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Updated: May 20, 2026
A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
[Eukaryotic expression of recombinant porcine single-chain IL-12 and its biologic activity]
Xue-mei Wang1, Yuan-ying Yuan, Qiang Fang
1Department of Microbiology and Parasitology, Bengbu Medical College, China. wangxuenm0508@sina.com
Aim:
To express the recombinant porcine single-chain interleukin-12 (pscIL-12) gene in CHO-K1 cells, and identify biological activity of pscIL-12 fusion protein.
Methods:
The recombinant pcDNA3.1(+)-pscIL-12 plasmid was transfected into the CHO-K1 cells using Sofast(TM); reagent. The levels of pscIL-12 fusion protein and IFN-γ produced by human peripheral blood mononuclear cells (PBMCs) stimulated with the supernatant of CHO-K1 cells were detected by ELISA. NK cell cytotoxicity was tested by MTT assay. The lymphocyte proliferation was examined by flow cytometry.
Results:
ELISA showed that the transfected CHO-K1 cells had a relatively higher expression of pscIL-12 fusion protein. And the pscIL-12 fusion protein possessed strong bioactivities in enhancing the NK cell cytotoxicity, increasing the IFN-γ production, and stimulating the lymphocyte proliferation.
Conclusion:
CHO-K1 cells transfected with pcDNA3.1(+)-pscIL-12 recombinant plasmid can successfully express pscIL-12 fusion protein, which has the expected biological activities.
