title: [Interleukin-6 gene cloning, expression and purification].
abstract: OBJECTIVE
  The main purpose of this paper is to study the batch production of recombinant human interleukin-6(rhIL-6).
  
  
  METHODS
  The cloned rhIL-6 gene is under the control of T7 promoter of pET30a vector and expressed in E. coli.
  
  
  RESULTS
  The ratio of expressed recombinant protein to total cell protein is more than 50%. The rhIL-6 molecular weight is 21,000, isoelectric point is 6.7. The purity of the rhIL-6 is more than 95%, and the activity of rhIL-6, determined by IL-6 dependent mice hybridoma cell line 7TD1 and MTT assay, is 0.35 ng/ml.
  
  
  CONCLUSIONS
  All results mentioned show that rhIL-6 meets the request of the middle scale production.
authors.affiliation: Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005.
authors.forename: X
authors.initials: X
authors.lastname: Ma
authors.forename: Z
authors.initials: Z
authors.lastname: Chen
authors.forename: H
authors.initials: H
authors.lastname: Zheng
authors.forename: B
authors.initials: B
authors.lastname: Huang
authors.forename: L
authors.initials: L
authors.lastname: Cai
mesh_terms: D003001:Cloning, Molecular; D004926:Escherichia coli / Q000378:metabolism; D015850:Interleukin-6 / Q000096:biosynthesis / Q000235:genetics* / Q000302:isolation & purification; D011401:Promoter Regions, Genetic; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification
chemical_list: D015850:Interleukin-6; D011994:Recombinant Proteins