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Volumn 19, Issue 30, 2013, Pages 5406-5413

SNAP-tag technology: A general introduction

Author keywords

CLIP tag; Fluorescence microscopy; In vivo imaging; Site specific labeling; SNAP tag

Indexed keywords

PROTEIN TAG; RECOMBINANT PROTEIN;

EID: 84881365783     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113199990514     Document Type: Review
Times cited : (30)

References (55)
  • 1
    • 0037225952 scopus 로고    scopus 로고
    • A general method for the covalent labeling of fusion proteins with small molecules in vivo
    • Keppler A, Gendreizig S, Gronemeyer T, et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat Biotechnol 2003; 21: 86-9.
    • (2003) Nat Biotechnol , vol.21 , pp. 86-89
    • Keppler, A.1    Gendreizig, S.2    Gronemeyer, T.3
  • 2
    • 33745712857 scopus 로고    scopus 로고
    • Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling
    • Gronemeyer T, Chidley C, Juillerat A, Heinis C, Johnsson K. Directed evolution of O6-alkylguanine-DNA alkyltransferase for applications in protein labeling. Protein Eng Des Sel 2006; 19: 309-16.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 309-316
    • Gronemeyer, T.1    Chidley, C.2    Juillerat, A.3    Heinis, C.4    Johnsson, K.5
  • 4
    • 66149167323 scopus 로고    scopus 로고
    • Site-specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase
    • Kampmeier F, Ribbert M, Nachreiner T, et al. Site-specific, covalent labeling of recombinant antibody fragments via fusion to an engineered version of 6-O-alkylguanine DNA alkyltransferase. Bioconjug Chem 2009; 20: 1010-5.
    • (2009) Bioconjug Chem , vol.20 , pp. 1010-1015
    • Kampmeier, F.1    Ribbert, M.2    Nachreiner, T.3
  • 5
    • 80052781568 scopus 로고    scopus 로고
    • Development of SNAP-tag fluorogenic probes for wash-free fluorescence imaging
    • Sun X, Zhang A, Baker B, et al. Development of SNAP-tag fluorogenic probes for wash-free fluorescence imaging. Chembiochem 2011; 12: 2217-26.
    • (2011) Chembiochem , vol.12 , pp. 2217-2226
    • Sun, X.1    Zhang, A.2    Baker, B.3
  • 6
    • 71749117935 scopus 로고    scopus 로고
    • Selective cross-linking of interacting proteins using self-labeling tags
    • Gautier A, Nakata E, Lukinavicius G, Tan KT, Johnsson K. Selective cross-linking of interacting proteins using self-labeling tags. J Am Chem Soc 2009; 131: 17954-62.
    • (2009) J Am Chem Soc , vol.131 , pp. 17954-17962
    • Gautier, A.1    Nakata, E.2    Lukinavicius, G.3    Tan, K.T.4    Johnsson, K.5
  • 7
    • 77950192252 scopus 로고    scopus 로고
    • Organelle-targetable fluorescent probes for imaging hydrogen peroxide in living cells via SNAP-Tag protein labeling
    • Srikun D, Albers AE, Nam CI, Iavarone AT, Chang CJ. Organelle-targetable fluorescent probes for imaging hydrogen peroxide in living cells via SNAP-Tag protein labeling. J Am Chem Soc 2010; 132: 4455-65.
    • (2010) J Am Chem Soc , vol.132 , pp. 4455-4465
    • Srikun, D.1    Albers, A.E.2    Nam, C.I.3    Iavarone, A.T.4    Chang, C.J.5
  • 8
    • 80053013758 scopus 로고    scopus 로고
    • Chemical tags for labeling proteins inside living cells
    • Jing C, Cornish VW. Chemical tags for labeling proteins inside living cells. Acc Chem Res 2011; 44: 784-92.
