Literature DB >> 20810632

Solubilization of Escherichia coli recombinant proteins from inclusion bodies.

Richard J Simpson.   

Abstract

The high levels of expression produced by molecular cloning techniques make bacteria particularly useful for producing recombinant proteins. However, these proteins often are difficult to purify, owing to their tendency to aggregate and precipitate within the bacteria as insoluble inclusion bodies. Formation of inclusion bodies is especially common for nonbacterial proteins. Although no single method can be applied to every protein, a number of strategies are available to solubilize inclusion body proteins. This protocol describes one such method.

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Year:  2010        PMID: 20810632     DOI: 10.1101/pdb.prot5485

Source DB:  PubMed          Journal:  Cold Spring Harb Protoc        ISSN: 1559-6095


  1 in total

1.  High-Throughput Screening of Heterologous Functional Amyloids Using Escherichia coli.

Authors:  Elizabeth A Yates; Luis A Estrella; Christopher R So
Journal:  Methods Mol Biol       Date:  2022
  1 in total

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