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- W2340985547 endingPage "175" @default.
- W2340985547 startingPage "151" @default.
- W2340985547 abstract "Protein fusion technology has enormously facilitated the efficient production and purification of individual recombinant proteins. The use of genetically engineered affinity and solubility-enhancing polypeptide tags has increased greatly in recent years and there now exists a considerable repertoire of these that can be used to solve issues related to the expression, stability, solubility, folding, and purification of their fusion partner. In the case of large-scale proteomic studies, the development of purification procedures tailored to individual proteins is not practicable, and affinity tags have therefore become indispensable tools for structural and functional proteomic initiatives that involve the expression of many proteins in parallel. Here, the rationale and applications of a range of established and more recently developed solubility-enhancing and affinity tags are outlined." @default.
- W2340985547 created "2016-06-24" @default.
- W2340985547 creator A5048539803 @default.
- W2340985547 creator A5091712318 @default.
- W2340985547 date "2010-10-08" @default.
- W2340985547 modified "2023-09-26" @default.
- W2340985547 title "Tagging Recombinant Proteins to Enhance Solubility and Aid Purification" @default.
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