title: Uninduced high-yield bacterial expression of fluorescent proteins.
abstract: Here we introduce a fast, cost-effective, and highly efficient method for production of soluble fluorescent proteins from bacteria. The method does not require optimization and does not use isopropyl β-d-1-thiogalactopyranoside (IPTG) induction. The method relies on uninduced expression in the BL21-Gold (DE3) strain of Escherichia coli and yields large amounts (up to 0.4 μmol) of fluorescent protein from a 250-ml culture. This method is much simpler than published methods and can be used to produce any fluorescent protein that is needed in biomedical research.
authors.affiliation: Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
authors.forename: Sarvenaz
authors.initials: S
authors.lastname: Sarabipour
authors.affiliation: Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
authors.forename: Christopher
authors.initials: C
authors.lastname: King
authors.affiliation: Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21218, USA; Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA. Electronic address: kh@jhu.edu.
authors.forename: Kalina
authors.initials: K
authors.lastname: Hristova
mesh_terms: D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression; D008164:Luminescent Proteins / Q000235:genetics*; D011994:Recombinant Proteins / Q000235:genetics
chemical_list: D008164:Luminescent Proteins; D011994:Recombinant Proteins
keywords: E. coli; FRET; Fluorescent protein; Gene expression; High yield; His-tag; Protein production