Author/Authors :
Boozarpour، Sohrab نويسنده Department of Genetics, Faculty of Biological Sciences, Tarbiat Modares University, P.O. Box 14115-154, Tehran, I.R. Iran , , Sadeghizadeh، Majid نويسنده , , Shokrgozar، Mohammad Ali نويسنده , , Hosseinkhani، Saman نويسنده , , Shojaosadati، Seyed Abbas نويسنده , , Gharavi، Sara نويسنده Department of Biology, Faculty of Science, Alzahra University, Tehran, IR Iran , , Ahangari، Ghasem نويسنده Department of Medical Genetics, National Institute of Genetic Engineering and Biotechnology , , Ranjbar، Bijan نويسنده ,
Abstract :
Selection of a system for successful recombinant protein production is important. The aim of this study was to produce high levels of human interleukin-2 (hIL-2) in soluble form. To this end, the pET32a vector in Escherichia coli BL21 (DE3) was used as an expression system, since it was previously used for the production of mouse IL-2 in soluble form. The results indicated that contrary to expectations, the expressed protein was in the form of inclusion bodies and perhaps amino acid differences between human and mouse IL-2 should be determinant. The hIL-2 protein is a small peptide, therefore its recovery as a biologically functional protein by the process of refolding may be feasible and could lead to high yields at the industrial scale.
