Literature DB >> 18988024

E. coli and insect cell expression, automated purification and quantitative analysis.

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.

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Year:  2009        PMID: 18988024     DOI: 10.1007/978-1-59745-196-3_10

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  3 in total

1.  Widening the bottleneck: increasing success in protein expression and purification.

Authors:  Ralph Hopkins; Dominic Esposito; William Gillette
Journal:  J Struct Biol       Date:  2010-07-29       Impact factor: 2.867

2.  Streamlined, automated protocols for the production of milligram quantities of untagged recombinant human cyclophilin-A (hCypA) and untagged human proliferating cell nuclear antigen (hPCNA) using AKTAxpress.

Authors:  Cornelia Ludwig; Martin A Wear; Malcolm D Walkinshaw
Journal:  Protein Expr Purif       Date:  2009-12-06       Impact factor: 1.650

3.  A Streamlined, Automated Protocol for the Production of Milligram Quantities of Untagged Recombinant Rat Lactate Dehydrogenase A Using ÄKTAxpressTM.

Authors:  Matthew W Nowicki; Elizabeth A Blackburn; Iain W McNae; Martin A Wear
Journal:  PLoS One       Date:  2015-12-30       Impact factor: 3.240

  3 in total

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