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Chinese Journal of Biotechnology ; (12): 589-592, 2007.
Article in Chinese | WPRIM | ID: wpr-327982

ABSTRACT

To produce membrane-permeable human epidermal growth factor (hEGF), a pPTD-hEGF prokaryocyte expression vector was constructed and transformed into E. coli BL 21 (DE3). The PTD-hEGF fusion protein was induced by 0.3 mmol/L of IPTG expressed in the form of inclusion body with an yield of 40% of the total protein in the cells, and then purified by Ni2+ -NTA affinity chromatography. The SDS-PAGE analysis showed a single fusion protein band with a molecular weight of 16 kD. The amino acid sequence was checked by MALDI-TOF-MS analysis. The genetic engineering PTD-hEGF fusion protein obviously promoted the proliferation and growth of the HEK-293 cells in vitro.


Subject(s)
Humans , Amino Acid Sequence , Cell Line , Cell Proliferation , Epidermal Growth Factor , Genetics , Escherichia coli , Genetics , Metabolism , Molecular Sequence Data , Recombinant Fusion Proteins , Genetics , Pharmacology , Transduction, Genetic
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