Capto ™ Q ImpRes is a BioProcess chromatography medium developed for large-scale purification of biopharmaceutical Proteins. The ability to run at higher flow rates and higher bed heights also increases flexibility in process design. By combining the high-fLow characteristics of Capto ™ media with a small particle size, Capto ™ Q ImpRes delivers excellent pressure-fLow properties with impressive resolution.
This chromatography media is part of an expanded high-resolution platform based on the high-fLow Agarose Capto ™ product line. Ĭapto ™ Q ImpRes is a strong anion exchanger for the high-throughput intermediate purification and polishing steps of a wide range of biomolecules. To view the Certificate of Analysis for this product, please visit. For more information on the batch specific expiration date, please contact technical service. Please be aware this product may be shipped 90 days before the expiration date. This work identifies salt-induced RSA as the cause of peak splitting of a mAb in CEX and also provides solutions to reduce the phenomenon.>55 mg binding capacity(> 55 mg BSA, > 48 mg ß-lactoglobulin) This is because higher pH conditions also increase RSA. However, experiments that were intended to reduce salt concentration by increasing the elution buffer pH did not significantly mitigate peak splitting. The addition of a positively charged amino acid (such as 50 mM histidine) into the CEX elution buffer resulted in elution at lower NaCl concentrations and also effectively reduced peak splitting.
Different salts were tested, showing that chaotropic salts such as CaCl 2 reduced the second elution peak by inducing less RSA. The finding of NaCl-induced RSA suggested that lower NaCl elution concentrations and different types of salts could mitigate RSA and thus eliminate peak splitting. It was determined that high NaCl concentrations in combination with high protein concentrations induced mAb X to form one RSA species that binds more strongly to the column, resulting in a large second elution peak. Multiple factors including resin type, load challenge, residence time and gradient slope were evaluated and demonstrated little effect on the peak splitting of mAb X. We report a case study in which the RSA of an IgG2 (mAb X) resulted in significant peak splitting during salt gradient elution in CEX. This work investigates the effects of RSA on a bind-and-elute mode cation exchange chromatography (CEX) unit operation. There are multiple studies that investigate the effect of RSA on product characteristics such as viscosity, opalescence, phase separation and aggregation. Some monoclonal antibodies (mAbs) are reported to display concentration-dependent reversible self-association (RSA).
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