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Updated: Jan 22, 2026

Optimization and Utilization of Agrobacterium-mediated Transient Protein Production in Nicotiana
Published on: April 19, 2014
A High-Throughput System for Transient and Stable Protein Production in Mammalian Cells
Sarah M Rue1, Paul W Anderson2,3, Michelle R Gaylord2
1Genomics Institute of the Novartis Research Foundation, San Diego, CA, USA. srue@gnf.org.
Abstract:
Recombinant protein expression and purification is an essential component of biomedical research and drug discovery. Advances in automation and laboratory robotics have enabled the development of highly parallel and rapid processes for cell culture and protein expression, purification, and analysis. Human embryonic kidney (HEK) cells and Chinese hamster ovary (CHO) cells have emerged as the standard host cell workhorses for producing recombinant secreted mammalian proteins by using both transient and stable production strategies. In this chapter we describe a fully automated custom platform, Protein Expression and Purification Platform (PEPP), used for transient protein production from HEK cells and stable protein production from CHO cells. Central to PEPP operation is a suite of custom robotic and instrumentation platforms designed and built at GNF, custom cell culture ware, and custom scheduling software referred to as Runtime. The PEPP platform enables cost-effective, facile, consistent production of proteins at quantities and quality useful for early stage drug discovery tasks such as screening, bioassays, protein engineering, and analytics.
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