SNAP- and CLIP-tag protein labeling systems enable the specific, covalent attachment of virtually any molecule to a protein of interest. There are two steps to using this system: cloning and expression of the protein of interest as a SNAP-tag® fusion, and labeling of the fusion with the SNAP-tag substrate of choice. The SNAP-tag is a small protein based on human O6-alkylguanine-DNA-alkyltransferase (hAGT), a DNA repair protein. SNAP-tag substrates are dyes, fluorophores, biotin, or beads conjugated to guanine or chloropyrimidine leaving groups via a benzyl linker. In the labeling reaction, the substituted benzyl group of the substrate is covalently attached to the SNAP-tag. CLIP-tag™ is a modified version of SNAP-tag, engineered to react with benzylcytosine rather than benzylguanine derivatives. When used in conjunction with SNAP-tag, CLIP-tag enables the orthogonal and complementary labeling of two proteins simultaneously in the same cells.
SNAP-tag® Technologies: Tools to Study Protein Function
Read about the NEB’s set of protein tools for the specific labeling (SNAP-, CLIP-, ACP- and MCP-tags) of fusion proteins.
- Cellular Imaging & Analysis Brochure
- Purification Beads, Columns and Resins Brochure
- Comparison of SNAP-tag®/CLIP-tag™ Technologies to GFP
- Labeling with SNAP-tag® Technology Troubleshooting Guide
- Genome-wide profiling of nuclease protected domains reveals physical properties of chromatin (2019)
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- Simultaneous dual protein labeling inside live cells
- Protein localization and translocation
- Pulse-chase experiments
- Receptor internalization studies
- Selective cell surface labeling
- Protein pull-down assays
- Protein detection in SDS-PAGE
- Flow cytometry
- High throughput binding assays in microtiter plates
- Biosensor interaction experiments
- FRET-based binding assays
- Single molecule labeling
- Super-resolution microscopy
Lukinavičius, G. et al. (2015) "Fluorescent labeling of SNAP-tagged proteins in cells" Methods Mol. Biol. 1266, 107-118.
Corrêa Jr., I. R. (2015) "Considerations and protocols for the synthesis of custom protein labeling probes" Methods Mol. Biol. 1266, 55-79.
Corrêa Jr., I. R. (2014) "Live-cell reporters for fluorescence imaging" Curr. Opin. Chem. Biol. 20, 36-45.
Bosch, P. J. et al. (2014) "Evaluation of fluorophores to label SNAP-tag fused proteins for multicolor single-molecule tracking microscopy in live cells" Biophys. J. 107, 803-814.
Smith, B. A. et al. (2013) "Three-color single molecule imaging shows WASP detachment from Arp2/3 complex triggers actin filament branch formation" eLife 2, e01008.
Jaiswal, R. et al. (2013) "The Formin Daam1 and Fascin Directly Collaborate to Promote Filopodia Formation" Curr. Biol. 23, 1373-1379.
Breitsprecher, D. et al. (2012) "Rocket Launcher Mechanism of Collaborative Actin Assembly Defined by Single-Molecule Imaging" Science 336, 1164-1168.
Hoskins, A. A. et al. (2011) "Ordered and dynamic assembly of single spliceosomes." Science 331 (6022), 1289-1295.
Zhao, Z. W. et al. (2014) "Spatial organization of RNA polymerase II inside a mammalian cell nucleus revealed by reflected light-sheet superresolution microscopy" Proc. Natl. Acad. Sci. USA 111, 681-686.
Lukinavičius, G. et al. (2013) "A near-infrared fluorophore for live-cell super-resolution microscopy of cellular proteins" Nat. Chem. 5, 132-139.
Jones, S. A. et al. (2011) "Fast, three-dimensional super-resolution imaging of live cells." Nat. Methods 8, 499-505.
Klein, T. et al. (2011) "Live-cell dSTORM with SNAP-tag fusion proteins." Nat. Methods 8, 7-9.
