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SNAP-tag® Substrates

NEB offers a large selection of fluorescent labels (substrates) for SNAP-fusion proteins. SNAP-tag® substrates consist of a fluorophore conjugated to guanine or chloropyrimidine leaving groups via a benzyl linker. Substrates label the SNAP-tag® without the need for additional enzymes. Cell-permeable substrates (SNAP-Cell®) are suitable for both intracellular and cell-surface labeling, whereas non-cell-permeable substrates (SNAP-Surface®) are specific for fusion proteins expressed on the cell surface only.

SNAP-tag®, SNAP-Cell® and SNAP-Surface® are registered trademarks of New England Biolabs, Inc.

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Protocols for SNAP-tag® Substrates

    Publications related to SNAP-tag® Substrates

  1. George N. et al. 2004. Specific labeling of cell surface proteins with chemically diverse compounds J .Am. Chem. Soc.  . 126, PubMedID: 15264811, DOI:
  2. La Clair, J.J. et al. 2004. Manipulation of carrier proteins in antibiotic biosynthesis Chem. Biol. . 11, PubMedID: 15123281, DOI:
  3. Prummer M. et al. 2006. Post-translational covalent labeling reveals heterogeneous mobility of individual G protein-coupled receptors in living cells ChemBioChem . 7, PubMedID: 16607667, DOI:
  4. Jacquier V. et al. 2006. Visualizing receptor trafficking in living PNAS . 103, PubMedID: 16980412, DOI:
  5. Meyer B.H. et al. 2006. Covalent labeling of cell-surface proteins for in vivo FRET studies FEBS Letters . 580, PubMedID: 16497304, DOI:
  6. Meyer B.H. et al. 2006. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells Proc. Natl. Acad. Sci. USA . 103, PubMedID: 16461466, DOI:
  7. Cravatt B.F. 2005. Live chemical reports from the cell surface Chem. Biol. . 12, PubMedID: 16183017, DOI:
  8. Vivero-Pol L. et al. 2005. Multicolor imaging of cell surface proteins J. Am. Chem. Soc. . 127, PubMedID: 16159249, DOI:
  9. Yin J. et al. 2005. Single-cell FRET imaging of transferrin receptor trafficking dynamics by Sfp-catalyzed, site-specific protein labeling Chem. Biol . 12, PubMedID: 16183024, DOI:
  10. Yin J. et al. 2005. Labeling proteins with small molecules by site-specific posttranslational modification J Am Chem Soc. 126 , PubMedID: 15212504, DOI:
  11. Mosiewicz, K. A. et al. 2010. Phosphopantetheinyl Transferase-Catalyzed Formation of Bioactive Hydrogels for Tissue Engineering J. Am. Chem. Soc. . 132, PubMedID: 20373804, DOI:
  12. Waichman S. et al. 2010. Functional Immobilization and Patterning of Proteins by an Enzymatic Transfer Reaction Anal. Chem. . 82 , PubMedID: 20092261, DOI:
  13. Zelman-Femiak, M. et al. 2010. Covalent quantum dot receptor linkage via the acyl carrier protein for single-molecule tracking, internalization, and trafficking studies BioTechniques . 49, PubMedID: 20701592, DOI:
  14. Liu E and Bruner S. D. 2007. Rational manipulation of carrier-domain geometry in nonribosomal peptide synthetases ChemBioChem. . 8, PubMedID: 17335097, DOI:
  15. Zhou Z. et al. 2007. Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases ACS Chemical Biology . 2, PubMedID: 17465518, DOI:
  16. Gralle M. et al. 2009. Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers J. Biol. Chem. . 284, PubMedID: 19336403, DOI:
  17. Neugart F. et al. 2009. Detection of ligand-induced CNTF receptor dimers in living cells by fluorescence cross correlation spectroscopy Biochim. Biophys. Acta.  .  1788 , PubMedID: 19482006, DOI:
  18. Eggeling C. et al. 2009. Direct observation of the nanoscale dynamics of membrane lipids in a living cell Nature . 457 , PubMedID: 19098897, DOI:
  19. Generosi J. et al. 2008. Photobleaching-free infrared near-field microscopy localizes molecules in neurons J. App. Phys. . 104, PubMedID: , DOI:
  20. Kropf M. et al. 2008. Subunit-specific surface mobility of differentially labeled AMPA receptor subunits Eur. J. Cell Biol. . 87, PubMedID: 18547676, DOI:
  21. Generosi J. et al. 2008. AMPA receptor imaging by infrared scanning near-field optical microscopy Physica Status Solidi C: Current Topics in Solid State Physics . 5, PubMedID: , DOI:
  22. Sunbul M. et al. 2008. Enzyme catalyzed site-specific protein labeling and cell imaging with quantum dots Chem. Comm. . , PubMedID: 19030541, DOI:

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This product is covered by one or more patents, trademarks and/or copyrights owned or controlled by New England Biolabs, Inc (NEB).

While NEB develops and validates its products for various applications, the use of this product may require the buyer to obtain additional third party intellectual property rights for certain applications.

For more information about commercial rights, please contact NEB's Global Business Development team at gbd@neb.com.

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.

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    Fluorescent Labeling of COS-7 Expressing SNAP-tag Fusion Proteins for Live Cell Imaging

    Watch as Chris Provost, of New England Biolabs, performs fluorescent imaging of live COS-7 cells expressing SNAP-tag® fusion proteins.

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    SNAP-tag Overview Tutorial

    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.