Hyun Kang 
For correspondence:- Email: hkang@dankook.ac.kr Tel:+82415501452
Received: 11 May 2014 Accepted: 9 July 2014 Published: 18 August 2014
Citation:
Kang H.
Biological Activities of Recombinant Liver X Receptor β-Ligand Binding Domain Protein in Tetracycline-Inducible ex
© 2014 The authors.
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Purpose: To investigate tetracycline-inducible ex
Methods: In this study, we have expressed and purified the recombinant liver X receptor β-ligand binding domain proteins in E. coli using a tetracycline inducible system. To allow for biological activities, we subcloned into pPROTet.E HN vector, expressed in E. coli cells under optimized conditions, purified and characterized the recombinant liver X receptor β-ligand-binding domain proteins using fluorescence polarization assay.
Results: The use of pPROTet.E HN vector simplified downstream purification processes, including cleavage and elution thereby increasing the solubility and yield of the protein of interest. There was a 2.3-fold increase in the efficiency of recombinant LXR β-ligand binding domain (LBD) production by optimizing the ex
Conclusion: These findings indicate that recombinant LXR β-LBD protein is a promising target for the development of molecular ligands with improved therapeutic windows.
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