[Interleukin-6 gene cloning, expression and purification].
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.
Ma
X
X
Institute of Basic Medical Sciences, CAMS and PUMC, Beijing 100005.
Chen
Z
Z
Zheng
H
H
Huang
B
B
Cai
L
L
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
D015850:Interleukin-6; D011994:Recombinant Proteins