title: [Expression in E. coli and chemotactic activity analyzing of recombinant CC-chemokine RANTES].
abstract: OBJECTIVE
  To further understand the structure and function of RANTES and provide basis for research for application.
  
  
  METHODS
  PCR product corresponding to region encoding mature RANTES protein was cloned into E. coli expression vector; purified recombinant protein was obtained by heparin affinity chromatography and its chemotactic activity was determined by Boyden chamber.
  
  
  RESULTS
  The recombinant RANTES was expressed in E. coli with high efficiency. Purified protein showed chemotactic activity to peripheral blood lymphocytes, U937 cells, and CCR4 stable-transfected HEK293 cells.
  
  
  CONCLUSIONS
  The purified recombinant protein exerted chemotactic activity on PBL and cultured cell lines, and we have established a experimental system for further study of structure and function of RANTES.
authors.affiliation: Laboratory of Molecular Immunology, Health Science Center, Peking University, Beijing 100083, China.
authors.forename: R H
authors.initials: RH
authors.lastname: Sun
authors.forename: Y
authors.initials: Y
authors.lastname: Wang
authors.forename: Y C
authors.initials: YC
authors.lastname: Zhong
authors.forename: D L
authors.initials: DL
authors.lastname: Ma
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D018946:Chemokine CCL5 / Q000096:biosynthesis* / Q000235:genetics / Q000494:pharmacology*; D002633:Chemotaxis / Q000187:drug effects*; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000494:pharmacology
chemical_list: D018946:Chemokine CCL5; D011994:Recombinant Proteins