    • (2011) Acc Chem Res , vol.44 , pp. 784-792
    • Jing, C.1    Cornish, V.W.2
  • 9
    • 80052942421 scopus 로고    scopus 로고
    • Bioconjugation of CdSe/ZnS nanoparticles with SNAP tagged proteins
    • Petershans A, Wedlich D, Fruk L. Bioconjugation of CdSe/ZnS nanoparticles with SNAP tagged proteins. Chem Commun (Camb) 2011; 47: 10671-3.
    • (2011) Chem Commun (Camb) , vol.47 , pp. 10671-10673
    • Petershans, A.1    Wedlich, D.2    Fruk, L.3
  • 10
    • 79959243915 scopus 로고    scopus 로고
    • Directed covalent immobilization of fluorescently labeled cytokines
    • Recker T, Haamann D, Schmitt A, et al. Directed covalent immobilization of fluorescently labeled cytokines. Bioconjug Chem 2011; 22: 1210-20.
    • (2011) Bioconjug Chem , vol.22 , pp. 1210-1220
    • Recker, T.1    Haamann, D.2    Schmitt, A.3
  • 11
    • 79952113111 scopus 로고    scopus 로고
    • Rapid optical imaging of EGF receptor expression with a single-chain antibody SNAP-tag fusion protein
    • Kampmeier F, Niesen J, Koers A, et al. Rapid optical imaging of EGF receptor expression with a single-chain antibody SNAP-tag fusion protein. Eur J Nucl Med Mol Imaging 2010; 37: 1926-34.
    • (2010) Eur J Nucl Med Mol Imaging , vol.37 , pp. 1926-1934
    • Kampmeier, F.1    Niesen, J.2    Koers, A.3
  • 12
    • 84867581008 scopus 로고    scopus 로고
    • In vivo imaging of immunotoxin treatment using Katushka-transfected A-431 cells in a murine xenograft tumour model
    • Pardo A, Stocker M, Kampmeier F, et al. In vivo imaging of immunotoxin treatment using Katushka-transfected A-431 cells in a murine xenograft tumour model. Cancer Immunol Immunother 2012; 61(10): 1617-26.
    • (2012) Cancer Immunol Immunother , vol.61 , Issue.10 , pp. 1617-1626
    • Pardo, A.1    Stocker, M.2    Kampmeier, F.3
  • 13
    • 84555177672 scopus 로고    scopus 로고
    • SNAP-tag technology mediates site specific conjugation of antibody fragments with a photosensitizer and improves target specific phototoxicity in tumor cells
    • Hussain AF, Kampmeier F, von Felbert V, et al. SNAP-tag technology mediates site specific conjugation of antibody fragments with a photosensitizer and improves target specific phototoxicity in tumor cells. Bioconjug Chem 2011; 22: 2487-95.
    • (2011) Bioconjug Chem , vol.22 , pp. 2487-2495
    • Hussain, A.F.1    Kampmeier, F.2    von Felbert, V.3
  • 14
    • 48049092838 scopus 로고    scopus 로고
    • HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis
    • Los GV, Encell LP, McDougall MG, et al. HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis. ACS Chem Biol 2008; 3: 373-82.
    • (2008) ACS Chem Biol , vol.3 , pp. 373-382
    • Los, G.V.1    Encell, L.P.2    McDougall, M.G.3
  • 15
    • 79956317609 scopus 로고    scopus 로고
    • Chemical tags: Applications in live cell fluorescence imaging
    • Wombacher R, Cornish VW. Chemical tags: applications in live cell fluorescence imaging. J Biophotonics 2011; 4: 391-402.
    • (2011) J Biophotonics , vol.4 , pp. 391-402
    • Wombacher, R.1    Cornish, V.W.2
  • 16
    • 77955840000 scopus 로고    scopus 로고
    • Selective covalent labeling of tag-fused GPCR proteins on live cell surface with a synthetic probe for their functional analysis
    • Nonaka H, Fujishima SH, Uchinomiya SH, Ojida A, Hamachi I. Selective covalent labeling of tag-fused GPCR proteins on live cell surface with a synthetic probe for their functional analysis. J Am Chem Soc 2010; 132: 9301-9.
