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Heat and High pH Forced Degradation of Antibodies on a
Biozen dSEC-2 Column
This application note demonstrates the applicability of the Biozen dSEC-2 column in understanding the biophysical integrity monoclonal antibodies and related proteins. Stability studies have been shown to generate impurities that feature a degree of denaturization thus exposing some hydrophobic regions of the folded protein's interior. The hydrophilic nature of the Biozen dSEC-2 stationary phase shows favorable aggregate profiles for forced degradation work under high salt conditions which is a known challenge when working with more hydrophobic hybrid particles for these studies.
Heat and High pH Forced Degradation of Antibodies on a Biozen dSEC-2 Column
This application note demonstrates the applicability of the Biozen dSEC-2 column in understanding the biophysical integrity monoclonal antibodies and related proteins. Stability studies have been shown to generate impurities that feature a degree of denaturization thus exposing some hydrophobic regions of the folded protein's interior. The hydrophilic nature of the Biozen dSEC-2 stationary phase shows favorable aggregate profiles for forced degradation work under high salt conditions which is a known challenge when working with more hydrophobic hybrid particles for these studies.
Document Type:
Technical Notes
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Size Exclusion
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