Pellett, P. A. et al. (2011) "Two-color STED microscopy in living cells." Biomed. Opt. Expr. 2, 2364-2371
Hein, B. et al. (2010) "Stimulated Emission Depletion Nanoscopy of Living Cells Using SNAP-Tag Fusion Proteins." Biophys. J. 98, 158-163.
Tissue and Animal Imaging:
Yang, G. et al. (2015) "Genetic targeting of chemical indicators in vivo" Nat. Methods 12, 137-139.
Kohl, J. et al. (2014) "Ultrafast tissue staining with chemical tags" Proc. Natl. Acad. Sci. USA 111, E3805-E3814.
Ivanova, A. et al. (2013) "Age-dependent labeling and imaging of insulin secretory granules" Diabetes 62, 3687-3696.
Gong, H. et al. (2012) "Near-Infrared Fluorescence Imaging of Mammalian Cells and Xenograft Tumors with SNAP-Tag" PLoS ONE 7(3): e34003.
Bojkowska K. et al. (2011) "Measuring in vivo protein half-life." Chem. Biol. 18, 805-815.
Cell-Surface Protein Labeling and Internalization Analysis:
Bitsikas, V. et al. (2014) "Clathrin-independent pathways do not contribute significantly to endocytic flux" eLife 3, e03970.
Jaensch, N. et al. (2014) "Stable Cell Surface Expression of GPI-Anchored Proteins, but not Intracellular Transport, Depends on their Fatty Acid Structure" Traffic 15, 1305-1329.
Cole, N. B. and Donaldson, J. G. (2012) "Releasable SNAP-tag Probes for Studying Endocytosis and Recycling" ACS Chem. Biol. 7, 464-469.
Rošić, S. et al. (2014) "Repetitive centromeric satellite RNA is essential for kinetochore formation and cell division" J. Cell Biol. 207, 335-349.
Stoops, E. H. et al. (2014) "SNAP-Tag to Monitor Trafficking of Membrane Proteins in Polarized Epithelial Cells" Methods Mol. Biol. 1174, 171-182.
Bordor, D. L. et al. (2012) "Analysis of Protein Turnover by Quantitative SNAP-Based Pulse-Chase Imaging" Curr. Protoc. Cell Biol. 55, 8.8.1-8.8.34.
Register, A. C. et al. (2014) "SH2-Catalytic Domain Linker Heterogeneity Influences Allosteric Coupling across the SFK Family" Biochemistry 53, 6910-6923.
Shi, G. et al. (2012) "SNAP-tag based proteomics approach for the study of the retrograde route" Traffic 13, 914-925.
Bieling, P. et al. (2010) "A minimal midzone protein module controls formation and length of antiparallel microtubule overlaps" Cell 142, 420-432.
Protein-Protein and Protein-Ligand Interactions:
Griss, R. et al. (2014) "Bioluminescent sensor proteins for point-of-care therapeutic drug monitoring" Nat. Chem. Biol. 10, 598-603.
Chidley, C. et al. (2011) "A yeast-based screen reveals that sulfasalazine inhibits tetrahydrobiopterin biosynthesis." Nat. Chem. Biol. 7, 375-383.
Gautier A. et al. (2009) "Selective Cross-Linking of Interacting Proteins using Self-Labeling Tags" J. Am. Chem. Soc. 131, 17954-17962.
Maurel D. et al. (2008) "Cell-surface protein-protein interaction analysis with time-resolved FRET and SNAP-tag technologies: application to GPCR oligomerization." Nat. Methods 5, 561-567.
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This product is intended for research purposes only. This product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
Watch as Chris Provost, of New England Biolabs, performs fluorescent imaging of live COS-7 cells expressing SNAP-tag® fusion proteins.
View an interactive tutorial explaining the mechanism of our SNAP-tag® technologies and reagents available for researchers wishing to study the function and localization of proteins in live or fixed cells.