    • (2010) J Am Chem Soc , vol.132 , pp. 9301-9309
    • Nonaka, H.1    Fujishima, S.H.2    Uchinomiya, S.H.3    Ojida, A.4    Hamachi, I.5
  • 18
    • 77955058619 scopus 로고    scopus 로고
    • Lighting up multiprotein complexes: Lessons from GPCR oligomerization
    • Ciruela F, Vilardaga JP, Fernandez-Duenas V. Lighting up multiprotein complexes: lessons from GPCR oligomerization. Trends Biotechnol 2010; 28: 407-15.
    • (2010) Trends Biotechnol , vol.28 , pp. 407-415
    • Ciruela, F.1    Vilardaga, J.P.2    Fernandez-Duenas, V.3
  • 19
    • 80054769493 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to G protein-coupled receptor oligomerization
    • Comps-Agrar L, Maurel D, Rondard P, et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to G protein-coupled receptor oligomerization. Methods Mol Biol 2011; 756: 201-14.
    • (2011) Methods Mol Biol , vol.756 , pp. 201-214
    • Comps-Agrar, L.1    Maurel, D.2    Rondard, P.3
  • 20
    • 39149145486 scopus 로고    scopus 로고
    • An engineered protein tag for multiprotein labeling in living cells
    • Gautier A, Juillerat A, Heinis C, et al. An engineered protein tag for multiprotein labeling in living cells. Chem Biol 2008; 15: 128-36.
    • (2008) Chem Biol , vol.15 , pp. 128-136
    • Gautier, A.1    Juillerat, A.2    Heinis, C.3
  • 21
    • 74049144192 scopus 로고    scopus 로고
    • Stimulated emission depletion nanoscopy of living cells using SNAP-tag fusion proteins
    • Hein B, Willig KI, Wurm CA, et al. Stimulated emission depletion nanoscopy of living cells using SNAP-tag fusion proteins. Biophys J 2010; 98: 158-63.
    • (2010) Biophys J , vol.98 , pp. 158-163
    • Hein, B.1    Willig, K.I.2    Wurm, C.A.3
  • 22
    • 84862262901 scopus 로고    scopus 로고
    • SNAP-tag Based Proteomics Approach for the Study of the Retrograde Route
    • Shi G, Azoulay M, Dingli F, et al. SNAP-tag Based Proteomics Approach for the Study of the Retrograde Route. Traffic 2012; 13: 914-25.
    • (2012) Traffic , vol.13 , pp. 914-925
    • Shi, G.1    Azoulay, M.2    Dingli, F.3
  • 23
    • 79960666968 scopus 로고    scopus 로고
    • A SNAP-tagged derivative of HIV-1--a versatile tool to study virus-cell interactions
    • Eckhardt M, Anders M, Muranyi W, et al. A SNAP-tagged derivative of HIV-1--a versatile tool to study virus-cell interactions. PLoS One 2011; 6: e22007.
    • (2011) PLoS One , vol.6
    • Eckhardt, M.1    Anders, M.2    Muranyi, W.3
  • 24
    • 84863040728 scopus 로고    scopus 로고
    • Sensitive Detection of Intracellular Sumoylation via SNAP Tag-Mediated Translation and RNA Polymerase-Based Amplification
    • Yang Y, Zhang C-y. Sensitive Detection of Intracellular Sumoylation via SNAP Tag-Mediated Translation and RNA Polymerase-Based Amplification. Anal Chem 2012; 84: 1229-34.
    • (2012) Anal Chem , vol.84 , pp. 1229-1234
    • Yang, Y.1    Zhang, C.-Y.2
  • 25
    • 44449096254 scopus 로고    scopus 로고
    • Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: Application to GPCR oligomerization
    • Maurel D, Comps-Agrar L, Brock C, et al. Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization. Nat Methods 2008; 5: 561-7.
