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Impressive Separation of a Fusion Protein

publication date: Sep 10, 2014
 | 
author/source: Thermo Fisher Scientific

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Thermo Fisher Scientific has developed a high-resolution hydrophobic interaction chromatography (HIC) method that can separate a fusion protein from a truncated version and a structural isomer.

Application Brief 171: High-Resolution Separation of a Fusion Protein demonstrates that two different HIC columns—the Thermo Scientific ProPac HIC-10 column and the new MAbPac HIC-10 column—can each perform this challenging separation. While the ProPac HIC-10 column is an established column for the analysis of monoclonal antibody post-translational modifications, the MAbPac HIC-10 column exhibits the best performance. The separation was also modified to facilitate fraction collection for further sample characterization.

Fusion proteins are created through the genetic engineering of two or more genes that originated from separate proteins and impart properties from each of the parent proteins. Drugs based on fusion proteins have proven successful in clinical treatments. These protein therapeutics require high-resolution methods for characterization and quality control techniques that are significantly different and more challenging than those used for small-molecule drugs. HIC can resolve proteins based on protein surface hydrophobicity, providing unique separation power complementary to other available techniques.


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