Cloning and Expression of Recombinant Human Bone Morphogenetic Protein-2 in E.Coli
Wang Jie
Abstract
Wang Jie
Abstract
Objective To construct a recombinant prokaryotic expression plasmid containg human bone morphogenetic protein-2 and express the protein in E.coli. Methods The mature peptide gene of human BMP-2 was amplified from human bone marrow and cloned into prokaryotic expression vector pBV220. The recombinant plasmid pBV220/BMP-2 was identified by DNA sequencing,before transfected into E.coli JM109. The recombinant protein expressed in E.coli was detected using western blot and ELISA.Results Sequencing analysis confirmed the sequence of recombinant BMP-2. The recombinant BMP2 protein was expressed with the right size as expected and displayed binding activity with its specific antibody.Conclusion The mature peptide gene of human BMP-2 has been successfully cloned and expressed in E.coli.
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Objective To construct a recombinant prokaryotic expression plasmid containg human bone morphogenetic protein-2 and express the protein in E.coli. Methods The mature peptide gene of human BMP-2 was amplified from human bone marrow and cloned into prokaryotic expression vector pBV220. The recombinant plasmid pBV220/BMP-2 was identified by DNA sequencing,before transfected into E.coli JM109. The recombinant protein expressed in E.coli was detected using western blot and ELISA.Results Sequencing analysis confirmed the sequence of recombinant BMP-2. The recombinant BMP2 protein was expressed with the right size as expected and displayed binding activity with its specific antibody.Conclusion The mature peptide gene of human BMP-2 has been successfully cloned and expressed in E.coli.
Key concepts: Recombinant DNA, Plasmid, Molecular biology, Cloning (programming), Biology, Bone morphogenetic protein 2, Bone morphogenetic protein, Gene