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Updated: Mar 24, 2026
High Yield Expression of Recombinant Human Proteins with the Transient Transfection of HEK293 Cells in Suspension
Published on: December 28, 2015
Expression, purification and characterization of a vascular endothelial growth factor fusion protein
Yu Zhang1, Yue Tong1, Mingming Gao2
1State Key Laboratory of Natural Medicines, School of Life Science and Technology, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, 210009, China.
Objectives:
To prepare recombinant tPep-(vascular endothelial growth factor) VEGF-B and assess its biological activity.
Results:
This new VEGF fusion protein was constructed using a targeting peptide and prepared using E.coli. The tPep-VEGF-B was refolded from inclusion bodies and purified using affinity chromatography. Its bioactivity was determined in vitro using proliferation assay and wounding healing assay, and in vivo in zebrafish. By using the optimized downstream process, recombinant tPep-VEGF-B can be obtained with a purity of >90 % and a yield of 80 mg protein/l culture medium. The refolded protein is highly effective in promoting cell migration in vitro and in enhancing angiogenesis in vivo.
Conclusion:
We have constructed a new VEGF fusion protein with potential therapeutic application in treating metabolic diseases.
