Abstract
We present a fluorescence activation-coupled protein labeling (FAPL) method, which employs small-molecular probes that exhibit almost no basal fluorescence but acquire strong fluorescence upon covalent binding to tag-proteins. This method enables real-time imaging of protein labeling without any washout process and is uniquely suitable for real-time imaging of protein dynamics on the cell surface. We applied this method to address the spatiotemporal dynamics of the EGF receptor during cell migration.
Original language | English (US) |
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Pages (from-to) | 6745-6751 |
Number of pages | 7 |
Journal | Journal of the American Chemical Society |
Volume | 133 |
Issue number | 17 |
DOIs | |
State | Published - May 4 2011 |
ASJC Scopus subject areas
- Catalysis
- General Chemistry
- Biochemistry
- Colloid and Surface Chemistry