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Volumn 30, Issue 22, 2014, Pages 6629-6635

Sandwich antibody arrays using recombinant antibody-binding protein L

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CHEMICAL DETECTION; CYCLOADDITION; RECOMBINANT PROTEINS;

EID: 84902134852     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la500822w     Document Type: Article
Times cited : (7)

References (42)
  • 1
    • 34347346201 scopus 로고    scopus 로고
    • Protein immobilization strategies for protein biochips
    • Rusmini, F.; Zhong, Z.; Feijen, J. Protein immobilization strategies for protein biochips Biomacromolecules 2007, 8, 1775-1789
    • (2007) Biomacromolecules , vol.8 , pp. 1775-1789
    • Rusmini, F.1    Zhong, Z.2    Feijen, J.3
  • 2
    • 84890587427 scopus 로고    scopus 로고
    • Preparation of small-molecule microarrays by trans-cyclooctene tetrazine ligation and their application in the high-throughput screening of protein-protein interaction inhibitors of bromodomains
    • Zhang, C.-J.; Tan, C. Y. J.; Ge, J.; Na, Z.; Chen, G. Y. J.; Uttamchandani, M.; Sun, H.; Yao, S. Q. Preparation of small-molecule microarrays by trans-cyclooctene tetrazine ligation and their application in the high-throughput screening of protein-protein interaction inhibitors of bromodomains Angew. Chem., Int. Ed. 2013, 52, 14060-14064
    • (2013) Angew. Chem., Int. Ed. , vol.52 , pp. 14060-14064
    • Zhang, C.-J.1    Tan, C.Y.J.2    Ge, J.3    Na, Z.4    Chen, G.Y.J.5    Uttamchandani, M.6    Sun, H.7    Yao, S.Q.8
  • 3
    • 84891513768 scopus 로고    scopus 로고
    • DNA microarrays on ultraviolet-modified surfaces for speciation of bacteria
    • Liu, Y.; He, J.; Yang, K.-L. DNA microarrays on ultraviolet-modified surfaces for speciation of bacteria Anal. Biochem. 2014, 447, 156-161
    • (2014) Anal. Biochem. , vol.447 , pp. 156-161
    • Liu, Y.1    He, J.2    Yang, K.-L.3
  • 5
    • 80555127376 scopus 로고    scopus 로고
    • Miniaturized, microarray-based assays for chemical proteomic studies of protein function
    • Blackburn, J. M.; Shoko, A.; Beeton-Kempen, N. Miniaturized, microarray-based assays for chemical proteomic studies of protein function Methods Mol. Biol. 2012, 800, 133-162
    • (2012) Methods Mol. Biol. , vol.800 , pp. 133-162
    • Blackburn, J.M.1    Shoko, A.2    Beeton-Kempen, N.3
  • 6
    • 70849112219 scopus 로고    scopus 로고
    • Antibody-based sensors: Principles, problems and potential for detection of pathogens and associated toxins
    • Byrne, B.; Stack, E.; Gilmartin, N.; O'Kennedy, R. Antibody-based sensors: principles, problems and potential for detection of pathogens and associated toxins Sensors 2009, 9, 4407-4445
    • (2009) Sensors , vol.9 , pp. 4407-4445
    • Byrne, B.1    Stack, E.2    Gilmartin, N.3    O'Kennedy, R.4
  • 7
    • 0015116634 scopus 로고
    • Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G
    • Engvall, E.; Perlmann, P. Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G Immunochemistry 1971, 8, 871-874
    • (1971) Immunochemistry , vol.8 , pp. 871-874
    • Engvall, E.1    Perlmann, P.2
  • 8
    • 34547535401 scopus 로고    scopus 로고
    • Specifically immobilized aldo/keto reductase AKR1A1 shows a dramatic increase in activity relative to the randomly immobilized enzyme
