ArticleChembiochem : a European journal of chemical biology2011
Development of SNAP-tag fluorogenic probes for wash-free fluorescence imaging.
Article in Chembiochem : a European journal of chemical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.
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121 citing papers in PubMed.
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- A novel cyan-emitting fluorescent α-amino acid: synthesis, photophysical characterization and live-cell imaging properties.RSC advances · 2026Article
- Single-Molecule Localization Microscopy in the Nucleus with Self-Labelling Tags: Halo, SNAP, and CLIP Tags.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Active regulation of the epidermal growth factor receptor by the membrane bilayer.bioRxiv : the preprint server for biology · 2025Article
- SNAP-tag2 for faster and brighter protein labeling.Nature chemical biology · 2025Article
- Chemigenetic Encoding of Fluorescent Dyes Enables High-Fidelity and Wash-Free Imaging of Proteins in Live Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
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- Triple Labeling Resolves a GPCR Intermediate State by Using Three-Color Single Molecule FRET.Journal of the American Chemical Society · 2025Article
- Conditional Control of Benzylguanine Reaction with the Self-Labeling SNAP-tag Protein.Bioconjugate chemistry · 2025Article
- Autoproteolytic mechanism of CdiA toxin release reconstitutedJournal of bacteriology · 2024Article
- ProDOL: a general method to determine the degree of labeling for staining optimization and molecular counting.Nature methods · 2024Article
- Multiplex basophil activation tests for allergy diagnosis: present and future applications.Frontiers in allergy · 2024Review
- Fluorescent Investigation of Proteins Using DNA-Synthetic Ligand Conjugates.Bioconjugate chemistry · 2023Review
- Design of a palette of SNAP-tag mimics of fluorescent proteins and their use as cell reporters.Cell discovery · 2023Article
- Visualization of multiple localizations of GLUT4 by fluorescent probes of PYP-tag with designed unnatural warhead.Chemical science · 2023Article
- Post-translational covalent assembly of CAR and synNotch receptors for programmable antigen targeting.Nature communications · 2023Article
- Nanoscale structural organization and stoichiometry of the budding yeast kinetochore.The Journal of cell biology · 2023Article
- Cell-Surface Targeting of Fluorophores inACS chemical neuroscience · 2023Article
61 more citing papers are in PubMed but not listed here.
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12 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The ability to specifically attach chemical probes to individual proteins represents a powerful approach to the study and manipulation of protein function in living cells. It provides a simple, robust and versatile approach to the imaging of fusion proteins in a wide range of experimental settings. However, a potential drawback of detection using chemical probes is the fluorescence background from unreacted or nonspecifically bound probes. In this report we present the design and application of novel fluorogenic probes for labeling SNAP-tag fusion proteins in living cells. SNAP-tag is an engineered variant of the human repair protein O(6)-alkylguanine-DNA alkyltransferase (hAGT) that covalently reacts with benzylguanine derivatives. Reporter groups attached to the benzyl moiety become covalently attached to the SNAP tag while the guanine acts as a leaving group. Incorporation of a quencher on the guanine group ensures that the benzylguanine probe becomes highly fluorescent only upon labeling of the SNAP-tag protein. We describe the use of intramolecularly quenched probes for wash-free labeling of cell surface-localized epidermal growth factor receptor (EGFR) fused to SNAP-tag and for direct quantification of SNAP-tagged β-tubulin in cell lysates. In addition, we have characterized a fast-labeling variant of SNAP-tag, termed SNAP(f), which displays up to a tenfold increase in its reactivity towards benzylguanine substrates. The presented data demonstrate that the combination of SNAP(f) and the fluorogenic substrates greatly reduces the background fluorescence for labeling and imaging applications. This approach enables highly sensitive spatiotemporal investigation of protein dynamics in living cells.
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