Broad host range vectors for expression of proteins with (Twin-) Strep-tag, His-tag and engineered, export optimized yellow fluorescent protein.
dc.contributor.author | Dammeyer, Thorben | |
dc.contributor.author | Timmis, Kenneth N | |
dc.contributor.author | Tinnefeld, Philip | |
dc.date.accessioned | 2013-10-22T09:32:58Z | |
dc.date.available | 2013-10-22T09:32:58Z | |
dc.date.issued | 2013 | |
dc.identifier.citation | Broad 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.issn | 1475-2859 | |
dc.identifier.pmid | 23687945 | |
dc.identifier.doi | 10.1186/1475-2859-12-49 | |
dc.identifier.uri | http://hdl.handle.net/10033/303768 | |
dc.description.abstract | In 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.iso | en | en |
dc.rights | Archived with thanks to Microbial cell factories | en |
dc.title | Broad host range vectors for expression of proteins with (Twin-) Strep-tag, His-tag and engineered, export optimized yellow fluorescent protein. | en |
dc.type | Article | en |
dc.contributor.department | Institut für Physikalische und Theoretische Chemie, NanoBioSciences, Technische Universität Braunschweig, Hans Sommer Str, 10, Braunschweig 38106, Germany. T.Dammeyer@tu-braunschweig.de | en |
dc.identifier.journal | Microbial cell factories | en |
refterms.dateFOA | 2018-06-13T03:42:05Z | |
html.description.abstract | In 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. |