Literature DB >> 17598072

Recombinant expression of mouse osteocalcin protein in Escherichia coli.

Ji-Hyun Kim1, Soonok Park, Hae-Won Kim, Jun-Hyeog Jang.   

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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Year:  2007        PMID： 17598072     DOI： 10.1007/s10529-007-9437-z

Source DB:  PubMed          Journal:  Biotechnol Lett        ISSN： 0141-5492            Impact factor:   2.461


  2 in total

1.  Murine GPRC6A Mediates Cellular Responses to L-Amino Acids, but Not Osteocalcin Variants.

Authors:  Patricia Rueda; Elizabeth Harley; Yao Lu; Gregory D Stewart; Stewart Fabb; Natalie Diepenhorst; Béatrice Cremers; Marie-Hélène Rouillon; Isabelle Wehrle; Anne Geant; Gwladys Lamarche; Katie Leach; William N Charman; Arthur Christopoulos; Roger J Summers; Patrick M Sexton; Christopher J Langmead
Journal:  PLoS One       Date:  2016-01-19       Impact factor: 3.240

2.  Uncarboxylated osteocalcin alleviates the inhibitory effect of high glucose on osteogenic differentiation of mouse bone marrow-derived mesenchymal stem cells by regulating TP63.

Authors:  Fangzi Gong; Le Gao; Luyao Ma; Guangxin Li; Jianhong Yang
Journal:  BMC Mol Cell Biol       Date:  2021-04-27
  2 in total

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