Recombinant expression of mouse osteocalcin protein in Escherichia coli |
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| Authors: | Ji-Hyun Kim Soonok Park Hae-Won Kim Jun-Hyeog Jang |
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| Affiliation: | (1) Department of Biochemistry and BK21 Center for Advanced Medical Education, Inha University College of Medicine, Incheon, 400-712, Korea;(2) Department of Biomaterials Science, School of Dentistry, Dankook University, Cheonan, 330-714, Korea |
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| Abstract: | Osteocalcin is the most abundant non-collagenous protein of bone. Recombinant mouse osteocalcin protein (mOC) that includes the highly conserved central domain for binding to hydroxyapatite (HA), a mineral component of bone, was expressed in Escherichia coli. Purified mOC protein exhibited a significant increase in HA adhesion and differentiation in osteoblast cells as well as binding to HA with high affinity. |
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| Keywords: | Bone Cell adhesion Extracellular matrix Osteoblast Osteocalcin |
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