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Cellular Analysis

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.

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Cellular Analysis includes these subcategories:
SNAP-tag® Substrates
CLIP-tag™ Substrates
Blocking Agents
Cellular Analysis Vectors
Biotin Labels
Building Blocks
FAQs for Cellular Analysis
    Publications related to Cellular Analysis
    • Maffei, M., Morelli, C., Graham, E., Patriarca, S., Donzelli, L., Doleschall, B., de Castro, Reis, F., Nocchi, L., Chadick, C.H., Reymond, L., Correa, I.R., Jr., Johnsson, K., Hackett, J.A., Heppenstall, P.A (2019) A ligand based system for receptor specific delivery of proteins Sci Rep; 9(1), 19214.. PubMedID: 31844114, DOI: 10.1038/s41598-019-55797-1
    • Eckhardt, M. et al. (2011) A SNAP-tagged detivative of HIV-1 - A versatile tool to study virus-cell interactions PLoS One; 6:e22007 . PubMedID: 21799764, DOI: 10.137/journal. P One .0022007
    • Hoskins, A. et al. (2011) Ordered and dynamic assembly of single spliceoseoms Science; 331 , 1289 . PubMedID: 21393538
    • Kufer S.K. et al. (2005) Covalent immobilization of recombinant fusion proteins with hAGT for single molecule force spectroscopy Eur Biophys J; 35, 72-78. PubMedID: 16160825
    • Cravatt B.F. (2005) Live chemical reports from the cell surface Chem Biol; 12, 954-956 . PubMedID: 16183017
    • Vivero-Pol L. et al. (2005) Multicolor imaging of cell surface proteins J Am Chem Soc; 127, 12770-12771 . PubMedID: 16159249
    • Juillerat A. et al. (2005) Engineering substrate specificity of O6-alkylguanine-DNA alkyltransferase for specific protein labeling in living cells Chembiochem; 6, 1263-1269 . PubMedID: 15934048
    • Yin J. et al. (2005) Labeling proteins with small molecules by site-specific posttranslational modification J Am Chem Soc; 126 , 7754-7755 . PubMedID: 15212504
    • Johnsson N. et al. (2005) Protein chemistry on the surface of living cells Chembiochem; 6 , 47-52 . PubMedID: 15558647
    • Yin J. et al. (2005) Single-cell FRET imaging of transferrin receptor trafficking dynamics by Sfp-catalyzed, site-specific protein labeling Chem Biol; 12, 999-1006 . PubMedID: 16183024
    • Tugulu S. et al. (2005) Protein-functionalized polymer brushes Biomacromolecules; 6, 1602-1607. PubMedID: 15877383
    • Regoes A. et al. (2005) SNAP-tag mediated live cell labeling as an alternative to GFP in anaerobic organisms Biotechniques; 39, 809-812 .
    • Gendreizig S. et al. (2003) Covalent labeling of fusion proteins with chemical probes in living cells Chimia; 57, 181-183 .
    • Juillerat A. et al. (2003) Directed evolution of O6-alkylguanine-DNA alkyltransferase for efficient labeling of fusion proteins with small molecules in vivo Chem Biol; 10, 313-317 .
    • Gendreizig, S. et al. (2003) Induced protein dimerizaton in vivo through covalent labeling J Am Chem Soc; 125, 14970-14971 . PubMedID: 14653715
    • Keppler A. et al. (2003) A general method for the covalent labeling of fusion proteins with small molecules in vivo Nat Biotechnol; 21, 86-89 .
    • Kindermann M. et al. (2003) Covalent and selective immobilization of fusion proteins J Am Chem Soc; 125, 7810-7811 . PubMedID: 12822993
    • George N. et al. (2004) Specific labeling of cell surface proteins with chemically diverse compounds J Am Chem Soc; 126, 8896-8897 . PubMedID: 15264811
    • Kindermann M. et al. (2004) Synthesis and characterization of bifunctional probes for the specific labeling of fusion proteins Bioorg Med Chem Lett; 14, 2725-2728 .
    • Huber W. et al. (2004) SPR-based interaction studies with small molecular weight ligands using hAGT fusion proteins Anal Biochem; 333, 280-288 . PubMedID: 15450803
    • Keppler A. et al. (2004) Labeling of fusion proteins of O6-alkylguanine-DNA alkyltransferase with small molecules in vitro and in vivo Methods; 32, 437-444. PubMedID: 15003606
