by José Arnau, PhD and John Pedersen
Volume 5, Issue 3 (Fall 2006)
Current expression technologies have enabled the production of thousands of recombinant proteins in diverse production hosts. Therapeutic recombinant proteins have been engineered for a variety of purposes including reduced antigenicity, longer half-life, simplified process development, and increased affinity. Protein engineering has relied on various high throughput methods (e.g., directed evolution, phage display) to identify candidate proteins with the desired therapeutic properties. The physiological and biochemical diversity of native and engineered proteins reflects on the abundance of production hosts, expression tools, and different approaches for protein purification. Notably, a key step in high-throughput protein production is purification, which is a bottleneck where large numbers of samples are involved. Universal purification methods that can be applied to virtually any protein, and that are amenable to automation, can be used to address this problem…
Citation:
Arnau J, Pedersen J. A Universal Platform for the Purification of Therapeutic Proteins Using Affinity Tags: The Use of Engineered Aminopeptidases for His-Tag Removal. BioProcess J, 2006; 5(3): 59-65. https://doi.org/10.12665/J53.Arnau