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Volumn 92, Issue 2, 2013, Pages 163-170

The Fh8 tag: A fusion partner for simple and cost-effective protein purification in Escherichia coli

Author keywords

Affinity tag; Calcium binding protein; Escherichia coli; Fh8 tag; Hydrophobic interaction chromatography

Indexed keywords

CALCIUM BINDING PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; SUPEROXIDE DISMUTASE;

EID: 84886288038     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.09.013     Document Type: Article
Times cited : (31)

References (35)
  • 1
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • DOI 10.1016/j.copbio.2006.06.003, PII S0958166906000875
    • D. Esposito, and D.K. Chatterjee Enhancement of soluble protein expression through the use of fusion tags Current Opinion in Biotechnology 17 2006 353 358 (Pubitemid 44163452)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 2
    • 0035542874 scopus 로고    scopus 로고
    • Applications of novel affinity cassette methods: Use of peptide fusion handles for the purification of recombinant proteins
    • DOI 10.1002/jmr.555
    • M.T.W. Hearn, and D. Acosta Applications of novel affinity cassette methods: use of peptide fusion handles for the purification of recombinant proteins Journal of Molecular Recognition 14 2001 323 369 (Pubitemid 34085332)
    • (2001) Journal of Molecular Recognition , vol.14 , Issue.6 , pp. 323-369
    • Hearn, M.T.W.1    Acosta, D.2
  • 3
    • 71549130731 scopus 로고    scopus 로고
    • Tagging for Protein Expression
    • Elsevier Inc.
    • A. Malhotra Tagging for Protein Expression Methods in Enzymology 2009 Elsevier Inc.
    • (2009) Methods in Enzymology
    • Malhotra, A.1
  • 5
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • DOI 10.1016/j.tibtech.2005.03.012, PII S0167779905000843
    • D.S. Waugh Making the most of affinity tags Trends in Biotechnology 23 2005 316 320 (Pubitemid 40726273)
    • (2005) Trends in Biotechnology , vol.23 , Issue.6 , pp. 316-320
    • Waugh, D.S.1
  • 6
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • D.B. Smith, and K.S. Johnson Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase Gene 67 1988 31 40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 7
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • C. Di Guan, P. Li, P.D. Riggs, and H. Inouye Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein Gene 15 67 1988 21 30
    • (1988) Gene , vol.15 , Issue.67 , pp. 21-30
    • Di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 8
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine-residues
    • E. Hochuli, H. Dobeli, and A. Schacher New metal chelate adsorbent selective for proteins and peptides containing neighboring histidine-residues Journal of Chromatography 411 1987 177 184
    • (1987) Journal of Chromatography , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 9
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • DOI 10.1016/j.pep.2005.12.002, PII S1046592805004262
    • J. Arnau, C. Lauritzen, G.E. Petersen, and J. Pedersen Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins Protein Expression and Purification 48 2006 1 13 (Pubitemid 43782626)
    • (2006) Protein Expression and Purification , vol.48 , Issue.1 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4
  • 10
    • 77049094645 scopus 로고    scopus 로고
    • Single-step affinity purification of recombinant proteins using the silica-binding Si-tag as a fusion partner
    • T. Ikeda, K. Ninomiya, R. Hirota, and A. Kuroda Single-step affinity purification of recombinant proteins using the silica-binding Si-tag as a fusion partner Protein Expression and Purification 71 2010 91 95
    • (2010) Protein Expression and Purification , vol.71 , pp. 91-95
    • Ikeda, T.1    Ninomiya, K.2    Hirota, R.3    Kuroda, A.4
  • 14
    • 77957297575 scopus 로고    scopus 로고
