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Volumn 36, Issue 10, 2009, Pages 1364-1669

Current strategies for polypeptide fusion tags removal

Author keywords

Fusion proteins; Intein; Polypeptide fusion tags; Protease; Tag removal

Indexed keywords


EID: 74549196928     PISSN: 10003282     EISSN: None     Source Type: Journal    
DOI: 10.3724/SP.J.1206.2009.00160     Document Type: Article
Times cited : (3)

References (39)
  • 1
    • 69249215474 scopus 로고    scopus 로고
    • Making the most of fusion tags technology in structural characterization of membrane proteins
    • Xie H, Guo X M, Chen H. Making the most of fusion tags technology in structural characterization of membrane proteins. Mol Biotech, 2009, 42 (2):135-145
    • (2009) Mol Biotech , vol.42 , Issue.2 , pp. 135-145
    • Xie, H.1    Guo, X.M.2    Chen, H.3
  • 2
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh D S. Making the most of affinity tags. TRENDS in Biotechnology, 2005, 23 (6):316-320
    • (2005) TRENDS in Biotechnology , vol.23 , Issue.6 , pp. 316-320
    • Waugh, D.S.1
  • 3
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl Micro Biotech, 2003, 60 (5):523-533
    • (2003) Appl Micro Biotech , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 4
    • 11844272620 scopus 로고    scopus 로고
    • Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein AreA causes a conformational change at the DNA-binding site
    • Chant A, Kraemer-Pecore C M, Watkin R, et al. Attachment of a histidine tag to the minimal zinc finger protein of the Aspergillus nidulans gene regulatory protein AreA causes a conformational change at the DNA-binding site. Prot Exp Puri, 2005, 39 (2):152-159
    • (2005) Prot Exp Puri , vol.39 , Issue.2 , pp. 152-159
    • Chant, A.1    Kraemer-Pecore, C.M.2    Watkin, R.3
  • 5
    • 3042543297 scopus 로고    scopus 로고
    • Expression and purification of rat recombinant aminopeptidase B secreted from baculovirus-infected insect cells
    • Cadel S, Gouzy-Darmon C, Petres S, et al. Expression and purification of rat recombinant aminopeptidase B secreted from baculovirus-infected insect cells. Prot Exp Puri, 2004, 36 (1):19-30
    • (2004) Prot Exp Puri , vol.36 , Issue.1 , pp. 19-30
    • Cadel, S.1    Gouzy-Darmon, C.2    Petres, S.3
  • 6
    • 0034283337 scopus 로고    scopus 로고
    • Relative position of the hexahistidine tag effects binding properties of a tumor-associated single-chain Fv construct
    • Goel A, Colcher D, Koo J S, et al. Relative position of the hexahistidine tag effects binding properties of a tumor-associated single-chain Fv construct. Biochim Biophys Acta, 2000, 1523 (1):13-20
    • (2000) Biochim Biophys Acta , vol.1523 , Issue.1 , pp. 13-20
    • Goel, A.1    Colcher, D.2    Koo, J.S.3
  • 7
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purifcation of recombinant proteins
    • Arnau J, Lauritzen C, Petersen G E, et al. Current strategies for the use of affinity tags and tag removal for the purifcation of recombinant proteins. Prot Exp Puri, 2006, 48 (1):1-13
    • (2006) Prot Exp Puri , vol.48 , Issue.1 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3
  • 8
    • 0036425272 scopus 로고    scopus 로고
    • A fusion protein system for the recombinant production of short disulfide-containing peptides
    • Fairlie W D, Uboldi A D, De Souza D P, et al. A fusion protein system for the recombinant production of short disulfide-containing peptides. Prot Exp Puri, 2002, 26 (1):171-178
    • (2002) Prot Exp Puri , vol.26 , Issue.1 , pp. 171-178
    • Fairlie, W.D.1    Uboldi, A.D.2    De Souza, D.P.3
  • 9
    • 28944441962 scopus 로고    scopus 로고
    • Influence of the protein oligomericity on final yield after affinity tag removal in purification of recombinant proteins