    • Keppler A. et al. (2004) Labeling of fusion proteins with synthetic fluorophores in live cells Proc Natl Acad Sci U S A; 101, 9955-9959.
    • La Clair, J.J. et al. (2004) Manipulation of carrier proteins in antibiotic biosynthesis Chem Biol; 11, 195-201 . PubMedID: 15123281
    • Dellagiacoma, C. et al. (2010) Targeted photoswitchable probe for nanoscopy of biological structures Chembiochem; PubMedID: 20540058, DOI: 10.1002/Cbic.201000189
    • Rhee S. G. et al. (2010) Methods for detection and measurement of hydrogen peroxide inside and outside of cells Mol Cell; 29 , 539-549 . PubMedID: 20526816
    • Hein B. et al. (2010) Stimulated emission depletion nanoscopy of living cells using SNAP-Tag fusion proteins Biophys J; 98 , 158-163 . PubMedID: 20074516
    • Alvarez-Curto J. et al. (2010) Ligand regulation of the quaternary organization of cell surface M3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogenous time-resolved FRET J Biol Chem; 285 , 23318-23330 . PubMedID: 20489201
    • Geissbuehler M. et al. (2010) Triplet imaging of oxygen consumption during the contraction of a single smooth muscle cell Biophys J; 98 , 339-349 . PubMedID: 22259112
    • Kampmeier, F. et al. (2010) Rapid optical imaging of EGF receptor expression with a single-chain antibody SNAP-tag fusion protein Eur J Nucl Med Mol Imaging; PubMedID: 20449589, DOI: 10.007/S00259-010-1482-5
    • Waichman S. et al. (2010) Functional Immobilization and Patterning of Proteins by an Enzymatic Transfer Reaction Anal Chem; 82 , 1478-1485 . PubMedID: 20092261
    • 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, 2. PubMedID: 20701592
    • Mosiewicz, K. A. et al. (2010) Phosphopantetheinyl Transferase-Catalyzed Formation of Bioactive Hydrogels for Tissue Engineering J Am Chem Soc; 132, 5972-5974 . PubMedID: 20373804
    • Campos, C. et al. (2010) Labeling cell structures and tracking cell lineage in zebrafish using SNAP-Tag Dev Dyn; 240 , 820-827. PubMedID: 21360787
    • Srikun, D. et al. (2010) Organelle-targetable fluorescent probes for imaging hydrogen peroxide in living cells via SNAP-tag protein labeling J Am Chem Soc; 132 , 4455-4465 . PubMedID: 20201528
    • Ciruela F. et al. (2010) Lighting up multiprotein complexes: lessons from GPCR oligomerization Trends Biotechnol; 28, 407-415 . PubMedID: 20542584
    • Kamiya M. and Johnsson K. (2010) Localizable and Highly Sensitive Calcium Indicator Based on a BODIPY Fluorophore Anal Chem; 82 , 6472-6479 . PubMedID: 20590099
    • Engin S. et al. (2010) Benzylguanine Thiol self-assembled monolayers for the immobilization of SNAP-tag proteins on microcontact-printed surface structures Langmuir; ASAP, PubMedID: 20369837
    • Maurel D. et al. (2010) Photoactivatable and photoconvertible fluorescent probes for protein labeling ACS Chem Biol; PubMedID: 20218675
    • Nicolle O. et al. (2010) Development of SNAP-tag-mediated live cell labeling as an alternative to GFP in Porphyromonas gingivalis FEMS�Immunol�Med Microbiol; 59 , 357-363 . PubMedID: 20482622
    • Ruggiu A. A. et al. (2010) Fura-2FF-based calcium indicator for protein labeling Org Biomol Chem; 8 , 3398-3401 . PubMedID: 20556282
    • Jongsma M.A., Litjens R. H. (2006) Self-assembling protein arrays on DNA chips by auto-labeling fusion proteins with a single DNA address Proteomics; 6, 2650-2655 . PubMedID: 16596705
    • Keppler A. et al. (2006) Fluorophores for live cell imaging of AGT fusion proteins across the visible spectrum Biotechniques; 41, 167-75 . PubMedID: 16925018
    • Prummer M. et al. (2006) Post-translational covalent labeling reveals heterogeneous mobility of individual G protein-coupled receptors in living cells Chembiochem; 7, 908-911 . PubMedID: 16607667
