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.
Original language | English (US) |
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Pages (from-to) | 155-157 |
Number of pages | 3 |
Journal | Analytical biochemistry |
Volume | 449 |
Issue number | 1 |
DOIs | |
State | Published - Mar 15 2014 |
Keywords
- E. coli
- FRET
- Fluorescent protein
- Gene expression
- High yield
- His-tag
- Protein production
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology