High level expression and purification of recombinant PEX protein in cultured skeletal muscle cell expression system |
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Authors: | Song Lin Ke Yang Zhang Zhi-Qian |
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Institution: | Department of Cell Biology, Peking University School of Oncology, Beijing Cancer Hospital & Institute, Beijing 100036, China. |
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Abstract: | Large quantities of recombinant proteins are needed for specific therapeutic and diagnostic applications. To achieve high-level expression in eukaryotic cells, the choice of cell line as well as the expression vector is critical. In this report, we demonstrate that a combination of the skeletal muscle cell line, QM7 and a cytomegalovirus promoter-based expression vector can achieve high-level expression of secretory recombinant proteins in eukaryotic cells. We also screened a serum-free medium containing 3 microg/ml insulin suitable for QM7 differentiation and identified a very potent signal peptide from MMP9, which effectively directs secretion of heterologous proteins. The C-terminal hemopexin-like domain of MMP-2, PEX, a powerful candidate for the treatment of diseases associated with neovascularization was expressed in QM7 cells with bioactivity. This skeletal muscle cell-based system may be employed for the production of human proteins of special interests, such as those for structural determination or therapeutical development. |
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Keywords: | QM7 Expression system Skeletal muscle PEX Signal peptide MMP9 |
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