    • Meyer B.H. et al. (2006) Covalent labeling of cell-surface proteins for in vivo FRET studies FEBS Lett; 580, 1654-1658 . PubMedID: 16497304
    • Sielaff I. et al. (2006) Protein function microarrays based on self-immobilizing and self-labeling fusion proteins Chembiochem; 7, 194-202. PubMedID: 16342318
    • Heinis C. et al. (2006) Evolving the substrate specificity of O6 alkylguanine DNA alkyltransferase through loop insertion for applications in molecular imaging ACS Chem Biol; 1, 575-584. PubMedID: 17168553
    • Gronemeyer T. et al. (2006) Adding value to fusion proteins through covalent labeling Curr Opin Biotechnol; 16 , PubMedID: 15967656
    • Tirat A. et al. (2006) Evaluation of two novel tag-based labeling technologies for site-specific modification of proteins Int J Biol Macromol.; 39, 66-76. PubMedID: 16503347
    • Jacquier V. et al. (2006) Visualizing receptor trafficking in living Proc Natl Acad Sci U S A; 103, 14325-14330 . PubMedID: 16980412
    • Gronemeyer T. et al. (2006) Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling Prot Eng Des Sel; 19, 309-16 . PubMedID: 12725859
    • Krayl M. et al. (2006) Fluorescence-mediated analysis of mitochondrial preprotein import in vitro Anal Biochem; 335, 81-9. PubMedID: 16750157
    • 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 U S A; 103, 2138-43 . PubMedID: 16461466
    • Foltz D.R. et al. (2009) Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP Cell; 137 , 472-84 . PubMedID: 19410544
    • Milenkovic L. et al. (2009) Lateral transport of smoothened from the plasma membrane to the membrane of the cilium J Cell Biol; 187 , 365-374 . PubMedID: 19193035
    • Böhme I and Beck-Sickinger A. G. (2009) Illuminating the life of GPCRs Cell Commun Signal; 7 , 16 . PubMedID: 19602276
    • Tivari R. and Parang K. (2009) Protein conjugates of SH3-domain ligands and ATP- competitive inhibitors as bivalent inhibitors of protein kinases Chembiochem; 10, 2445 - 2448 . PubMedID: 19731277
    • Chattopadhaya S. et al. (2009) Expanding the chemical Biologist's tool kit: chemical labelling strategies and its applications Curr Med Chem; 16 , 4527-4543 . PubMedID: 19903152
    • Neugart F. et al. (2009) Detection of ligand-induced CNTF receptor dimers in living cells by fluorescence cross correlation spectroscopy Biochim Biophys Acta;  1788 , 1890-1900 . PubMedID: 19482006
    • Farr G. A. et al. (2009) Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells J Cell Biol; 186 , 269-282 . PubMedID: 19620635
    • Brun M.A. et al. (2009) Semisynthetic fluorescent sensor proteins based on self-labeling protein tags J Am Chem Soc; 131 , 5873-5784 . PubMedID: 19348459
    • Bannwarth et. al. (2009) Indo-1 Derivatives for local calcium sensing ACS Chem Biol; 4 , 179-190 . PubMedID: 19193035
    • Ahier A. et al. (2009) A new family of receptor tyrosine kinases with a venus flytrap binding domain in insects and other invertebrates activated by aminoacids PLoS One; 4, e5651 . PubMedID: 19461966
    • Eggeling C. et al. (2009) Direct observation of the nanoscale dynamics of membrane lipids in a living cell Nature; 457 , 1159-1163. PubMedID: 19098897
    • Sletten E. and Bertozzi C. (2009) Bioorthogonal Chemistry: Fishing for Selectivity in a Sea of Functionality Angew Chem Int Ed Eng; 48 , 6974-6998 . PubMedID: 19714693
    • Uano Y. and Matsuzaki K. (2009) Tag-probe labeling methods for live-cell imaging of membrane proteins Biochim Biophys Acta; 1788 , 2124-2131 . PubMedID: 19646952
    • Degorce F. et al. (2009) HTRF: A technology tailored for drug discovery - a review of theoretical aspects and recent applications Curr Chem Genomics;  3 , 22-32 . PubMedID: 20161833
    • Gautier A. et al. (2009) Selective cross-linking of interacting proteins using self-labeling tags J Am Chem Soc; 131, 17954-17962 . PubMedID: 19916541