    • A heme fusion tag for protein affinity purification and quantification
    • W.B. Asher, and K.L. Bren A heme fusion tag for protein affinity purification and quantification Protein Science 19 2010 1830 1839
    • (2010) Protein Science , vol.19 , pp. 1830-1839
    • Asher, W.B.1    Bren, K.L.2
  • 15
    • 34447617851 scopus 로고    scopus 로고
    • basic-A novel purification tag for efficient protein recovery
    • DOI 10.1016/j.chroma.2007.05.091, PII S0021967307010096, 26th International Symposium on the Separation of Proteins, Peptides and Polynucleotides
    • M. Hedhammar, and S. Hober Z(basic) - A novel purification tag for efficient protein recovery Journal of Chromatography A 1161 2007 22 28 (Pubitemid 47088521)
    • (2007) Journal of Chromatography A , vol.1161 , Issue.1-2 , pp. 22-28
    • Hedhammar, M.1    Hober, S.2
  • 16
    • 75349113817 scopus 로고    scopus 로고
    • The Dock tag, an affinity tool for the purification of recombinant proteins, based on the interaction between dockerin and cohesin domains from Clostridium josui cellulosome
    • Y. Kamezaki, C. Enomoto, Y. Ishikawa, T. Koyama, S. Naya, T. Suzuki, and K. Sakka The Dock tag, an affinity tool for the purification of recombinant proteins, based on the interaction between dockerin and cohesin domains from Clostridium josui cellulosome Protein Expression and Purification 70 2010 23 31
    • (2010) Protein Expression and Purification , vol.70 , pp. 23-31
    • Kamezaki, Y.1    Enomoto, C.2    Ishikawa, Y.3    Koyama, T.4    Naya, S.5    Suzuki, T.6    Sakka, K.7
  • 17
    • 36448981741 scopus 로고    scopus 로고
    • A rapid and universal tandem-purification strategy for recombinant proteins
    • DOI 10.1110/ps.072894407
    • A.J. McCluskey, G.M.K. Poon, and J. Gariepy A rapid and universal tandem-purification strategy for recombinant proteins Protein Science 16 2007 2726 2732 (Pubitemid 350172759)
    • (2007) Protein Science , vol.16 , Issue.12 , pp. 2726-2732
    • Mccluskey, A.J.1    Poon, G.M.K.2    Gariepy, J.3
  • 21
    • 84880514065 scopus 로고    scopus 로고
    • The novel Fh8 and H fusion partners for soluble protein expression in Escherichia coli: A comparison with the traditional gene fusion technology
    • S.J. Costa, A. Almeida, A. Castro, L. Domingues, and H. Besir The novel Fh8 and H fusion partners for soluble protein expression in Escherichia coli: a comparison with the traditional gene fusion technology Applied Microbiology and Biotechnology 97 2013 6779 6791
    • (2013) Applied Microbiology and Biotechnology , vol.97 , pp. 6779-6791
    • Costa, S.J.1    Almeida, A.2    Castro, A.3    Domingues, L.4    Besir, H.5
  • 22
    • 84886293153 scopus 로고    scopus 로고
    • Purification of calcium-binding proteins using hydrophobic interaction chromatography
    • C. Rozanas Purification of calcium-binding proteins using hydrophobic interaction chromatography Life Science News I 1998 1 14
    • (1998) Life Science News i , pp. 1-14
    • Rozanas, C.1
  • 23
    • 0037377353 scopus 로고    scopus 로고
    • Purification and immunohistochemical analysis of calcium-binding proteins expressed in the chick pineal gland
    • DOI 10.1034/j.1600-079X.2003.00031.x
    • F. Shimizu, K. Sanada, and Y. Fukada Purification and immunohistochemical analysis of calcium-binding proteins expressed in the chick pineal gland Journal of Pineal Research 34 2003 208 216 (Pubitemid 36356848)
    • (2003) Journal of Pineal Research , vol.34 , Issue.3 , pp. 208-216
    • Shimizu, F.1    Sanada, K.2    Fukada, Y.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of head of bacteriophage-T4 Nature 227 1970 680
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 25
