Data presenting a modified bacterial expression vector for expressing and purifying Nus solubility-tagged proteins

Nidhi Gupta, Heng Wu, Jonathan R. Terman

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

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 languageEnglish (US)
Pages (from-to)1227-1231
Number of pages5
JournalData in Brief
Volume8
DOIs
StatePublished - Sep 2016

Keywords

  • Axon guidance
  • Mical
  • Plexin
  • Redox
  • Repulsion
  • Semaphorin

ASJC Scopus subject areas

  • General

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