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.
OBJECTIVE: The main purpose of this paper is to study the batch production of recombinant humaninterleukin-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.