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Updated: May 28, 2026
Non-chromatographic Purification of Recombinant Elastin-like Polypeptides and their Fusions with Peptides and Proteins from Escherichia coli
Published on: June 9, 2014
Expression and purification of two alternative peptides for mechano-growth factor in Escherichia coli
Li Song1, Wen-Si Zhu, Jun-Li Dong
1Institute of Biotechnology, Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, Shanxi University, Taiyuan, 030006, China. lsong@sxu.edu.cn
Abstract:
Two genes, MGFc (40) and MGFc (24), encoding different E peptides of mechano-growth factor (MGF), were obtained by a four-step PCR strategy and subcloned into pRSETC and pGEX-6p-1. Recombinant MGFc(40) protein (4 mg l(-1)) was expressed and purified by affinity chromatography using His60 Ni Superflow. Recombinant MGFc(24) protein was purified using a glutathione-Sepharose 4B column. After enzymatic cleavage of the GST-tail, 1 mg MGFc(24) protein l(-1) was obtained. MGFc(40) and MGFc(24), which are involved in proliferation and differentiation, stimulated cell proliferation and inhibited cell differentiation of C2C12 cells.
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