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Fluorescent labeling of SNAP-tagged proteins in cells.


Lukinavicius,  G.
Laboratory of Chromatin Labeling and Imaging, Max Planck Institute for Biophysical Chemistry, Max Planck Society;

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Lukinavicius, G., Reymond, L., & Johnsson, K. (2015). Fluorescent labeling of SNAP-tagged proteins in cells. In A. Gautier, & M. J. Hinner (Eds.), Site-Specific Protein Labeling (pp. 107-118). New York, N.Y.: Springer Nature. doi:10.1007/978-1-4939-2272-7_7.

Cite as: http://hdl.handle.net/21.11116/0000-0001-E423-6
One of the most prominent self-labeling tags is SNAP-tag. It is an in vitro evolution product of the human DNA repair protein O 6-alkylguanine-DNA alkyltransferase (hAGT) that reacts specifically with benzylguanine (BG) and benzylchloropyrimidine (CP) derivatives, leading to covalent labeling of SNAP-tag with a synthetic probe (Gronemeyer et al., Protein Eng Des Sel 19:309–316, 2006; Curr Opin Biotechnol 16:453–458, 2005; Keppler et al., Nat Biotechnol 21:86–89, 2003; Proc Natl Acad Sci U S A 101:9955–9959, 2004). SNAP-tag is well suited for the analysis and quantification of fused target protein using fluorescence microscopy techniques. It provides a simple, robust, and versatile approach to the imaging of fusion proteins under a wide range of experimental conditions.