    • Kenig M, Peternel S, Gaberc-Porekar V, et al. Influence of the protein oligomericity on final yield after affinity tag removal in purification of recombinant proteins. J Chromato A, 2006, 1101(1-2):293-306
    • (2006) J Chromato A , vol.1101 , Issue.1-2 , pp. 293-306
    • Kenig, M.1    Peternel, S.2    Gaberc-Porekar, V.3
  • 10
    • 0036100312 scopus 로고    scopus 로고
    • Covalent cross-linking of proteins without chemical reagents
    • Simons B L, King M C, Cyr T, et al. Covalent cross-linking of proteins without chemical reagents. Protein Science, 2002, 11 (6):1558-1564
    • (2002) Protein Science , vol.11 , Issue.6 , pp. 1558-1564
    • Simons, B.L.1    King, M.C.2    Cyr, T.3
  • 11
    • 0141539517 scopus 로고    scopus 로고
    • A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa
    • Jenny R J, Mann K G, Lundblad R L. A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa. Prot Exp Puri, 2003, 31 (1):1-11
    • (2003) Prot Exp Puri , vol.31 , Issue.1 , pp. 1-11
    • Jenny, R.J.1    Mann, K.G.2    Lundblad, R.L.3
  • 12
    • 42749093598 scopus 로고    scopus 로고
    • Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag
    • Shahravan S H, Qu X L, Chan I S, et al. Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag. Prot Exp Puri, 2008, 59 (2):314-319
    • (2008) Prot Exp Puri , vol.59 , Issue.2 , pp. 314-319
    • Shahravan, S.H.1    Qu, X.L.2    Chan, I.S.3
  • 13
    • 33847128295 scopus 로고    scopus 로고
    • Use of dual affinity tags for expression and purification of functional peripheral cannabinoid receptor
    • Yeliseev A, Zoubak L, Gawrisch K. Use of dual affinity tags for expression and purification of functional peripheral cannabinoid receptor. Prot Exp Puri, 2007, 53 (1):153-163
    • (2007) Prot Exp Puri , vol.53 , Issue.1 , pp. 153-163
    • Yeliseev, A.1    Zoubak, L.2    Gawrisch, K.3
  • 14
    • 10644262375 scopus 로고    scopus 로고
    • Expression, refolding, and purification of recombinant human granzyme B
    • Lorentsen R H, Fynbo C H, Thøgersen H C, et al. Expression, refolding, and purification of recombinant human granzyme B. Prot Exp Puri, 2005, 39 (1):18-26
    • (2005) Prot Exp Puri , vol.39 , Issue.1 , pp. 18-26
    • Lorentsen, R.H.1    Fynbo, C.H.2    Thøgersen, H.C.3
  • 15
    • 11844292771 scopus 로고    scopus 로고
    • High level expression and single-step purification of hexahistidine-tagged L-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set
    • Chatterjee S, Schoepe J, Lohmer S, et al. High level expression and single-step purification of hexahistidine-tagged L-2-hydroxyisocaproate dehydrogenase making use of a versatile expression vector set. Prot Exp Puri, 2005, 39 (2):137-143
    • (2005) Prot Exp Puri , vol.39 , Issue.2 , pp. 137-143
    • Chatterjee, S.1    Schoepe, J.2    Lohmer, S.3
  • 16
    • 0033541686 scopus 로고    scopus 로고
    • 4Lys on enterokinase cleavage of a fusion protein
    • 4Lys on enterokinase cleavage of a fusion protein. Anal Biochem, 1999, 269 (1):10-16
    • (1999) Anal Biochem , vol.269 , Issue.1 , pp. 10-16
    • Hosfield, T.1    Lu, Q.2
  • 17
    • 33646097216 scopus 로고    scopus 로고
    • Gi/o proteins: Expression for direct activation enquiry
    • Di Cesare Mannelli L, Pacini A, Toscano A, et al. Gi/o proteins: expression for direct activation enquiry. Prot Exp Puri, 2006, 47 (1):303-310
    • (2006) Prot Exp Puri , vol.47 , Issue.1 , pp. 303-310
    • Di Cesare Mannelli, L.1    Pacini, A.2    Toscano, A.3
  • 18
    • 57649112190 scopus 로고    scopus 로고
    • Purification and characterization of anthranilate synthase component I (TrpE) from Mycobacterium tuberculosis H37Rv
    • Lin X H, Xu S F, Yang Y P, et al. Purification and characterization of anthranilate synthase component I (TrpE) from Mycobacterium tuberculosis H37Rv. Prot Exp Puri, 2009, 64 (1):8-15
    • (2009) Prot Exp Puri , vol.64 , Issue.1 , pp. 8-15
