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ABSTRACT: Background
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.Results
Here, we introduce a series of new RK2 based broad
SUBMITTER: Dammeyer T
PROVIDER: S-EPMC3680311 | biostudies-literature | 2013 May
REPOSITORIES: biostudies-literature