProtein A HC-650F, TOYOPEARL AF-rProtein A-650F, and another commercially available high-capacity protein A resin.