    • (2008) Nat Methods , vol.5 , pp. 561-567
    • Maurel, D.1    Comps-Agrar, L.2    Brock, C.3
  • 26
    • 70149112322 scopus 로고    scopus 로고
    • Semisynthetic fluorescent sensor proteins based on self-labeling protein tags
    • Brun MA, Tan KT, Nakata E, Hinner MJ, Johnsson K. Semisynthetic fluorescent sensor proteins based on self-labeling protein tags. J Am Chem Soc 2009; 131: 5873-84.
    • (2009) J Am Chem Soc , vol.131 , pp. 5873-5884
    • Brun, M.A.1    Tan, K.T.2    Nakata, E.3    Hinner, M.J.4    Johnsson, K.5
  • 27
    • 85027931231 scopus 로고    scopus 로고
    • A yeast-based screen reveals that sulfasalazine inhibits tetrahydrobiopterin biosynthesis
    • Chidley C, Haruki H, Pedersen MG, Muller E, Johnsson K. A yeast-based screen reveals that sulfasalazine inhibits tetrahydrobiopterin biosynthesis. Nat Chem Biol 2011; 7: 375-83.
    • (2011) Nat Chem Biol , vol.7 , pp. 375-383
    • Chidley, C.1    Haruki, H.2    Pedersen, M.G.3    Muller, E.4    Johnsson, K.5
  • 28
    • 84861658335 scopus 로고    scopus 로고
    • Exploiting ligand-protein conjugates to monitor ligand-receptor interactions
    • Haruki H, Gonzalez MR, Johnsson K. Exploiting ligand-protein conjugates to monitor ligand-receptor interactions. PLoS One 2012; 7: e37598.
    • (2012) PLoS One , vol.7
    • Haruki, H.1    Gonzalez, M.R.2    Johnsson, K.3
  • 29
    • 78650121289 scopus 로고    scopus 로고
    • A fluorescent ligand-binding alternative using Tag-lite(R) technology
    • Zwier JM, Roux T, Cottet M, et al. A fluorescent ligand-binding alternative using Tag-lite(R) technology. J Biomol Screen 2010; 15: 1248-59.
    • (2010) J Biomol Screen , vol.15 , pp. 1248-1259
    • Zwier, J.M.1    Roux, T.2    Cottet, M.3
  • 30
    • 77954917965 scopus 로고    scopus 로고
    • Ligand regulation of the quaternary organization of cell surface M3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET
    • Alvarez-Curto E, Ward RJ, Pediani JD, Milligan G. Ligand regulation of the quaternary organization of cell surface M3 muscarinic acetylcholine receptors analyzed by fluorescence resonance energy transfer (FRET) imaging and homogeneous time-resolved FRET. J Biol Chem 2010; 285: 23318-30.
    • (2010) J Biol Chem , vol.285 , pp. 23318-23330
    • Alvarez-Curto, E.1    Ward, R.J.2    Pediani, J.D.3    Milligan, G.4
  • 31
    • 79951963422 scopus 로고    scopus 로고
    • Ligand-induced internalization of the orexin OX(1) and cannabinoid CB(1) receptors assessed via N-terminal SNAP and CLIP-tagging
    • Ward RJ, Pediani JD, Milligan G. Ligand-induced internalization of the orexin OX(1) and cannabinoid CB(1) receptors assessed via N-terminal SNAP and CLIP-tagging. Br J Pharmacol 2011; 162: 1439-52.
    • (2011) Br J Pharmacol , vol.162 , pp. 1439-1452
    • Ward, R.J.1    Pediani, J.D.2    Milligan, G.3
  • 32
    • 79955419149 scopus 로고    scopus 로고
    • Real-time measurements of protein dynamics using fluorescence activation-coupled protein labeling method
    • Komatsu T, Johnsson K, Okuno H, et al. Real-time measurements of protein dynamics using fluorescence activation-coupled protein labeling method. J Am Chem Soc 2011; 133: 6745-51.