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • H. Schagger, and G. von Jagow Tricine-sodium dodecyl sulfate- polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Analytical Biochemistry 166 1987 368 379 (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Analytical Biochemistry 72 1976 248 254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0016272750 scopus 로고
    • Involvement of superoxide anion radical in autoxidation of pyrogallol and a convenient assay for superoxide-dismutase
    • S. Marklund, and G. Marklund Involvement of superoxide anion radical in autoxidation of pyrogallol and a convenient assay for superoxide-dismutase European Journal of Biochemistry 47 1974 469 474
    • (1974) European Journal of Biochemistry , vol.47 , pp. 469-474
    • Marklund, S.1    Marklund, G.2
  • 29
    • 0035805436 scopus 로고    scopus 로고
    • Hydrophobic interaction chromatography of proteins
    • DOI 10.1016/S0168-1656(01)00237-1, PII S0168165601002371
    • J.A. Queiroz, C.T. Tomaz, and J.M.S. Cabral Hydrophobic interaction chromatography of proteins Journal of Biotechnology 87 2001 143 159 (Pubitemid 32241097)
    • (2001) Journal of Biotechnology , vol.87 , Issue.2 , pp. 143-159
    • Queiroz, J.A.1    Tomaz, C.T.2    Cabral, J.M.S.3
  • 30
    • 34547218939 scopus 로고    scopus 로고
    • Effects of salts on protein-surface interactions: Applications for column chromatography
    • DOI 10.1002/jps.20821
    • K. Tsumoto, D. Ejima, A.M. Senczuk, Y. Kita, and T. Arakawa Effects of salts on protein-surface interactions: applications for column chromatography Journal of Pharmaceutical Sciences 96 2007 1677 1690 (Pubitemid 47122947)
    • (2007) Journal of Pharmaceutical Sciences , vol.96 , Issue.7 , pp. 1677-1690
    • Tsumoto, K.1    Ejima, D.2    Senczuk, A.M.3    Kita, Y.4    Arakawa, T.5
  • 31
    • 0034032199 scopus 로고    scopus 로고
    • Effect of calcium and zinc on the activity and thermostability of superoxide dismutase
    • N.T. Bakardjieva, K.N. Christov, and N.V. Christova Effect of calcium and zinc on the activity and thermostability of superoxide dismutase Biologia Plantarum 43 2000 73 78 (Pubitemid 30334094)
    • (2000) Biologia Plantarum , vol.43 , Issue.1 , pp. 73-78
    • Bakardjieva, N.T.1    Christov, K.M.2    Christova, N.V.3
  • 32
    • 20444495296 scopus 로고    scopus 로고
    • Effect of pH changes on water release values in hydrophobic interaction chromatographic systems
    • DOI 10.1016/j.chroma.2005.04.005, PII S0021967305007260
    • F. Xia, D. Nagrath, and S.M. Cramer Effect of pH changes on water release values in hydrophobic interaction chromatographic systems Journal of Chromatography A 1079 2005 229 235 (Pubitemid 40813204)
    • (2005) Journal of Chromatography A , vol.1079 , Issue.SPEC. ISS. 1-2 , pp. 229-235
    • Xia, F.1    Nagrath, D.2    Cramer, S.M.3
  • 33
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • K. Terpe Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems Applied Microbiology and Biotechnology 60 2003 523 533 (Pubitemid 36169526)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 34
    • 0031214792 scopus 로고    scopus 로고
    • 6-Tag and maltose-binding-protein double-affinity fusion system
    • DOI 10.1006/prep.1997.0759
    • K.D. Pryor, and B. Leiting High-level expression of soluble protein in Escherichia coli using a His(6)-tag and maltose-binding-protein double-affinity fusion system Protein Expression and Purification 10 1997 309 319 (Pubitemid 27354171)
    • (1997) Protein Expression and Purification , vol.10 , Issue.3 , pp. 309-319
    • Pryor, K.D.1    Leiting, B.2
  • 35
    • 80053636591 scopus 로고    scopus 로고
    • High throughput construction and small scale expression screening of multi-tag vectors in Escherichia coli
    • L.E. Bird High throughput construction and small scale expression screening of multi-tag vectors in Escherichia coli Methods 55 2011 29 37
    • (2011) Methods , vol.55 , pp. 29-37
    • Bird, L.E.1


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