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

Authors :
Liu GQ
Wu HY
Zhang GB
Ma HB
Ma ZN
Ju SG
Zhang XG
Source :
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology [Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi] 2007 Aug; Vol. 23 (8), pp. 715-8.
Publication Year :
2007

Abstract

Aim: To investigate the biological activity of recombinant human IL-17 protein in vitro.<br />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.<br />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.<br />Conclusion: IL-17/His recombinant protein is of high biological activity, which can be used to make further study of auto-immune diseases.

Details

Language :
Chinese
ISSN :
1007-8738
Volume :
23
Issue :
8
Database :
MEDLINE
Journal :
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology
Publication Type :
Academic Journal
Accession number :
17618562