Source:http://linkedlifedata.com/resource/pubmed/id/18988024
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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2008-11-6
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1064-3745
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
498
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
143-56
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pubmed:meshHeading |
pubmed-meshheading:18988024-Animals,
pubmed-meshheading:18988024-Baculoviridae,
pubmed-meshheading:18988024-Cells,
pubmed-meshheading:18988024-Escherichia coli,
pubmed-meshheading:18988024-Insects,
pubmed-meshheading:18988024-Microchip Analytical Procedures,
pubmed-meshheading:18988024-Polymerase Chain Reaction,
pubmed-meshheading:18988024-Recombinant Proteins
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pubmed:year |
2009
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pubmed:articleTitle |
E. coli and insect cell expression, automated purification and quantitative analysis.
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pubmed:affiliation |
Gene Expression, Vertex Pharmaceuticals, Cambridge, MA, USA.
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pubmed:publicationType |
Journal Article
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