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Methods Mol Biol. 2019;2025:51-68. doi: 10.1007/978-1-4939-9624-7_3.

Semiautomated Small-Scale Purification Method for High-Throughput Expression Analysis of Recombinant Proteins.

Author information

1
Department of Biomolecular Resources, Genentech, Inc., South San Francisco, CA, USA.
2
Department of Early Stage Cell Culture, Genentech, Inc., South San Francisco, CA, USA.
3
23andMe Inc., South San Francisco, CA, USA.
4
Department of Biomolecular Resources, Genentech, Inc., South San Francisco, CA, USA. krafte1@gene.com.

Abstract

The expression analysis of recombinant proteins is a challenging step in any high-throughput protein production pipeline. Often multiple expression systems and a variety of expression construct designs are considered for the production of a protein of interest. There is a strong need to triage constructs rapidly and systematically. This chapter describes a semiautomated method for the simultaneous purification and characterization of proteins expressed from multiple samples of expression cultures from the E. coli, baculovirus expression vector system, and mammalian transient expression systems. This method assists in the selection of the most promising expression construct(s) or the most favorable expression condition(s) to move forward into large-scale protein production.

KEYWORDS:

BEVS; Baculovirus; E. coli; High-throughput protein expression; Mammalian transient expression; Parallel protein purification; Recombinant protein expression

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