Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional N-terminal protein domains were obtained by expression in E. coli. The N-terminal domains were s-tag (15-a.a. oligopeptide from bovine pancreatic ribonuclease A) and lz (leucine zipper dimerization domain from yeast transcription factor GCN4). The s-tag-BMP-2 and lz-BMP-2 were purified by a procedure that excluded a long refolding stage. The resulting dimeric proteins displayed higher solubility compared to rhBMP-2 without additional protein domains. Biological activity of both proteins was demonstrated in vitro by induction of alkaline phosphatase in C2C12 cells, and the activity of s-tag-BMP-2 in vivo was shown in various experimental animal models.
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Karyagina, A. S., Boksha, I. S., Grunina, T. M., Demidenko, A. V., Poponova, M. S., Sergienko, O. V., … Lunin, V. G. (2017). Two variants of recombinant human bone morphogenetic protein-2 (rhBMP-2) with additional protein domains: Synthesis in an Escherichia coli heterologous expression system. Biochemistry (Moscow), 82(5), 613–624. https://doi.org/10.1134/S0006297917050091
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