| Literature DB >> 18988024 |
Stephen P Chambers1, John R Fulghum, Douglas A Austen, Fan Lu, Susanne E Swalley.
Abstract
The production of recombinant proteins usually involves the exploration of a wide variety of expression and purification methodologies in the pursuit of a strategy tailored to a particular protein. The methods applied are reliant on exploiting individual differences between expression systems or the variations in specific protein properties. These bespoke strategies have not lent themselves to high-throughput methodologies. Ultimately the development of robust generic methods capable of simplifying and stabilizing the process, allowing automation, was necessary to increase throughput. This chapter describes a series of high-throughput methods used to express, purify, and quantify recombinant protein produced in E. coli or insect cells.Entities:
Mesh:
Substances:
Year: 2009 PMID: 18988024 DOI: 10.1007/978-1-59745-196-3_10
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745