    • Lin, X.H.1    Xu, S.F.2    Yang, Y.P.3
  • 19
    • 3543063548 scopus 로고    scopus 로고
    • A self-cleavable sortase fusion for one-step purification of free recombinant proteins
    • Mao H. A self-cleavable sortase fusion for one-step purification of free recombinant proteins. Prot Exp Puri, 2004, 37 (1):253-263
    • (2004) Prot Exp Puri , vol.37 , Issue.1 , pp. 253-263
    • Mao, H.1
  • 21
    • 37349073090 scopus 로고    scopus 로고
    • Production and comprehensive quality control of recombinant human Interleukin-1 beta: A case study for a process development strategy
    • Block H, Kubicek J, Labahn J, et al. Production and comprehensive quality control of recombinant human Interleukin-1 beta: A case study for a process development strategy. Prot Exp Puri, 2008, 57 (2):244-254
    • (2008) Prot Exp Puri , vol.57 , Issue.2 , pp. 244-254
    • Block, H.1    Kubicek, J.2    Labahn, J.3
  • 22
    • 40549118522 scopus 로고    scopus 로고
    • The use of TAGZyme for the efficient removal of n-terminal His-tags
    • Arnau J, Lauritzen C, Petersen G E, et al. The use of TAGZyme for the efficient removal of n-terminal His-tags. Metho Mol Biol, 2008, 421:229-243
    • (2008) Metho Mol Biol , vol.421 , pp. 229-243
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3
  • 23
    • 34648828739 scopus 로고    scopus 로고
    • Cloning strategy, production and purification of proteins with exopeptidase-cleavable His-tags
    • Arnau J, Lauritzen C, Pedersen J. Cloning strategy, production and purification of proteins with exopeptidase-cleavable His-tags. Nature Protocols, 2006, 1 (5):2326-2333
    • (2006) Nature Protocols , vol.1 , Issue.5 , pp. 2326-2333
    • Arnau, J.1    Lauritzen, C.2    Pedersen, J.3
  • 24
    • 34548582108 scopus 로고    scopus 로고
    • Improving the purification of NAD (+) - dependent formate dehydrogenase from Candida methylica
    • Ordu E B, Karaguler N G. Improving the purification of NAD (+) - dependent formate dehydrogenase from Candida methylica. Prep Biochem Biotech, 2007, 37 (4):333-341
    • (2007) Prep Biochem Biotech , vol.37 , Issue.4 , pp. 333-341
    • Ordu, E.B.1    Karaguler, N.G.2
  • 25
    • 0033117468 scopus 로고    scopus 로고
    • Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases
    • Pedersen J, Lauritzen C, Madsen M T, et al. Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases. Prot Exp Puri, 1999, 15 (3):389-400
    • (1999) Prot Exp Puri , vol.15 , Issue.3 , pp. 389-400
    • Pedersen, J.1    Lauritzen, C.2    Madsen, M.T.3
  • 26
    • 33845993905 scopus 로고    scopus 로고
    • The proteomics of N-terminal methionine cleavage
    • Frottin F, Martinez A, Peynot P, et al. The proteomics of N-terminal methionine cleavage. Mole Cell Prot, 2006, 5 (12):2336-2349
    • (2006) Mole Cell Prot , vol.5 , Issue.12 , pp. 2336-2349
    • Frottin, F.1    Martinez, A.2    Peynot, P.3
  • 28
    • 0036084146 scopus 로고    scopus 로고
    • InBase, the intein database
    • Perler F B. InBase, the intein database. Nucl Acid Res, 2002, 30 (1):383-384
    • (2002) Nucl Acid Res , vol.30 , Issue.1 , pp. 383-384
    • Perler, F.B.1
  • 29
    • 74549166510 scopus 로고    scopus 로고
    • http://www.neb.com/neb/inteins.html
  • 30
    • 4444274531 scopus 로고    scopus 로고
    • Intein-mediated fusion expression, high efficient refolding, and one-step purification of gelonin toxin
    • Guo C, Li Z, Shi Y, et al. Intein-mediated fusion expression, high efficient refolding, and one-step purification of gelonin toxin. Prot Exp Puri, 2004, 37 (2):361-367
    • (2004) Prot Exp Puri , vol.37 , Issue.2 , pp. 361-367
    • Guo, C.1    Li, Z.2    Shi, Y.3
  • 31
    • 0033614484 scopus 로고    scopus 로고
    • Characterization of a self-splicing mini-intein and its conversion into autocatalytic N-and C-terminal cleavage elements: Facile production of protein building blocks for protein ligation
