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Volumn 498, Issue , 2009, Pages 157-172

Hexahistidine-tagged maltose-binding protein as a fusion partner for the production of soluble recombinant proteins in Escherichia coli

Author keywords

Fusion protein; Gateway cloning; Hexahistidine tag; His tag; His6MBP; Inclusion body; Maltose binding protein; MBP; Recombinational cloning; Solubility enhancer; TEV protease; Tobacco etch virus protease

Indexed keywords

ESCHERICHIA COLI; NICOTIANA TABACUM; TOBACCO ETCH VIRUS;

EID: 84934437421     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-196-3_11     Document Type: Article
Times cited : (30)

References (17)
  • 1
    • 4744359693 scopus 로고    scopus 로고
    • Turning protein crystallization from an art into a science
    • Chayen, N. E. (2004) Turning protein crystallization from an art into a science. Curr. Opin. Struct. Biol. 14, 577-583
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 577-583
    • Chayen, N.E.1
  • 2
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of its fusion partners
    • Kapust, R. B., and Waugh, D. S. (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of its fusion partners. Protein Sci. 8, 1668-1674
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 4
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • Hammarstrom, M., Hellgren, N., van Den Berg, S., Berglund, H., and Hard, T. (2002) Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11, 313-321
    • (2002) Protein Sci , vol.11 , pp. 313-321
    • Hammarstrom, M.1    Hellgren, N.2    van Den Berg, S.3    Berglund, H.4    Hard, T.5
  • 5
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: Identification of protein features that correlate with successful expression
    • doi:10.1186/1472-6750/4/32
    • Dyson, M. R., Shadbolt, P. S., Vincent, K. J., Perera, R. L., and McCafferty, J. (2004) Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotech. 4, 32 doi:10.1186/1472-6750/4/32
    • (2004) BMC Biotech , vol.4 , pp. 32
    • Dyson, M.R.1    Shadbolt, P.S.2    Vincent, K.J.3    Perera, R.L.4    McCafferty, J.5
  • 6
    • 23044514646 scopus 로고    scopus 로고
    • Construction of a set of gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli
    • Busso, D., Delagoutte-Busso, B., and Moras, D. (2005) Construction of a set of gateway-based destination vectors for high-throughput cloning and expression screening in Escherichia coli. Anal. Biochem. 343, 313-321
    • (2005) Anal. Biochem , vol.343 , pp. 313-321
    • Busso, D.1    Delagoutte-Busso, B.2    Moras, D.3
  • 8
    • 0033939720 scopus 로고    scopus 로고
    • Expression and purification of recombinant proteins by fusion to maltose-binding protein
    • Riggs, P. (2000) Expression and purification of recombinant proteins by fusion to maltose-binding protein. Mol. Biotechnol. 15, 51-63
    • (2000) Mol. Biotechnol , vol.15 , pp. 51-63
    • Riggs, P.1
  • 9
    • 0031214792 scopus 로고    scopus 로고
    • High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose binding protein double-affinity fusion system
    • Pryor, K. A., and Leiting, B. (1997) High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose binding protein double-affinity fusion system. Protein Expr. Purif. 10, 309-319
    • (1997) Protein Expr. Purif , vol.10 , pp. 309-319
    • Pryor, K.A.1    Leiting, B.2
  • 10
    • 0036362061 scopus 로고    scopus 로고
    • Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
    • Routzahn, K. M. and Waugh, D. S. (2002) Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins. J. Struct. Funct. Genomics 2, 83-92
    • (2002) J. Struct. Funct. Genomics , vol.2 , pp. 83-92
    • Routzahn, K.M.1    Waugh, D.S.2
  • 11
    • 28844475180 scopus 로고    scopus 로고
    • Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli
    • Nallamsetty, S., Austin, B. P., Penrose, K. J., and Waugh, D. S. (2005) Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli. Protein Sci. 14, 2964-2971
    • (2005) Protein Sci , vol.14 , pp. 2964-2971
    • Nallamsetty, S.1    Austin, B.P.2    Penrose, K.J.3    Waugh, D.S.4
  • 12
    • 33847247484 scopus 로고    scopus 로고
    • A generic method for the production of recombinant proteins in Escherichia coli using a dual hexahistidine-maltose-binding protein affinity tag
    • Tropea, J. E., Cherry, S., Nallamsetty, S., Bignon, C., and Waugh, D. S. (2007) A generic method for the production of recombinant proteins in Escherichia coli using a dual hexahistidine-maltose-binding protein affinity tag. Methods Mol. Biol. 363, 1-19
    • (2007) Methods Mol. Biol , vol.363 , pp. 1-19
    • Tropea, J.E.1    Cherry, S.2    Nallamsetty, S.3    Bignon, C.4    Waugh, D.S.5
  • 13
    • 0033939135 scopus 로고    scopus 로고
    • Controlled intracellular processing of fusion proteins by TEV protease
    • Kapust, R. B. and Waugh, D. S. (2000) Controlled intracellular processing of fusion proteins by TEV protease. Protein Expr. Purif. 19, 312-318
    • (2000) Protein Expr. Purif , vol.19 , pp. 312-318
    • Kapust, R.B.1    Waugh, D.S.2
  • 14
    • 0037208811 scopus 로고    scopus 로고
    • Maltose-binding protein as a solubility enhancer
    • Fox, J. D. and Waugh, D. S. (2003) Maltose-binding protein as a solubility enhancer. Methods Mol. Biol. 205, 99-117
    • (2003) Methods Mol. Biol , vol.205 , pp. 99-117
    • Fox, J.D.1    Waugh, D.S.2
  • 15
    • 0037468510 scopus 로고    scopus 로고
    • Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers
    • Fox, J. D., Routzahn, K. M., Bucher, M. H., and Waugh, D. S. (2003) Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers. FEBS Lett. 537, 53-57
    • (2003) FEBS Lett , vol.537 , pp. 53-57
    • Fox, J.D.1    Routzahn, K.M.2    Bucher, M.H.3    Waugh, D.S.4
  • 17
    • 0036087525 scopus 로고    scopus 로고
    • High-throughput screening of soluble recombinant proteins
    • (2002) High-throughput screening of soluble recombinant proteins. Protein Sci. 11, 1714-1719
    • (1714) Protein Sci , vol.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.