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Abstract
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In the last two decades, prokaryotic expression systems, particularly E. coli was a dominant expression system
suitable for laboratory research as well for commercial production. Because of many advantages such as low cost
and ease of culture and high growth rate, it is suitable for production of recombinant proteins for pharmaceutical
applications. Human insulin-like growth factor (hIGF-1) is one of these pharmaceutical proteins, which is
essential for embryo development and cell proliferation and differentiation, and stimulation of different cell
types. In this research, IGF-1 expression using the expression vector pGBKT7-IGF1, in E. coli strain BL21 was
evaluated. Results showed that noticeable amount of the IGF-1 protein is produced in E. coli.
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