    • Donovan C. et al. (2009) Characterization and subcellular localization of bacterial flotillin homologue Microbiology; 155 , 1786-1799 . PubMedID: 19383680
    • Cornish, V. W. (2009) Fluorescence in living systems: applications in chemical biology Wiley Encyc. of Chem. Biol. ; 2 , 28-38 .
    • Kapmeier F. et al. (2009) Site-Specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase Bioconjugate Chem; 23-Apr , PubMedID: 19388673
    • Gralle M. et al. (2009) Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers J Biol Chem; 284, 15016-15025 . PubMedID: 19336403
    • Stein V. and Hollfeder F. (2009) An efficient method to assemble linear DNA templates for in vitro screening and selection systems Nucleic Acids Res; 37, e122/1-e122/9 . PubMedID: 19617373
    • Hill Z. B. (2009) A chemical genetic method for generating bivalent inhibitors of protein kinases J Am Chem Soc; 131, 6686-6688 . PubMedID: 19391594
    • Johnsson K. (2009) Visualizing biochemical activities in living cells Nat Chem Biol; 5 , 63-65 . PubMedID: 19148167
    • Carroll C.W. et al. (2009) Centromere assembly requires the direct recognition of CENP-A nucleosomes by CENP-N Nat�Cell�Biol; 11 , 896-902 . PubMedID: 19543270
    • Samoshkin A. et al. (2009) Human condensin function is essential for centromeric chromatin assembly and proper sister kinetochore orientation PLoS One; 4 , e6831 . PubMedID: 19714251
    • Keppler A. et al. (2009) Chromophore-assisted laser inactivation of α- and γ-tubulin SNAP-tag fusion proteins inside living cells ACS Chem Biol; 4 , 127-138 . PubMedID: 19191588
    • Jansen L. et al (2007) Propagation of centromeric chromatin requires exit from mitosis J Cell Biol; 176, 795-805. PubMedID: 17339380
    • Lemercier, G. et al. (2007) Inducing and sensing protein-protein interactions in living cells by selective cross-linking Angew Chem Int Ed Eng; 4281-4284 . PubMedID: 17465435
    • O'Hare H.M. et al. (2007) Chemical probes shed light on protein function Curr Opin Struct Biol; 17 , 488-94 . PubMedID: 17851069
    • Böhme. et al. (2007) Tracking of human Y receptors in living cells- A fluorescence approach Peptides; 28, 226-234 . PubMedID: 17207557
    • Johnsson N. and Johnsson K. (2007) Chemical tools for biomolecular imaging ACS Chem Biol; 2 , 31-38 . PubMedID: 17243781
    • Stein, V. et al. (2007) A covalent chemical genotype-phenotype linkage for in vitro protein evolution Chembiochem; 8, 2191-4 . PubMedID: 17948318
    • Liu E and Bruner S. D. (2007) Rational manipulation of carrier-domain geometry in nonribosomal peptide synthetases Chembiochem; 8, 617 - 621 . PubMedID: 17335097
    • Zhou Z. et al. (2007) Genetically encoded short peptide tags for orthogonal protein labeling by Sfp and AcpS phosphopantetheinyl transferases ACS Chem Biol; 2, 337-346 . PubMedID: 17465518
    • Stenoien D. L. et al. (2007) Cellular trafficking of phospholamban and formation of functional sarcoplasmic reticulum during myocyte differentiation Am J Physiol Cell Physiol; 292 , C2084-C2094 . PubMedID: 17287364
    • Pick H. et al. (2007) Distribution plasticity of the human estrogen receptor alpha in live cells: distinct imaging of consecutively expressed receptors J Mol Biol; 14, 1213-1223. PubMedID: 17991486
    • Mottram L. F. et al. (2007) A Concise Synthesis of the Pennsylvania green fluorophore and labeling of intracellular targets with O6-Benzylguanine Derivatives Org Lett; 9, 3741-3744 . PubMedID: 17705395
    • Fururta, K. et al. (2008) Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Plk1 J Biol Chem; 283 , 36465-36473 . PubMedID: 18984586
    • Schulz C. and Köhn M. (2008) Simultaneous protein tagging in two colors Chem Biol; 15, PubMedID: 18291310
    • 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, 2641-2644 .