    • (2011) J Am Chem Soc , vol.133 , pp. 6745-6751
    • Komatsu, T.1    Johnsson, K.2    Okuno, H.3
  • 33
    • 80051683944 scopus 로고    scopus 로고
    • One-and two-photon live cell imaging using a mutant SNAP-Tag protein and its FRET substrate pairs
    • Zhang CJ, Li L, Chen GY, Xu QH, Yao SQ. One-and two-photon live cell imaging using a mutant SNAP-Tag protein and its FRET substrate pairs. Org Lett 2011; 13: 4160-3.
    • (2011) Org Lett , vol.13 , pp. 4160-4163
    • Zhang, C.J.1    Li, L.2    Chen, G.Y.3    Xu, Q.H.4    Yao, S.Q.5
  • 34
    • 84866488153 scopus 로고    scopus 로고
    • Development of a split SNAP-tag protein complementation assay for visualization of protein-protein interactions in living cells
    • Mie M, Naoki T, Uchida K, Kobatake E. Development of a split SNAP-tag protein complementation assay for visualization of protein-protein interactions in living cells. Analyst 2012; 137: 4760-5.
    • (2012) Analyst , vol.137 , pp. 4760-4765
    • Mie, M.1    Naoki, T.2    Uchida, K.3    Kobatake, E.4
  • 35
    • 33644808569 scopus 로고    scopus 로고
    • SNAP-tag mediated live cell labeling as an alternative to GFP in anaerobic organisms
    • Regoes A, Hehl AB. SNAP-tag mediated live cell labeling as an alternative to GFP in anaerobic organisms. Biotechniques 2005; 39: 809-810+812.
    • (2005) Biotechniques , vol.39
    • Regoes, A.1    Hehl, A.B.2
  • 36
    • 0034035538 scopus 로고    scopus 로고
    • Stage-specific expression and targeting of cyst wall protein-green fluorescent protein chimeras in Giardia
    • Hehl AB, Marti M, Kohler P. Stage-specific expression and targeting of cyst wall protein-green fluorescent protein chimeras in Giardia. Mol Biol Cell 2000; 11: 1789-800.
    • (2000) Mol Biol Cell , vol.11 , pp. 1789-1800
    • Hehl, A.B.1    Marti, M.2    Kohler, P.3
  • 37
    • 0035007851 scopus 로고    scopus 로고
    • Assessment of GFP fluorescence in cells of Streptococcus gordonii under conditions of low pH and low oxygen concentration
    • Hansen MC, Palmer RJ, Jr., Udsen C, White DC, Molin S. Assessment of GFP fluorescence in cells of Streptococcus gordonii under conditions of low pH and low oxygen concentration. Microbiology 2001; 147: 1383-91.
    • (2001) Microbiology , vol.147 , pp. 1383-1391
    • Hansen, M.C.1    Palmer Jr., R.J.2    Udsen, C.3    White, D.C.4    Molin, S.5
  • 38
    • 77954648994 scopus 로고    scopus 로고
    • Development of SNAP-tag-mediated live cell labeling as an alternative to GFP in Porphyromonas gingivalis
    • Nicolle O, Rouillon A, Guyodo H, et al. Development of SNAP-tag-mediated live cell labeling as an alternative to GFP in Porphyromonas gingivalis. FEMS Immunol Med Microbiol 2010; 59: 357-63.
    • (2010) FEMS Immunol Med Microbiol , vol.59 , pp. 357-363
    • Nicolle, O.1    Rouillon, A.2    Guyodo, H.3
  • 39
    • 0033639092 scopus 로고    scopus 로고
    • Development of a noninvasive reporter system for gene expression in Porphyromonas gingivalis
    • Liu Y, Abaibou H, Fletcher HM. Development of a noninvasive reporter system for gene expression in Porphyromonas gingivalis. Plasmid 2000; 44: 250-61.
    • (2000) Plasmid , vol.44 , pp. 250-261
    • Liu, Y.1    Abaibou, H.2    Fletcher, H.M.3
  • 40
    • 79952677694 scopus 로고    scopus 로고
    • Labelling cell structures and tracking cell lineage in zebrafish using SNAP-tag
    • Campos C, Kamiya M, Banala S, Johnsson K, Gonzalez-Gaitan M. Labelling cell structures and tracking cell lineage in zebrafish using SNAP-tag. Dev Dyn 2011; 240: 820-7.
