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BASIC RESEARCH
Year : 2018  |  Volume : 8  |  Issue : 7  |  Page : 360-364

Expression of fluorescent tagged recombinant erythroferrone protein


1 Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand; Department of Biochemistry, University of Medicine, Mandalay, Myanmar
2 Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai, Thailand
3 Protein-Ligand Engineering and Molecular Biology Laboratory, National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, Thailand Science Park, Pathum Thani, Thailand

Correspondence Address:
Somdet Srichairatanakool
Department of Biochemistry, Faculty of Medicine, Chiang Mai University, Chiang Mai 50200
Thailand
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/2221-1691.237079

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Objective: To produce fluorescent tagged recombinant erythroferrone protein (ERFE_eGFP) for laboratory investigations. Methods: Erythroferrone (ERFE) gene was fused to green fluorescent protein (eGFP) gene and cloned in a pSecTag2Hygro plasmid. The constructed plasmid was amplified in Escherichia coli DH5 α and the eGFP-fused ERFE (ERFE_eGFP) protein was expressed in human embryonic kidney (HEK293T) cell line. Results: The plasmid constructed from colony C6 contained ERFE_eGFP with the correct restriction sizes of 4.2 kb and expressed secretory ERFE_eGFP fusion protein (approximately size of 75 kDa) in HEK293T cell line. Conclusions: ERFE_eGFP recombinant protein is successfully expressed as a secretory functional protein and could be sensitively detected using fluorometry. This fusion protein might benefit future applications for localization of cellular ERFE receptors and competitive immunoassay of ERFE concentration.


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