    • Holland-Nell, K.; Beck-Sickinger, A. G. Specifically immobilized aldo/keto reductase AKR1A1 shows a dramatic increase in activity relative to the randomly immobilized enzyme ChemBioChem 2007, 8, 1071-1076
    • (2007) ChemBioChem , vol.8 , pp. 1071-1076
    • Holland-Nell, K.1    Beck-Sickinger, A.G.2
  • 9
    • 80053018151 scopus 로고    scopus 로고
    • Bioorthogonal chemistry for site-specific labeling and surface immobilization of proteins
    • Chen, Y.-X.; Triola, G.; Waldmann, H. Bioorthogonal chemistry for site-specific labeling and surface immobilization of proteins Acc. Chem. Res. 2011, 44, 762-773
    • (2011) Acc. Chem. Res. , vol.44 , pp. 762-773
    • Chen, Y.-X.1    Triola, G.2    Waldmann, H.3
  • 10
    • 79954591761 scopus 로고    scopus 로고
    • Significance of antibody orientation unraveled: Well-oriented antibodies recorded high binding affinity
    • Tajima, N.; Takai, M.; Ishihara, K. Significance of antibody orientation unraveled: well-oriented antibodies recorded high binding affinity Anal. Chem. 2011, 83, 1969-1976
    • (2011) Anal. Chem. , vol.83 , pp. 1969-1976
    • Tajima, N.1    Takai, M.2    Ishihara, K.3
  • 11
    • 31444456883 scopus 로고    scopus 로고
    • Fabrication of antibody arrays using thermally responsive elastin fusion proteins
    • Gao, D.; McBean, N.; Schultz, J. S.; Yan, Y.; Mulchandani, A.; Chen, W. Fabrication of antibody arrays using thermally responsive elastin fusion proteins J. Am. Chem. Soc. 2006, 128, 676-677
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 676-677
    • Gao, D.1    McBean, N.2    Schultz, J.S.3    Yan, Y.4    Mulchandani, A.5    Chen, W.6
  • 12
    • 61449147053 scopus 로고    scopus 로고
    • Photoactivable antibody binding protein: Site-selective and covalent coupling of antibody
    • Jung, Y.; Lee, J. M.; Kim, J.-w.; Yoon, J.; Cho, H.; Chung, B. H. Photoactivable antibody binding protein: Site-selective and covalent coupling of antibody Anal. Chem. 2009, 81, 936-942
    • (2009) Anal. Chem. , vol.81 , pp. 936-942
    • Jung, Y.1    Lee, J.M.2    Yoon, J.3    Cho, H.4    Chung, B.H.5
  • 13
    • 84862927415 scopus 로고    scopus 로고
    • Comparative study of random and oriented antibody immobilization as measured by dual polarization interferometry and surface plasmon resonance spectroscopy
    • Song, H. Y.; Zhou, X. D.; Hobley, J.; Su, X. D. Comparative study of random and oriented antibody immobilization as measured by dual polarization interferometry and surface plasmon resonance spectroscopy Langmuir 2012, 28, 997-1004
    • (2012) Langmuir , vol.28 , pp. 997-1004
    • Song, H.Y.1    Zhou, X.D.2    Hobley, J.3    Su, X.D.4
  • 14
    • 82955217276 scopus 로고    scopus 로고
    • A mussel adhesive protein fused with the BC domain of protein A is a functional linker material that efficiently immobilizes antibodies onto diverse surfaces
    • Kim, C. S.; Choi, Y. S.; Ko, W.; Seo, J. H.; Lee, J.; Cha, H. J. A mussel adhesive protein fused with the BC domain of protein A is a functional linker material that efficiently immobilizes antibodies onto diverse surfaces Adv. Funct. Mater. 2011, 21, 4101-4108
    • (2011) Adv. Funct. Mater. , vol.21 , pp. 4101-4108
    • Kim, C.S.1    Choi, Y.S.2    Ko, W.3    Seo, J.H.4    Lee, J.5    Cha, H.J.6
  • 15
    • 84879384935 scopus 로고    scopus 로고
    • Regioselective covalent immobilization of recombinant antibody-binding proteins A, G, and L for construction of antibody arrays
    • Seo, J.-s.; Lee, S.; Poulter, C. D. Regioselective covalent immobilization of recombinant antibody-binding proteins A, G, and L for construction of antibody arrays J. Am. Chem. Soc. 2013, 135, 8973-8980
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 8973-8980
    • Lee, S.1    Poulter, C.D.2
  • 16
    • 84894473464 scopus 로고    scopus 로고
    • Regio- and chemoselesctive immobilization of proteins on gold surfaces
    • Choi, S.-r.; Seo, J.-s.; Bohaty, R.; Poulter, C. D. Regio- and chemoselesctive immobilization of proteins on gold surfaces Bioconjugate Chem. 2014, 25, 269-275
    • (2014) Bioconjugate Chem. , vol.25 , pp. 269-275
    • Bohaty, R.1    Poulter, C.D.2
  • 17
    • 33746329936 scopus 로고    scopus 로고
    • Regio- and chemoselective covalent immobilization of proteins through unnatural amino acids
    • Gauchet, C.; Labadie, G. R.; Poulter, C. D. Regio- and chemoselective covalent immobilization of proteins through unnatural amino acids J. Am. Chem. Soc. 2006, 128, 9274-9275
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 9274-9275
    • Gauchet, C.1    Labadie, G.R.2    Poulter, C.D.3
  • 19
    • 36649023058 scopus 로고    scopus 로고
    • Farnesyl diphosphate analogues with ω-bioorthogonal azide and alkyne functional groups for protein farnesyl Transferase-catalyzed ligation reactions
    • Labadie, G. R.; Viswanathan, R.; Poulter, C. D. Farnesyl diphosphate analogues with ω-bioorthogonal azide and alkyne functional groups for protein farnesyl Transferase-catalyzed ligation reactions J. Org. Chem. 2007, 72, 9291-9297
    • (2007) J. Org. Chem. , vol.72 , pp. 9291-9297
    • Labadie, G.R.1    Viswanathan, R.2    Poulter, C.D.3
  • 20
    • 33745983268 scopus 로고    scopus 로고
    • Staphylococcus aureus protein A activates TNFR1 signaling through conserved IgG binding domains
    • Gomez, M. I.; O'Seaghdha, M.; Magargee, M.; Foster, T. J.; Prince, A. S. Staphylococcus aureus protein A activates TNFR1 signaling through conserved IgG binding domains J. Biol. Chem. 2006, 281, 20190-20196
    • (2006) J. Biol. Chem. , vol.281 , pp. 20190-20196
    • Gomez, M.I.1    O'Seaghdha, M.2    Magargee, M.3    Foster, T.J.4    Prince, A.S.5
  • 21
    • 0026056921 scopus 로고
    • Streptococcal protein G. Gene structure and protein binding properties
    • Sjöbring, U.; Björck, L.; Kastern, W. Streptococcal protein G. Gene structure and protein binding properties J. Biol. Chem. 1991, 266, 399-405
    • (1991) J. Biol. Chem. , vol.266 , pp. 399-405
    • Sjöbring, U.1    Björck, L.2    Kastern, W.3
  • 22
    • 0029131806 scopus 로고
    • Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins
    • Tashiro, M.; Montelione, G. T. Structures of bacterial immunoglobulin-binding domains and their complexes with immunoglobulins Curr. Opin. Struct. Biol. 1995, 5, 471-481
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 471-481
    • Tashiro, M.1    Montelione, G.T.2
  • 23
    • 0024308778 scopus 로고
    • Protein L: An immunoglobulin light chain binding bacterial protein. Characterization of binding and physiochemical properties
    • Äkerström, B.; Björck, L. Protein L: an immunoglobulin light chain binding bacterial protein. Characterization of binding and physiochemical properties J. Biol. Chem. 1989, 264, 19740-19746
    • (1989) J. Biol. Chem. , vol.264 , pp. 19740-19746
    • Äkerström, B.1    Björck, L.2
  • 25
    • 0022384947 scopus 로고
    • Protein G: A powerful tool for binding and detection of monoclonal and polyclonal antibodies
    • Äkerström, B.; Brodin, T.; Reis, K.; Björck, L. Protein G: a powerful tool for binding and detection of monoclonal and polyclonal antibodies J. Immunol. 1985, 135, 2589-2592
    • (1985) J. Immunol. , vol.135 , pp. 2589-2592
    • Äkerström, B.1    Brodin, T.2    Reis, K.3    Björck, L.4
  • 26
    • 0026788385 scopus 로고
    • Protein L from Peptostreptococcus magnus binds to the κ light chain variable domain
    • Nilson, B. H. K.; Solomon, A.; Björck, L.; Äkerström, B. Protein L from Peptostreptococcus magnus binds to the κ light chain variable domain J. Biol. Chem. 1992, 267, 2234-2239
    • (1992) J. Biol. Chem. , vol.267 , pp. 2234-2239
    • Nilson, B.H.K.1    Solomon, A.2    Björck, L.3    Äkerström, B.4
  • 27
    • 0026453116 scopus 로고
    • Protein LG: A hybrid molecule with unique immunoglobulin binding properties
    • Kihlberg, B. M.; Sjöbring, U.; Kastern, W.; Björck, L. Protein LG: a hybrid molecule with unique immunoglobulin binding properties J. Biol. Chem. 1992, 267, 25583-25588
    • (1992) J. Biol. Chem. , vol.267 , pp. 25583-25588
    • Kihlberg, B.M.1    Sjöbring, U.2    Kastern, W.3    Björck, L.4
  • 28
    • 1542267773 scopus 로고    scopus 로고
    • Contributions of amino acid side chains to the kinetics and thermodynamics of the bivalent binding of protein L to Ig κ light Chain
    • Svensson, H. G.; Wedemeyer, W. J.; Ekstrom, J. L.; Callender, D. R.; Kortemme, T.; Kim, D. E.; Sjöbring, U.; Baker, D. Contributions of amino acid side chains to the kinetics and thermodynamics of the bivalent binding of protein L to Ig κ light Chain Biochemistry 2004, 43, 2445-2457
    • (2004) Biochemistry , vol.43 , pp. 2445-2457
    • Svensson, H.G.1    Wedemeyer, W.J.2    Ekstrom, J.L.3    Callender, D.R.4    Kortemme, T.5    Kim, D.E.6    Sjöbring, U.7    Baker, D.8
  • 29
    • 2442435550 scopus 로고    scopus 로고
    • P54nrb associates with the 5′ splice site within large transcription/splicing complexes
    • Kameoka, S.; Duque, P.; Konarska, M. M. p54nrb associates with the 5′ splice site within large transcription/splicing complexes EMBO J. 2004, 23, 1782-1791
    • (2004) EMBO J. , vol.23 , pp. 1782-1791
    • Kameoka, S.1    Duque, P.2    Konarska, M.M.3
  • 31
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • Rostovtsev, V. V.; Green, L. G.; Fokin, V. V.; Sharpless, K. B. A stepwise Huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes Angew. Chem., Int. Ed. 2002, 41, 2596-2599
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 32
    • 41049109363 scopus 로고    scopus 로고
    • Copper-free azide-alkyne cycloadditions: New insights and perspectives
    • Lutz, J.-F. Copper-free azide-alkyne cycloadditions: new insights and perspectives Angew. Chem., Int. Ed. 2008, 47, 2182-2184
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 2182-2184
    • Lutz, J.-F.1
  • 34
    • 56449125290 scopus 로고    scopus 로고
    • Microarray-based study of carbohydrate-protein binding by gold nanoparticle probes
    • Gao, J.; Liu, D.; Wang, Z. Microarray-based study of carbohydrate-protein binding by gold nanoparticle probes Anal. Chem. 2008, 80, 8822-8827
    • (2008) Anal. Chem. , vol.80 , pp. 8822-8827
    • Gao, J.1    Liu, D.2    Wang, Z.3
  • 35
    • 84864420850 scopus 로고    scopus 로고
    • Epoxy-functionalized surfaces for microarray applications: Surface chemical analysis and fluorescence labeling of surface species
    • Funk, C.; Dietrich, P. M.; Gross, T.; Min, H.; Unger, W. E. S.; Weigel, W. Epoxy-functionalized surfaces for microarray applications: surface chemical analysis and fluorescence labeling of surface species Surf. Interface Anal. 2012, 44, 890-894
    • (2012) Surf. Interface Anal. , vol.44 , pp. 890-894
    • Funk, C.1    Dietrich, P.M.2    Gross, T.3    Min, H.4    Unger, W.E.S.5    Weigel, W.6
  • 36
    • 84860535513 scopus 로고    scopus 로고
    • High-resolution single-molecule recognition imaging of the molecular details of ricin-aptamer interaction
    • Wang, B.; Guo, C.; Zhang, M.; Park, B.; Xu, B. High-resolution single-molecule recognition imaging of the molecular details of ricin-aptamer interaction J. Phys. Chem. B 2012, 116, 5316-5322
    • (2012) J. Phys. Chem. B , vol.116 , pp. 5316-5322
    • Wang, B.1    Guo, C.2    Zhang, M.3    Park, B.4    Xu, B.5
  • 37
    • 3242774436 scopus 로고    scopus 로고
    • Imaging the binding ability of proteins immobilized on surfaces with different orientations by using liquid crystals
    • Luk, Y.-Y.; Tingey, M. L.; Dickson, K. A.; Raines, R. T.; Abbott, N. L. Imaging the binding ability of proteins immobilized on surfaces with different orientations by using liquid crystals J. Am. Chem. Soc. 2004, 126, 9024-9032
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 9024-9032
    • Luk, Y.-Y.1    Tingey, M.L.2    Dickson, K.A.3    Raines, R.T.4    Abbott, N.L.5
  • 38
    • 33746294443 scopus 로고    scopus 로고
    • Site-specific protein modification through CuI-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication
    • Lin, P.-C.; Ueng, S.-H.; Tseng, M.-C.; Ko, J.-L.; Huang, K.-T.; Yu, S.-C.; Adak, A. K.; Chen, Y.-J.; Lin, C.-c. Site-specific protein modification through CuI-catalyzed 1,2,3-triazole formation and its implementation in protein microarray fabrication Angew. Chem., Int. Ed. 2006, 45, 4286-4290
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 4286-4290
    • Lin, P.-C.1    Ueng, S.-H.2    Tseng, M.-C.3    Ko, J.-L.4    Huang, K.-T.5    Yu, S.-C.6    Adak, A.K.7    Chen, Y.-J.8
  • 40
    • 0021276488 scopus 로고
    • Purification and some properties of streptococcal protein G, a novel IgG-binding reagent
    • Bjöerck, L.; Kronvall, G. Purification and some properties of streptococcal protein G, a novel IgG-binding reagent J. Immunol. 1984, 133, 969-974
    • (1984) J. Immunol. , vol.133 , pp. 969-974
    • Bjöerck, L.1    Kronvall, G.2
  • 41
    • 0028926048 scopus 로고
    • Protein-protein interactions: Methods for detection and analysis
    • Phizicky, E. M.; Fields, S. Protein-protein interactions: methods for detection and analysis Microbiol. Rev. 1995, 59, 94-123
    • (1995) Microbiol. Rev. , vol.59 , pp. 94-123
    • Phizicky, E.M.1    Fields, S.2
  • 42
    • 0031003589 scopus 로고    scopus 로고
    • Effectiveness of a protein A for antibody immobilization for a fiber optic biosensor
    • Anderson, G. P.; Jacoby, M. A.; Ligler, F. S.; King, K. D. Effectiveness of a protein A for antibody immobilization for a fiber optic biosensor Biosens. Bioelectron. 1997, 12, 329-336
    • (1997) Biosens. Bioelectron. , vol.12 , pp. 329-336
    • Anderson, G.P.1    Jacoby, M.A.2    Ligler, F.S.3    King, K.D.4


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