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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
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    Publications related to Cellular Analysis
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  48. Southwell, A.L. et al. 2008. Intrabodies binding the proline-rich domains of mutant huntingtin increase its turnover and reduce neurotoxicity J. Neurosci. . 28, PubMedID: 18768695, DOI:
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  50. Erhardt, S. et al. 2008. Genome-wide analysis reveals a cell cycle-dependent mechanism controling centromere propagation J. Cell Biol.. 183 , PubMedID: 19047461, DOI:
  51. Mao S. et al. 2008. Optical lock-in detection of FRET using synthetic and genetically encoded optical switches Biophys. J. . 94, PubMedID: 18281383, DOI:
  52. 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:
  53. Schulz C. and Köhn M. 2008. Simultaneous protein tagging in two colors Chemistry & Biology . 15, PubMedID: 18291310, DOI:
  54. Fururta, K. et al. 2008. Diffusion and directed movement: in vitro motile properties of fission yeast kinesin-14 Plk1 J. Biol. Chem.  . 283 , PubMedID: 18984586, DOI:
  55. Iversen L. et al. 2008. Templated protein assembly on micro-contact-printed surface patterns. Use of the SNAP-tag protein functionality  Langumuir. May 17, PubMedID: 18484753, DOI:
  56. Gautier A. et al. 2008. An engineered protein tag for multiprotein labeling in living cells Chemistry & Biology . 15, PubMedID: 18291317, DOI:
  57. Tomat, E. et al. 2008. Organelle-specific zinc detection using zinpyr-labeled fusion proteins in live cells J. Am. Chem. Soc. . 130 , PubMedID: 18973293, DOI:
  58. O'Hare H.M. et al. 2007. Chemical probes shed light on protein function Curr. Opin. Struct. Biol. . 17 , PubMedID: 17851069, DOI:
  59. Lemercier, G. et al. 2007. Inducing and sensing protein-protein interactions in living cells by selective cross-linking Angew Chem. Int. Ed . , PubMedID: 17465435, DOI:
  60. Böhme. et al. 2007. Tracking of human Y receptors in living cells- A fluorescence approach Peptides. 28, PubMedID: 17207557, DOI:
  61. Johnson K. 2008. SNAP-tag Technologies: Novel tools to study protein function NEB Expressions . 3.3 , PubMedID: , DOI:
  62. Generosi J. et al. 2008. Photobleaching-free infrared near-field microscopy localizes molecules in neurons J. App. Phys. . 104, PubMedID: , DOI:
  63. Adams D. G. et al. 2008. Cellular Ser/Thr-kinase assays using generic peptide substrates Curr. Chem. Gen. . 1 , PubMedID: 20161828, DOI:
  64. Maurel D. et al. 2008. Cell-surface protein-protein interaction analysis with time-resolved FRET and SNAP-tag technologies: application to GPCR oligomerization Nature Methods . 5, PubMedID: 18488035, DOI:
  65. 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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  69. Liu E and Bruner S. D. 2007. Rational manipulation of carrier-domain geometry in nonribosomal peptide synthetases ChemBioChem. . 8, PubMedID: 17335097, DOI:
  70. Stein, V. et al. 2007. A covalent chemical genotype-phenotype linkage for in vitro protein evolution ChemBioChem. . 8, PubMedID: 17948318, DOI:
  71. Johnsson N. and Johnsson K. 2007. Chemical tools for biomolecular imaging ACS Chem. Biol. . 2 , PubMedID: 17243781, DOI:
  72. Lin M.Z. and Wang L. 2008. Selective labeling of proteins with chemical probes in living cells Physiology . 23 , PubMedID: 18556466, DOI:
  73. Banala J. et al. 2008. Caged substrates for protein labeling and immobilization Chembiochem . 4, PubMedID: 18033718, DOI:
  74. 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, PubMedID: 17705395, DOI:
  75. McMurray, M.A. and Thorner, J. 2008. Septin stability and recycling during dynamic structural transitions in cell division and development Current Biology . 18 , PubMedID: 18701287, DOI:
  76. Eckhardt, M. et al. 2011. A SNAP-tagged detivative of HIV-1 - A versatile tool to study virus-cell interactions PLoS One . , PubMedID: 21799764, DOI: 10.137/journal. P One .0022007
  77. 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, PubMedID: 12325014, DOI:
  78. Hoskins, A. et al. 2011. Ordered and dynamic assembly of single spliceoseoms Science . 331 , PubMedID: 21393538, DOI:
  79. Gronemeyer T. et al. 2006. Adding value to fusion proteins through covalent labeling Curr. Opin. Biotechn. . 16 , PubMedID: 15967656, DOI:
  80. Cravatt B.F. 2005. Live chemical reports from the cell surface Chem. Biol. . 12, PubMedID: 16183017, DOI:
  81. Meyer B.H. et al. 2006. Covalent labeling of cell-surface proteins for in vivo FRET studies FEBS Letters . 580, PubMedID: 16497304, DOI:
  82. Vivero-Pol L. et al. 2005. Multicolor imaging of cell surface proteins J. Am. Chem. Soc. . 127, PubMedID: 16159249, DOI:
  83. Gronemeyer T. et al. 2006. Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling Prot. Eng. Des. Sel. . 19, PubMedID: 12725859, DOI:
  84. Johnsson N. et al. 2005. Protein chemistry on the surface of living cells Chembiochem. . 6 , PubMedID: 15558647, DOI:
  85. Tirat A. et al. 2006. Evaluation of two novel tag-based labeling technologies for site-specific modification of proteins Int. J. Biol. Macromol.. 39, PubMedID: 16503347, DOI:
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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
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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