    • (2011) Dev Dyn , vol.240 , pp. 820-827
    • Campos, C.1    Kamiya, M.2    Banala, S.3    Johnsson, K.4    Gonzalez-Gaitan, M.5
  • 41
    • 84859136002 scopus 로고    scopus 로고
    • Near-infrared fluorescence imaging of mammalian cells and xenograft tumors with SNAP-tag
    • Gong H, Kovar JL, Baker B, et al. Near-infrared fluorescence imaging of mammalian cells and xenograft tumors with SNAP-tag. PLoS One 2012; 7: e34003.
    • (2012) PLoS One , vol.7
    • Gong, H.1    Kovar, J.L.2    Baker, B.3
  • 42
    • 79959501855 scopus 로고    scopus 로고
    • Measuring in vivo protein half-life
    • Bojkowska K, Santoni de Sio F, Barde I, et al. Measuring in vivo protein half-life. Chem Biol 2011; 18: 805-15.
    • (2011) Chem Biol , vol.18 , pp. 805-815
    • Bojkowska, K.1    de Sio, S.F.2    Barde, I.3
  • 43
    • 77958089655 scopus 로고    scopus 로고
    • Image-guided surgery using invisible near-infrared light: Fundamentals of clinical translation
    • Gioux S, Choi HS, Frangioni JV. Image-guided surgery using invisible near-infrared light: fundamentals of clinical translation. Mol Imaging 2010; 9: 237-55.
    • (2010) Mol Imaging , vol.9 , pp. 237-255
    • Gioux, S.1    Choi, H.S.2    Frangioni, J.V.3
  • 44
    • 84859708867 scopus 로고    scopus 로고
    • Photodynamic therapy: Current evidence and applications in dermatology
    • Lee Y, Baron ED. Photodynamic therapy: current evidence and applications in dermatology. Semin Cutan Med Surg 2011; 30: 199-209.
    • (2011) Semin Cutan Med Surg , vol.30 , pp. 199-209
    • Lee, Y.1    Baron, E.D.2
  • 45
    • 0346729780 scopus 로고    scopus 로고
    • Photosensitizer-antibody conjugates for detection and therapy of cancer
    • van Dongen GA, Visser GW, Vrouenraets MB. Photosensitizer-antibody conjugates for detection and therapy of cancer. Adv Drug Deliv Rev 2004; 56: 31-52.
    • (2004) Adv Drug Deliv Rev , vol.56 , pp. 31-52
    • van Dongen, G.A.1    Visser, G.W.2    Vrouenraets, M.B.3
  • 46
    • 71549165122 scopus 로고    scopus 로고
    • Amperometric Monitoring of the Neuropeptide "Substance-P" Level in Biological Fluids
    • Horak J, Enderle B, Bakirci H, Urban GA. Amperometric Monitoring of the Neuropeptide "Substance-P" Level in Biological Fluids. Procedia Chemistry 2009: 1275-8.
    • (2009) Procedia Chemistry , pp. 1275-1278
    • Horak, J.1    Enderle, B.2    Bakirci, H.3    Urban, G.A.4
  • 47
    • 78349296066 scopus 로고    scopus 로고
    • The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins
    • Aliprandi M, Sparacio E, Pivetta F, et al. The availability of a recombinant anti-SNAP antibody in VHH format amplifies the application flexibility of SNAP-tagged proteins. J Biomed Biotechnol 2010; 2010: 658954.
    • (2010) J Biomed Biotechnol , pp. 658954
    • Aliprandi, M.1    Sparacio, E.2    Pivetta, F.3
  • 48
    • 80755125455 scopus 로고    scopus 로고
    • Microspot-based ELISA in microfluidics: Chemiluminescence and colorimetry detection using integrated thin-film hydrogenated amorphous silicon photodiodes
    • Novo P, Franca Prazeres DM, Chu V, Conde JP. Microspot-based ELISA in microfluidics: chemiluminescence and colorimetry detection using integrated thin-film hydrogenated amorphous silicon photodiodes. Lab Chip 2011; 11: 4063-71.