    • Erhardt, S. et al. (2008) Genome-wide analysis reveals a cell cycle-dependent mechanism controling centromere propagation J Cell Biol; 183 , 805-818 . PubMedID: 19047461
    • Mao S. et al. (2008) Optical lock-in detection of FRET using synthetic and genetically encoded optical switches Biophys J; 94, 4515-24 . PubMedID: 18281383
    • Southwell, A.L. et al. (2008) Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity J Neurosci; 28, 9013-20 . PubMedID: 18768695
    • Kropf M. et al. (2008) Subunit-specific surface mobility of differentially labeled AMPA receptor subunits Eur J Cell Biol; 87, 763-778 . PubMedID: 18547676
    • Chidley C. et al. (2008) A designed protein for the specific and covalent heteroconjugation of biomolecules Bioconjugate Chem; 19 , 1753-1756 . PubMedID: 18754573
    • 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, 561-7 . PubMedID: 18488035
    • Generosi J. et al. (2008) Photobleaching-free infrared near-field microscopy localizes molecules in neurons J Appl Physiol; 104, 106102-1/3.
    • Tomat, E. et al. (2008) Organelle-specific zinc detection using zinpyr-labeled fusion proteins in live cells J Am Chem Soc; 130 , PubMedID: 18973293
    • Gautier A. et al. (2008) An engineered protein tag for multiprotein labeling in living cells Chem Biol; 15, 128-136. PubMedID: 18291317
    • Iversen L. et al. (2008) Templated protein assembly on micro-contact-printed surface patterns. Use of the SNAP-tag protein functionality Langmuir; May 17, PubMedID: 18484753
    • Howland S.W. et al. (2008) Inducing efficient cross-priming using antigen-coated yeast particles J Immunother ; 31 , 607-19. PubMedID: 18600183
    • Gautier A. et al. (2008) AGT/SNAP-Tag: A versatile tag for covalent protein labeling from probes and tags to study biomolecular function Ed. Edited by Miller, L. W. ; 89-107 .
    • Sunbul M. et al. (2008) Enzyme catalyzed site-specific protein labeling and cell imaging with quantum dots Chem Commun; 5927-5929 . PubMedID: 19030541
    • Adams D. G. et al. (2008) Cellular Ser/Thr-kinase assays using generic peptide substrates Curr Chem Genomics; 1 , 54-64 . PubMedID: 20161828
    • Johnson K. (2008) SNAP-tag Technologies: Novel tools to study protein function NEB Expressions ; 3.3 , 1-3 .
    • McMurray, M.A. and Thorner, J. (2008) Septin stability and recycling during dynamic structural transitions in cell division and development Curr Biol; 18 , 1203-1208 . PubMedID: 18701287
    • Banala J. et al. (2008) Caged substrates for protein labeling and immobilization Chembiochem; 4, PubMedID: 18033718
    • Lin M.Z. and Wang L. (2008) Selective labeling of proteins with chemical probes in living cells Physiology; 23 , 131-141 . PubMedID: 18556466
    • Damoiseaux, R. et al (2002) Towards the generation of artificial O6-alkylguanine-DNA alkyltransferases: in vitro selection of antibodies with reactive cysteine residues Chembiochem; 3, 573-575 . PubMedID: 12325014
  • 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
Selected Publications by Application

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.

Single-Molecule Imaging

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.

Super-Resolution Imaging

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.

Pulse-Chase Analysis:

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.

Pull-Down Studies:

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.
  • Clone and express once, then use with a variety of substrates
  • Non-toxic to living cells
  • Wide selection of fluorescent substrates
  • Highly specific covalent labeling
  • Simultaneous dual labeling
Protein Labeling with SNAP-tag and CLIP-tag
The SNAP- (gold) or CLIP-tag (purple) is fused to the protein of interest (blue). Labeling occurs through covalent attachment to the tag, releasing either a guanine or a cytosine moiety.

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