Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/100578
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dc.titleEngineering a novel secretion signal for cross-host recombinant protein expression
dc.contributor.authorTan, N.S.
dc.contributor.authorHo, B.
dc.contributor.authorDing, J.L.
dc.date.accessioned2014-10-27T08:27:24Z
dc.date.available2014-10-27T08:27:24Z
dc.date.issued2002
dc.identifier.citationTan, N.S.,Ho, B.,Ding, J.L. (2002). Engineering a novel secretion signal for cross-host recombinant protein expression. Protein Engineering 15 (4) : 337-345. ScholarBank@NUS Repository.
dc.identifier.issn02692139
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100578
dc.description.abstractProtein secretion is conferred by a hydrophobic secretion signal usually located at the N-terminal of the polypeptide. We report here, the identification of a novel secretion signal (SS) that is capable of directing the secretion of recombinant proteins from both prokaryotes and eukaryotes. Secretion of fusion reporter proteins was demonstrated in Escherichia coli, Saccharomyces cerevisiae and six different eukaryotic cells. Estrogen-inducibility and secretion of fusion reporter protein was demonstrated in six common eukaryotic cell lines. The rate of protein secretion is rapid and its expression profile closely reflects its intracellular concentration of mRNA. In bacteria and yeast, protein secretion directed by SS is dependent on the growth culture condition and rate of induction. This secretion signal allows a flexible strategy for the production and secretion of recombinant proteins in numerous hosts, and to conveniently and rapidly study protein expression.
dc.sourceScopus
dc.subjectBroad hosts
dc.subjectProtein expression
dc.subjectSecretion signal
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.sourcetitleProtein Engineering
dc.description.volume15
dc.description.issue4
dc.description.page337-345
dc.description.codenPRENE
dc.identifier.isiutNOT_IN_WOS
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