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.
Original language | English (US) |
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Pages (from-to) | 1227-1231 |
Number of pages | 5 |
Journal | Data in Brief |
Volume | 8 |
DOIs | |
State | Published - Sep 2016 |
Keywords
- Axon guidance
- Mical
- Plexin
- Redox
- Repulsion
- Semaphorin
ASJC Scopus subject areas
- General