Literature DB >> 20978975

Tag removal by site-specific cleavage of recombinant fusion proteins.

Adam Charlton1, Michael Zachariou.   

Abstract

Where an affinity tag has served its purpose it may become desirable to remove it from the protein of interest. This chapter describes the removal of such fusion partners from the intended protein product by cleavage with site-specific endoproteases. Methods to achieve proteolytic cleavage of the fusion proteins are provided, along with techniques for optimising the yield of authentic product.

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Year:  2011        PMID: 20978975     DOI: 10.1007/978-1-60761-913-0_19

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


  3 in total

1.  Self-cleaved expression of recombinant lysostaphin from its cellulose binding domain fusion.

Authors:  Kuan-Jung Chen; Cheng-Kang Lee
Journal:  Appl Microbiol Biotechnol       Date:  2022-07-06       Impact factor: 5.560

Review 2.  Stramenopile microalgae as "green biofactories" for recombinant protein production.

Authors:  Imke de Grahl; Sigrun Reumann
Journal:  World J Microbiol Biotechnol       Date:  2021-08-28       Impact factor: 3.312

Review 3.  Several affinity tags commonly used in chromatographic purification.

Authors:  Xinyu Zhao; Guoshun Li; Shufang Liang
Journal:  J Anal Methods Chem       Date:  2013-12-26       Impact factor: 2.193

  3 in total

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