    • (2011) Lab Chip , vol.11 , pp. 4063-4071
    • Novo, P.1    Franca, P.D.M.2    Chu, V.3    Conde, J.P.4
  • 49
    • 46949095594 scopus 로고    scopus 로고
    • Templated protein assembly on micro-contact-printed surface patterns. Use of the SNAP-tag protein functionality
    • Iversen L, Cherouati N, Berthing T, Stamou D, Martinez KL. Templated protein assembly on micro-contact-printed surface patterns. Use of the SNAP-tag protein functionality. Langmuir 2008; 24: 6375-81.
    • (2008) Langmuir , vol.24 , pp. 6375-6381
    • Iversen, L.1    Cherouati, N.2    Berthing, T.3    Stamou, D.4    Martinez, K.L.5
  • 50
    • 84874431905 scopus 로고    scopus 로고
    • A monoclonal antibody for the detection of SNAP/CLIP-tagged proteins
    • 10.1016/j.imlet.2012.10.007
    • Puettmann C, Kolberg K, Hagen S, et al. A monoclonal antibody for the detection of SNAP/CLIP-tagged proteins. Immunol Lett 2012; 10.1016/j.imlet.2012.10.007.
    • (2012) Immunol Lett
    • Puettmann, C.1    Kolberg, K.2    Hagen, S.3
  • 51
    • 38849128296 scopus 로고    scopus 로고
    • A covalent chemical genotype-phenotype linkage for in vitro protein evolution
    • Stein V, Sielaff I, Johnsson K, Hollfelder F. A covalent chemical genotype-phenotype linkage for in vitro protein evolution. Chembiochem 2007; 8: 2191-4.
    • (2007) Chembiochem , vol.8 , pp. 2191-2194
    • Stein, V.1    Sielaff, I.2    Johnsson, K.3    Hollfelder, F.4
  • 52
    • 80052756136 scopus 로고    scopus 로고
    • SNAP dendrimers: Multivalent protein display on dendrimer-like DNA for directed evolution
    • Kaltenbach M, Stein V, Hollfelder F. SNAP dendrimers: multivalent protein display on dendrimer-like DNA for directed evolution. Chembiochem 2011; 12: 2208-16.
    • (2011) Chembiochem , vol.12 , pp. 2208-2216
    • Kaltenbach, M.1    Stein, V.2    Hollfelder, F.3
  • 53
    • 77957307977 scopus 로고    scopus 로고
    • Ground and excited state reactions of new red fluorescent dyes with the DNA base guanosine
    • Nord S, Sauer M, Arden-Jacob J, et al. Ground and excited state reactions of new red fluorescent dyes with the DNA base guanosine. J. Fluoresc. 1997; 7: 15-18.
    • (1997) J. Fluoresc , vol.7 , pp. 15-18
    • Nord, S.1    Sauer, M.2    Arden-Jacob, J.3
  • 54
    • 77957320956 scopus 로고    scopus 로고
    • Quenched substrates for live-cell labeling of SNAP-tagged fusion proteins with improved fluorescent background
    • Stohr K, Siegberg D, Ehrhard T, et al. Quenched substrates for live-cell labeling of SNAP-tagged fusion proteins with improved fluorescent background. Anal Chem 2010; 82: 8186-93.
    • (2010) Anal Chem , vol.82 , pp. 8186-8193
    • Stohr, K.1    Siegberg, D.2    Ehrhard, T.3
  • 55
    • 84858668201 scopus 로고    scopus 로고
    • Releasable SNAP-tag probes for studying endocytosis and recycling
    • Cole NB, Donaldson JG. Releasable SNAP-tag probes for studying endocytosis and recycling. ACS Chem Biol 2012; 7: 464-9.
    • (2012) ACS Chem Biol , vol.7 , pp. 464-469
    • Cole, N.B.1    Donaldson, J.G.2


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