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Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC
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SYSNO ASEP 0313119 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Single-step affinity purification of recombinant proteins using a self-excising module from Neisseria meningitidis FrpC Title Jednokroková afinitní purifikace rekombinantních proteinů založená na samoštěpícím modulu proteinu FrpC bakterie Neisseria meningitidis Author(s) Sadílková, Lenka (MBU-M)
Osička, Radim (MBU-M) RID, ORCID
Šulc, Miroslav (MBU-M) RID, ORCID
Linhartová, Irena (MBU-M) RID, ORCID
Novák, Petr (MBU-M) RID, ORCID
Šebo, Peter (MBU-M) RID, ORCIDSource Title Protein Science. - : Wiley - ISSN 0961-8368
Roč. 17, č. 10 (2008), s. 1834-1843Number of pages 10 s. Language eng - English Country US - United States Keywords asp-pro bond ; frpc ; purification Subject RIV EE - Microbiology, Virology R&D Projects KAN200520702 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR) GA310/06/0720 GA ČR - Czech Science Foundation (CSF) CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000259401900021 DOI 10.1110/ps.035733.108 Annotation We developed a self-excising tag allowing single-step affinity chromatography purification of untagged recombinant proteins. It consists of a 250 residue-long self-processing module of Neisseria meningitidis FrpC protein with a C-terminal affinity tag. N-terminus of the module is fused to the C-terminus of a target protein of interest. Upon binding of the fusion protein to an affinity matrix from cell lysate and washing out of contaminating proteins, site-specific cleavage of the Asp-Pro bond linking the target protein to the self-excising tag is induced by calcium ions. This results in release of the target protein with only a single aspartic acid residue added at the C-terminus, while the self-excising affinity tag remains trapped on the affinity matrix Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2009
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