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

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 i...

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Bibliographic Details
Published in:Bulletin of experimental biology and medicine 2017-12, Vol.164 (2), p.148-151
Main Authors: Bartov, M. S., Gromov, A. V., Manskih, V. N., Makarova, E. B., Rubshtein, A. P., Poponova, M. S., Savina, D. M., Savin, K. S., Nikitin, K. E., Grunina, T. M., Boksha, I. S., Orlova, P. A., Krivozubov, M. S., Subbotina, M. E., Lunin, V. G., Karyagina, A. S., Gintsburg, A. L.
Format: Article
Language:English
Subjects:
Analysis
Animal models
Biomedical and Life Sciences
Biomedicine
Biophysics and Biochemistry
Bone matrix
Bone morphogenetic protein 2
Bone morphogenetic proteins
Cell Biology
E coli
Escherichia coli
Femur
Internal Medicine
Laboratory animals
Laboratory Medicine
Pathology
Protein purification
Proteins
Regeneration
Skull
Titanium
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Description
Summary: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.
ISSN:0007-4888
1573-8221
DOI:10.1007/s10517-017-3945-1