Recombinant human bone morphogenetic protein-2 with an additional s-tag domain (s-tag-BMP-2) synthesized in E. coli is characterized by higher solubility and activity than the protein without additional s-tag domain, which increases the yield during purification and simplifies protein introduction into the osteoplastic materials. The high osteoinductivity of the demineralized bone matrix with s-tag-BMP-2 was shown on the model of regeneration of cranial defects of a critical size in mice and on the model of implantation of porous titanium matrix into defects of femoral and tibial bones in rabbits.
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Translated from Byulleten’ Eksperimental’noi Biologii i Meditsiny, Vol. 164, No. 8, pp. 173-176, August, 2017
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Bartov, M.S., Gromov, A.V., Manskih, V.N. et al. Recombinant Human Bone Morphogenetic Protein-2 (rhBMP-2) with Additional Protein Domain Synthesized in E. coli: In Vivo Osteoinductivity in Experimental Models on Small and Large Laboratory Animals. Bull Exp Biol Med 164, 148–151 (2017). https://doi.org/10.1007/s10517-017-3945-1
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DOI: https://doi.org/10.1007/s10517-017-3945-1