title: [Gene cloning and prokaryotic expression of the PID domain of human DOC-2 molecule].
abstract: OBJECTIVE
  To clone the PID domain of human DOC-2 (nDOC-2) and express it in E.coli DH5alpha.
  
  
  METHODS
  The cDNA fragment encoding the PID domain of nDOC-2 was amplified by RT-PCR from normal human ovarian tissue and cloned to pUC19. The DNA fragment from the pUC19-nDOC-2 digested with BamH I and EcoR I was ligated to the BamH I/EcoR I digested prokaryotic expression vector pGEX-4T-1.The expression of fusion protein was induced with IPTG and the expressed product was identified by SDS-PAGE.
  
  
  RESULTS
  (1)The sequencing and endonucleases digestion analysis showed that the fragment of nDOC-2 gene was insert into vectors pUC19 and pGEX-4T-1;(2)SDS-PAGE showed the nDOC-2 gene had been expressed in E.coli DH5alpha.
  
  
  CONCLUSIONS
  The PID domain of nDOC-2 was expressed successfully in prokaryote, which makes preparation for further researching the function of DOC-2 and preparing antibodies to DOC-2 protein.
authors.affiliation: Department of Obstetrics and Gynecology,Xijing Hospital, Fourth Military Medical University, Xi'an 710032 China.
authors.forename: Shu-Juan
authors.initials: SJ
authors.lastname: Liu
authors.forename: Wei-Guo
authors.initials: WG
authors.lastname: Zheng
authors.forename: Zong-Ling
authors.initials: ZL
authors.lastname: Ji
authors.forename: Su-Min
authors.initials: SM
authors.lastname: Chen
authors.forename: Xin-Hai
authors.initials: XH
authors.lastname: Zhang
authors.forename: Li-Jun
authors.initials: LJ
authors.lastname: Yang
mesh_terms: D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D015870:Gene Expression; D005822:Genetic Vectors; D006801:Humans; D010957:Plasmids