title: Cloning, Expression, and in vitro Functional Activity Assay of phiC31 Integrase cDNA in Escherichia coli.
abstract: OBJECTIVE
  The aim of present study was cloning and expression of phiC31 integrase cDNA in a bacterial expression vector. Thus, an intra molecular assay vector was applied to show in vitro activity of recombinant protein.
  
  
  METHODS
  In this experimental study, phiC31 cDNA was subcloned into a prokaryotic expression vector and transformed into E.coli Bl21 (DE3). Recombinant phiC31 integrase was purified form the bacterial cell lysates and its activity was verified by an in vitro functional assessment.
  
  
  RESULTS
  Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the puriﬁed phiC31 integrase confirmed the size of protein (70 kDa). Finally, the functionality of purified phiC31 integrase was verified.
  
  
  CONCLUSIONS
  The results of this study indicated that the purified integrase has a great potential application for in vitro site-specific integration.
authors.affiliation: 1. Department of Animal Science, Ferdowsi University of Mashhad, Mashhad, Iran.
authors.forename: Mohammad Hadi
authors.initials: MH
authors.lastname: Sekhavati
authors.forename: Mojtaba
authors.initials: M
authors.lastname: Tahmoorespur
authors.forename: Kamran
authors.initials: K
authors.lastname: Ghaedi
authors.forename: Kianoush
authors.initials: K
authors.lastname: Dormiani
authors.forename: Mohammad Reza
authors.initials: MR
authors.lastname: Nassiri
authors.forename: Yahya
authors.initials: Y
authors.lastname: Khazaie
authors.forename: Mahboubeh
authors.initials: M
authors.lastname: Foruzanfar
authors.forename: Morteza
authors.initials: M
authors.lastname: Hosseini
authors.forename: Mohammad Hossein
authors.initials: MH
authors.lastname: Nasr Esfahani
keywords: E.coli BL21 (DE3); Site-Specific Integration; phiC31