Uninduced high-yield bacterial expression of fluorescent proteins

Sarvenaz Sarabipour; Christopher King; Kalina Hristova

doi:10.1016/j.ab.2013.12.027

Uninduced high-yield bacterial expression of fluorescent proteins

Anal Biochem. 2014 Mar 15:449:155-7. doi: 10.1016/j.ab.2013.12.027. Epub 2013 Dec 28.

Authors

Sarvenaz Sarabipour¹, Christopher King², Kalina Hristova³

Affiliations

¹ Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
² Program in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
³ 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.

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.

Keywords: E. coli; FRET; Fluorescent protein; Gene expression; High yield; His-tag; Protein production.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Escherichia coli / genetics*
Gene Expression
Luminescent Proteins / genetics*
Recombinant Proteins / genetics

Substances

Luminescent Proteins
Recombinant Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding