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Volumn 13, Issue 3, 2002, Pages 131-142

Automated high-throughput purification of 6xHis-tagged proteins

Author keywords

Automation; High throughput; His tag; Immobilized metal affinity chromatography (IMAC); Ni NTA

Indexed keywords


EID: 84867517334     PISSN: 15240215     EISSN: 19434731     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (42)
  • 1
    • 0035313732 scopus 로고    scopus 로고
    • Protein and antibody arrays and their medical applications
    • Cahill D. Protein and antibody arrays and their medical applications. J Immunol Methods 2001;250:81-91.
    • (2001) J Immunol Methods , vol.250 , pp. 81-91
    • Cahill, D.1
  • 2
    • 0035477627 scopus 로고    scopus 로고
    • Screening for soluble expression of recombinant proteins in a 96-well format
    • Knaust RKC, Nordlund P. Screening for soluble expression of recombinant proteins in a 96-well format. Anal Biochem 2001;297:79-85.
    • (2001) Anal Biochem , vol.297 , pp. 79-85
    • Knaust, R.K.C.1    Nordlund, P.2
  • 3
    • 0034629284 scopus 로고    scopus 로고
    • Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing
    • Pizza M, Scarlato V, Masignani V, et al. Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing. Science 2000;287: 1816-1820.
    • (2000) Science , vol.287 , pp. 1816-1820
    • Pizza, M.1    Scarlato, V.2    Masignani, V.3
  • 4
    • 0343526348 scopus 로고    scopus 로고
    • High-throughput protein expression of cDNA products as a tool in functional genomics
    • Larsson M, Gräslund S, Yuan L, et al. High-throughput protein expression of cDNA products as a tool in functional genomics. J Biotechnol 2000;80:143-157.
    • (2000) J Biotechnol , vol.80 , pp. 143-157
    • Larsson, M.1    Gräslund, S.2    Yuan, L.3
  • 6
    • 84867495321 scopus 로고    scopus 로고
    • The Protein Structure Factory
    • The Protein Structure Factory (http://www.rzpd.de/psf/).
  • 7
    • 0033757822 scopus 로고    scopus 로고
    • An overview of structural genomics
    • Burley S. An overview of structural genomics. Nat Struct Biol (Suppl) 2000;7:932-934.
    • (2000) Nat Struct Biol (Suppl) , vol.7 , pp. 932-934
    • Burley, S.1
  • 9
    • 0034990508 scopus 로고    scopus 로고
    • A structural genomics approach to the study of quorum sensing: Crystal structures of three LuxS orthologs
    • Lewis, HA, Furlong EB, Laubert B, et al. A structural genomics approach to the study of quorum sensing: Crystal structures of three LuxS orthologs. Structure 2001;9:527-537.
    • (2001) Structure , vol.9 , pp. 527-537
    • Lewis, H.A.1    Furlong, E.B.2    Laubert, B.3
  • 10
    • 0037022657 scopus 로고    scopus 로고
    • Proteome-scale purification of human proteins from bacteria
    • Braun P, Hu Y, Shen B, et al. Proteome-scale purification of human proteins from bacteria. Proc Natl Acad Sci USA 2002;99:2654-2659.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 2654-2659
    • Braun, P.1    Hu, Y.2    Shen, B.3
  • 12
    • 0033847231 scopus 로고    scopus 로고
    • A microarray enzyme-based immunosorbent assay for autoimmune diagnostics
    • Joos TA, Schrenk M, Höpfl P, et al. A microarray enzyme-based immunosorbent assay for autoimmune diagnostics. Electrophoresis 2000;21(13):2641-2650.
    • (2000) Electrophoresis , vol.21 , Issue.13 , pp. 2641-2650
    • Joos, T.A.1    Schrenk, M.2    Höpfl, P.3
  • 13
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeth G, Schreiber SL. Printing proteins as microarrays for high-throughput function determination. Science 2000;289:1760-1763.
    • (2000) Science , vol.289 , pp. 1760-1763
    • Macbeth, G.1    Schreiber, S.L.2
  • 14
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu, H., Bilgin, M., Bangham, R., et al. Global analysis of protein activities using proteome chips. Science 2001;293:2101-2105.
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3
  • 15
    • 0033624216 scopus 로고    scopus 로고
    • Automated purification of His6-tagged proteins allows exhaustive screening of libraries generated by random mutagenesis
    • Lanio T, Jeltsch A, Pingoud A. Automated purification of His6-tagged proteins allows exhaustive screening of libraries generated by random mutagenesis. Biotechniques 2000;29:338-342.
    • (2000) Biotechniques , vol.29 , pp. 338-342
    • Lanio, T.1    Jeltsch, A.2    Pingoud, A.3
  • 16
    • 0029964397 scopus 로고    scopus 로고
    • Use of a 96-well format for the affinity purification of maltose-binding protein (MBP) fusion proteins
    • Felleisen R, Zimmermann V, Gottstein B, Müller N. Use of a 96-well format for the affinity purification of maltose-binding protein (MBP) fusion proteins. Biotechniques 1996;20:616-620.
    • (1996) Biotechniques , vol.20 , pp. 616-620
    • Felleisen, R.1    Zimmermann, V.2    Gottstein, B.3    Müller, N.4
  • 17
    • 84867502762 scopus 로고    scopus 로고
    • Rapid screening of multiple clones for GST fusion protein expression
    • Amersham Pharmacia Biotech
    • Bell PA, Dunst RW, Ridnour H. Rapid screening of multiple clones for GST fusion protein expression. Life Scie News 1 (Amersham Pharmacia Biotech), 1998;1-3.
    • (1998) Life Scie News , vol.1 , pp. 1-3
    • Bell, P.A.1    Dunst, R.W.2    Ridnour, H.3
  • 18
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • Rigaut G, Shevchenko A, Rutz B, Wilm M, Mann M, Séraphin B. A generic protein purification method for protein complex characterization and proteome exploration. Nat Biotechnol 1999;17:1030-1032.
    • (1999) Nat Biotechnol , vol.17 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Séraphin, B.6
  • 19
    • 0037050026 scopus 로고    scopus 로고
    • Functional organization of the yeast proteome by systematic analysis of protein complexes
    • Gavin A-C, Bösche M, Krause R, et al. Functional organization of the yeast proteome by systematic analysis of protein complexes. Nature 2002;415:141-147.
    • (2002) Nature , vol.415 , pp. 141-147
    • Gavin, A.-C.1    Bösche, M.2    Krause, R.3
  • 20
    • 0030780364 scopus 로고    scopus 로고
    • Mutagenesis of a flexible loop in streptavidin leads to higher affinity to Strp-tag II peptide and improved performance in recombinant protein purification
    • Voss S, Skerra A. Mutagenesis of a flexible loop in streptavidin leads to higher affinity to Strp-tag II peptide and improved performance in recombinant protein purification. Protein Eng 1997;10:975-982.
    • (1997) Protein Eng , vol.10 , pp. 975-982
    • Voss, S.1    Skerra, A.2
  • 22
    • 0022340978 scopus 로고
    • Isolation of monoclonal antibodies specific for human c-myc protooncogene
    • Evans GI, Lewis GK, Ramsay G, Bishop JM. Isolation of monoclonal antibodies specific for human c-myc protooncogene. Mol Cell Biol 1985;12:3610-3616.
    • (1985) Mol Cell Biol , vol.12 , pp. 3610-3616
    • Evans, G.I.1    Lewis, G.K.2    Ramsay, G.3    Bishop, J.M.4
  • 23
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard BL, Chubet, RG, Vizard DL. Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. Biotechniques 1994;16:730-735.
    • (1994) Biotechniques , vol.16 , pp. 730-735
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 25
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine residues
    • Hochuli E, Dobeli H, Schacher A. New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine residues J Chromatogr 1987; 411:177-184.
    • (1987) J Chromatogr , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 27
    • 0034957669 scopus 로고    scopus 로고
    • High-throughput proteomics: Protein expression and purification in the postgenomic world
    • Lesley SA. High-throughput proteomics: Protein expression and purification in the postgenomic world. Protein Express Purif 2001;22:159-164.
    • (2001) Protein Express Purif , vol.22 , pp. 159-164
    • Lesley, S.A.1
  • 31
    • 33646791241 scopus 로고    scopus 로고
    • Interactions of 6xHistagged protein kinase A catalytic subunit examined using Ni-NTA Magnetic Agarose Beads
    • Zimmermann B, Herberg FW. Interactions of 6xHistagged protein kinase A catalytic subunit examined using Ni-NTA Magnetic Agarose Beads. QIAGEN News 1998;4:9-10.
    • (1998) QIAGEN News , vol.4 , pp. 9-10
    • Zimmermann, B.1    Herberg, F.W.2
  • 32
    • 34547571328 scopus 로고    scopus 로고
    • Justus-Liebig-University of Giessen, Germany. Rinnert and Beck compared Ni-NTA coated surfaces (HisSorb plates, QIAGEN) with polystyrene plates in diagnosis of schistosomiasis by immunoassay using 6xHis-tagged Schistosoma mansoni antigen Sm32. Application of infected serum samples from school children in Mali resulted in good ELISA signals in the case of antigen directly oriented on the Ni-NTA surface whereas the signals were in the range of the uninfected control sera when the antigen was randomly adsorbed to polystyrene
    • Rinnert T, Beck E. Personal communication. Justus-Liebig-University of Giessen, Germany. Rinnert and Beck compared Ni-NTA coated surfaces (HisSorb plates, QIAGEN) with polystyrene plates in diagnosis of schistosomiasis by immunoassay using 6xHis-tagged Schistosoma mansoni antigen Sm32. Application of infected serum samples from school children in Mali resulted in good ELISA signals in the case of antigen directly oriented on the Ni-NTA surface whereas the signals were in the range of the uninfected control sera when the antigen was randomly adsorbed to polystyrene.
    • Personal Communication
    • Rinnert, T.1    Beck, E.2
  • 33
    • 84867495323 scopus 로고    scopus 로고
    • Increased sensitivity in bioassays using improved Ni-NTA HisSorb plates and strips
    • Increased sensitivity in bioassays using improved Ni-NTA HisSorb plates and strips. QIAGEN News 2002;1:18-19. www.qiagen.com/literature/qiagennews/0102/1019238_QNews12002_18_19.pdf
    • (2002) QIAGEN News , vol.1 , pp. 18-19
  • 34
    • 84867507184 scopus 로고    scopus 로고
    • Establishing interaction studies using Ni-NTA Magnetic Agarose Beads
    • Steinert K, Emmerlich M, Ribbe J. Establishing interaction studies using Ni-NTA Magnetic Agarose Beads. QIAGEN News 2000;2:3-7.
    • (2000) QIAGEN News , vol.2 , pp. 3-7
    • Steinert, K.1    Emmerlich, M.2    Ribbe, J.3
  • 35
    • 0027496477 scopus 로고
    • Identification and functional analysis of chaperonin 10, the GroES homolog from yeast mitochondria
    • Rospert S, Glick BS, Jenö P, et al. Identification and functional analysis of chaperonin 10, the GroES homolog from yeast mitochondria. Proc Natl Acad Sci USA 1993;90:10967-10971.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10967-10971
    • Rospert, S.1    Glick, B.S.2    Jenö, P.3
  • 36
    • 0027772982 scopus 로고
    • Physiological inhibitors of the catalytic subunit of cAMP-dependent protein kinase: Effect of MgATP on protein-protein interactions
    • Herberg FW, Taylor SS. Physiological inhibitors of the catalytic subunit of cAMP-dependent protein kinase: Effect of MgATP on protein-protein interactions. Biochemistry 1993;32:14015-14021.
    • (1993) Biochemistry , vol.32 , pp. 14015-14021
    • Herberg, F.W.1    Taylor, S.S.2
  • 37
    • 0034667862 scopus 로고    scopus 로고
    • Electrospray mass spectra of three proprietary detergents
    • Yang-Boja E, DeFlippers F, Fales HM. Electrospray mass spectra of three proprietary detergents. Anal Biochem 2000;285:205-210.
    • (2000) Anal Biochem , vol.285 , pp. 205-210
    • Yang-Boja, E.1    Deflippers, F.2    Fales, H.M.3
  • 38
    • 0009770156 scopus 로고    scopus 로고
    • Significantly higher yields from automated protein purification procedures
    • Römer U, Blümer J, Schäfer F. Significantly higher yields from automated protein purification procedures. QIAGEN News 2001;5:12-15.
    • (2001) QIAGEN News , vol.5 , pp. 12-15
    • Römer, U.1    Blümer, J.2    Schäfer, F.3
  • 39
    • 0028864247 scopus 로고
    • PALEX, a dual-tag prokaryotic expression vector for the purification of full-length proteins
    • Panagiotidis CA, Silverstein SJ.PALEX, a dual-tag prokaryotic expression vector for the purification of full-length proteins. Gene 1995;164:45-47.
    • (1995) Gene , vol.164 , pp. 45-47
    • Panagiotidis, C.A.1    Silverstein, S.J.2
  • 40
    • 84867437703 scopus 로고    scopus 로고
    • High-throughput sample preparation for protein and peptide structural characterization
    • Sheer DG, Pitt AM. High-throughput sample preparation for protein and peptide structural characterization. J Biomol Tech 1999;10(1):21-25.
    • (1999) J Biomol Tech , vol.10 , Issue.1 , pp. 21-25
    • Sheer, D.G.1    Pitt, A.M.2
  • 42


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