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[Prokaryotic expression, purification and biological activity of recombinant human IL-17/His protein].
- 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.
- Subjects :
- Blotting, Western
Cells, Cultured
Escherichia coli genetics
Escherichia coli metabolism
Granulocyte-Macrophage Colony-Stimulating Factor metabolism
HeLa Cells drug effects
HeLa Cells metabolism
Humans
Interleukin-6 metabolism
Plasmids
Reverse Transcriptase Polymerase Chain Reaction
Interleukin-17 genetics
Interleukin-17 metabolism
Recombinant Proteins genetics
Recombinant Proteins metabolism
Subjects
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