    • Mathys S, Evans T C, Chute I C, et al. Characterization of a self-splicing mini-intein and its conversion into autocatalytic N-and C-terminal cleavage elements: facile production of protein building blocks for protein ligation. Gene, 1999, 231(1-2):1-13
    • (1999) Gene , vol.231 , Issue.1-2 , pp. 1-13
    • Mathys, S.1    Evans, T.C.2    Chute, I.C.3
  • 32
    • 0029838842 scopus 로고    scopus 로고
    • The mechanism of protein splicing and its modulation by mutation
    • Xu M Q, Perler F B. The mechanism of protein splicing and its modulation by mutation. EMBO Journal, 1996, 15 (19):5146-5153
    • (1996) EMBO Journal , vol.15 , Issue.19 , pp. 5146-5153
    • Xu, M.Q.1    Perler, F.B.2
  • 33
    • 0036421180 scopus 로고    scopus 로고
    • Expression of the class 1 outer-membrane protein of Neisseria meningitidis in Escherichia coli and purification using a self-cleavable affinity tag
    • Humphries H E, Christodoulides M, Heckels J E. Expression of the class 1 outer-membrane protein of Neisseria meningitidis in Escherichia coli and purification using a self-cleavable affinity tag. Prot Exp Puri, 2002, 26 (2):243-248
    • (2002) Prot Exp Puri , vol.26 , Issue.2 , pp. 243-248
    • Humphries, H.E.1    Christodoulides, M.2    Heckels, J.E.3
  • 34
    • 23244448024 scopus 로고    scopus 로고
    • Use of Ssp dnaB derived mini-intein as a fusion partner for production of recombinant human brain natriuretic peptide in Escherichia coli
    • Sun Z, Chen J, Yao H, et al. Use of Ssp dnaB derived mini-intein as a fusion partner for production of recombinant human brain natriuretic peptide in Escherichia coli. Prot Exp Puri, 2005, 43 (1):26-32
    • (2005) Prot Exp Puri , vol.43 , Issue.1 , pp. 26-32
    • Sun, Z.1    Chen, J.2    Yao, H.3
  • 35
    • 0036915084 scopus 로고    scopus 로고
    • Intein-mediated affinity-fusion purification of the Escherichia coli RecA protein
    • Singleton S F, Simonette R A, Sharma N C, et al. Intein-mediated affinity-fusion purification of the Escherichia coli RecA protein. Prot Exp Puri, 2002, 26 (3):476-488
    • (2002) Prot Exp Puri , vol.26 , Issue.3 , pp. 476-488
    • Singleton, S.F.1    Simonette, R.A.2    Sharma, N.C.3
  • 36
    • 36048948927 scopus 로고    scopus 로고
    • Towards the elimination of chromatography in protein purification: Expressing proteins engineered to purify themselves
    • Mee C, Banki M R, Wood D W. Towards the elimination of chromatography in protein purification: expressing proteins engineered to purify themselves. Chem Engin J, 2008, 135(1-2):56-62
    • (2008) Chem Engin J , vol.135 , Issue.1-2 , pp. 56-62
    • Mee, C.1    Banki, M.R.2    Wood, D.W.3
  • 37
    • 37349089033 scopus 로고    scopus 로고
    • Tris is a non-innocent buffer during intein-mediated protein cleavage
    • Peroza E A, Freisinger E. Tris is a non-innocent buffer during intein-mediated protein cleavage. Prot Exp Puri, 2008, 57 (2):217-225
    • (2008) Prot Exp Puri , vol.57 , Issue.2 , pp. 217-225
    • Peroza, E.A.1    Freisinger, E.2
  • 38
    • 22444444258 scopus 로고    scopus 로고
    • Novel and economical purification of recombinant proteins: Intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
    • Banki M R, Gerngross T U, Wood D W. Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Prot Sci, 2005, 14 (6):1387-1395
    • (2005) Prot Sci , vol.14 , Issue.6 , pp. 1387-1395
    • Banki, M.R.1    Gerngross, T.U.2    Wood, D.W.3
  • 39
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastin-like polypeptide tags
    • Banki M R, Feng L, Wood D W. Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nat Methods, 2005, 2 (9):659-661
    • (2005) Nat Methods , vol.2 , Issue.9 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.