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dc.contributor.authorDammeyer, Thorben
dc.contributor.authorTimmis, Kenneth N
dc.contributor.authorTinnefeld, Philip
dc.date.accessioned2013-10-22T09:32:58Z
dc.date.available2013-10-22T09:32:58Z
dc.date.issued2013
dc.identifier.citationBroad host range vectors for expression of proteins with (Twin-) Strep-tag, His-tag and engineered, export optimized yellow fluorescent protein. 2013, 12:49 Microb. Cell Fact.en
dc.identifier.issn1475-2859
dc.identifier.pmid23687945
dc.identifier.doi10.1186/1475-2859-12-49
dc.identifier.urihttp://hdl.handle.net/10033/303768
dc.description.abstractIn current protein research, a limitation still is the production of active recombinant proteins or native protein associations to assess their function. Especially the localization and analysis of protein-complexes or the identification of modifications and small molecule interaction partners by co-purification experiments requires a controllable expression of affinity- and/or fluorescence tagged variants of a protein of interest in its native cellular background. Advantages of periplasmic and/or homologous expressions can frequently not be realized due to a lack of suitable tools. Instead, experiments are often limited to the heterologous production in one of the few well established expression strains.
dc.language.isoenen
dc.rightsArchived with thanks to Microbial cell factoriesen
dc.titleBroad host range vectors for expression of proteins with (Twin-) Strep-tag, His-tag and engineered, export optimized yellow fluorescent protein.en
dc.typeArticleen
dc.contributor.departmentInstitut für Physikalische und Theoretische Chemie, NanoBioSciences, Technische Universität Braunschweig, Hans Sommer Str, 10, Braunschweig 38106, Germany. T.Dammeyer@tu-braunschweig.deen
dc.identifier.journalMicrobial cell factoriesen
refterms.dateFOA2018-06-13T03:42:05Z
html.description.abstractIn current protein research, a limitation still is the production of active recombinant proteins or native protein associations to assess their function. Especially the localization and analysis of protein-complexes or the identification of modifications and small molecule interaction partners by co-purification experiments requires a controllable expression of affinity- and/or fluorescence tagged variants of a protein of interest in its native cellular background. Advantages of periplasmic and/or homologous expressions can frequently not be realized due to a lack of suitable tools. Instead, experiments are often limited to the heterologous production in one of the few well established expression strains.


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