ArticleData in brief2016
Data presenting a modified bacterial expression vector for expressing and purifying Nus solubility-tagged proteins.
Article in Data in brief, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- Enhanced Production of the Mical Redox Domain for Enzymology and F-actin Disassembly Assays.International journal of molecular sciences · 2021Article
- The MICALs are a Family of F-actin Dismantling Oxidoreductases Conserved from Drosophila to Humans.Scientific reports · 2018Article
- A simple and efficient method for generating high-quality recombinant Mical enzyme for in vitro assays.Protein expression and purification · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Bacteria are the predominant source for producing recombinant proteins but while many exogenous proteins are expressed, only a fraction of those are soluble. We have found that a new actin regulatory enzyme Mical is poorly soluble when expressed in bacteria but the use of a Nus fusion protein tag greatly increases its solubility. However, available vectors containing a Nus tag have been engineered in a way that hinders the separation of target proteins from the Nus tag during protein purification. We have now used recombinant DNA approaches to overcome these issues and reengineer a Nus solubility tag-containing bacterial expression vector. The data herein present a modified bacterial expression vector useful for expressing proteins fused to the Nus solubility tag and separating such target proteins from the Nus tag during protein purification.
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