[Prokaryotic expression, purification and biological activity of recombinant human IL-17/His protein].

Aim: To investigate the biological activity of recombinant human IL-17 protein in vitro.

Methods: The gene region of human IL-17 was cloned by RT-PCR. After identification by sequencing, the hIL-17 gene encoding function domain was cloned into expression plasmid PQE3.0 and transfect into E.coli M15. By the induction of Isopropyl-beta-D-Thiogalacto-Pyranoside (IPTG), recombinant IL-17/His protein was effectively expressed in E.coli M15. The recombinant protein was identified by Western blot.

Results: After denaturation, renaturation and purification by HiTrap affinity column, the recombinant protein stimulated HeLa, a human uterine cervix cancer cell line, to excrete IL-6 and GM-CSF in vitro.

Conclusion: IL-17/His recombinant protein is of high biological activity, which can be used to make further study of auto-immune diseases.