کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10767389 | 1050723 | 2007 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
High level expression and purification of recombinant PEX protein in cultured skeletal muscle cell expression system
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
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چکیده انگلیسی
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 μg/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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 357, Issue 1, 25 May 2007, Pages 258-263
Journal: Biochemical and Biophysical Research Communications - Volume 357, Issue 1, 25 May 2007, Pages 258-263
نویسندگان
Lin Song, Yang Ke, Zhi-Qian Zhang,