메뉴 건너뛰기




Volumn 44, Issue 1, 2005, Pages 32-38

High expression and purification of the recombinant camelid anti-MUC1 single domain antibodies in Escherichia coli

Author keywords

Expression; MUC1; Purification; Single domain antibody

Indexed keywords

CA 15-3 ANTIGEN; DIAGNOSTIC AGENT; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 26044454570     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.04.008     Document Type: Article
Times cited : (32)

References (28)
  • 1
    • 0032146225 scopus 로고    scopus 로고
    • Recombinant antibody fragments
    • P.J. Hudson Recombinant antibody fragments Curr. Opin. Biotechnol. 9 1998 395 402
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 395-402
    • Hudson, P.J.1
  • 2
    • 0028988662 scopus 로고
    • Cloning, expression and characterization of a single-chain antibody fragment to the herbicide paraquat
    • B.M. Graham, A.J.R. Porter, and W.J. Harris Cloning, expression and characterization of a single-chain antibody fragment to the herbicide paraquat J. Chem. Technol. Biotechnol. 63 1995 279 289
    • (1995) J. Chem. Technol. Biotechnol. , vol.63 , pp. 279-289
    • Graham, B.M.1    Porter, A.J.R.2    Harris, W.J.3
  • 3
    • 0031456403 scopus 로고    scopus 로고
    • Stereoselectivity of antibodies for the bioanalysis of chiral drugs
    • P.A. Got, and J.M. Scherrmann Stereoselectivity of antibodies for the bioanalysis of chiral drugs Pharm. Res. 14 1997 1516 1523
    • (1997) Pharm. Res. , vol.14 , pp. 1516-1523
    • Got, P.A.1    Scherrmann, J.M.2
  • 4
    • 0030989963 scopus 로고    scopus 로고
    • The structural and functional basis of antibody catalysis
    • H. Wade, and T.S. Scanlan The structural and functional basis of antibody catalysis Annu. Rev. Biophys. Biomol. Struct. 26 1997 461 493
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 461-493
    • Wade, H.1    Scanlan, T.S.2
  • 5
    • 8044237717 scopus 로고    scopus 로고
    • High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions
    • U. Horn, W. Strittmatter, A. Krebber, U. Knupfer, M. Kujau, R. Wenderoth, K. Muller, S. Matzku, A. Pluckthum, and D. Riesenberg High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions Appl. Microbiol. Biotechnol. 46 1996 524 532
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 524-532
    • Horn, U.1    Strittmatter, W.2    Krebber, A.3    Knupfer, U.4    Kujau, M.5    Wenderoth, R.6    Muller, K.7    Matzku, S.8    Pluckthum, A.9    Riesenberg, D.10
  • 6
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • C.V. Barbas III, A.S. Kang, R.A. Lerner, and S.J. Benkovic Assembly of combinatorial antibody libraries on phage surfaces: the gene III site Proc. Natl. Acad. Sci. USA 88 18 1991 7978 7982
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , Issue.18 , pp. 7978-7982
    • Barbas III, C.V.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 7
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • A. Skerra, and A. Pluckthunn Assembly of a functional immunoglobulin Fv fragment in Escherichia coli Science 240 4855 1988 1038 1040
    • (1988) Science , vol.240 , Issue.4855 , pp. 1038-1040
    • Skerra, A.1    Pluckthunn, A.2
  • 8
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • R. Glockshuber, M. Malia, I. Pfitzinger, and A. Pluckthun A comparison of strategies to stabilize immunoglobulin Fv-fragments Biochemistry 29 1990 1362 1367
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Pluckthun, A.4
  • 9
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • E.S. Ward, D. Gussow, A.D. Griffiths, P.T. Jones, and G. Winter Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli Nature 341 1989 544 546
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 12
    • 0036570726 scopus 로고    scopus 로고
    • Selection by phage display of llama conventional V(H) fragments with heavy chain antibody V(H)H properties
    • J. Tanha, G. Dubuc, T. Hirama, S. Narang, and C.R. MacKenzie Selection by phage display of llama conventional V(H) fragments with heavy chain antibody V(H)H properties J. Immunol. Methods 263 2002 97 109
    • (2002) J. Immunol. Methods , vol.263 , pp. 97-109
    • Tanha, J.1    Dubuc, G.2    Hirama, T.3    Narang, S.4    MacKenzie, C.R.5
  • 17
    • 0026576245 scopus 로고
    • Epitope mapping of anti-breast and anti-ovarian mucin monoclonal antibodies
    • P.X. Xing, J. Prenzoska, and I.F.C. McKenzie Epitope mapping of anti-breast and anti-ovarian mucin monoclonal antibodies Mol. Immunol. 29 5 1992 641 650
    • (1992) Mol. Immunol. , vol.29 , Issue.5 , pp. 641-650
    • Xing, P.X.1    Prenzoska, J.2    McKenzie, I.F.C.3
  • 20
    • 0024999277 scopus 로고
    • Anti-colorectal carcinoma monoclonal antibodies reactive with human milk fat globular membranes
    • J.G. Teh, P.X. Xing, and I.F.C. McKenzie Anti-colorectal carcinoma monoclonal antibodies reactive with human milk fat globular membranes Immunol. Cell Biol. 68 1990 207 216
    • (1990) Immunol. Cell Biol. , vol.68 , pp. 207-216
    • Teh, J.G.1    Xing, P.X.2    McKenzie, I.F.C.3
  • 21
    • 0029966497 scopus 로고    scopus 로고
    • MUC1 glycoforms in breast cancer-cell line T47D as a model for carcinoma-associated alterations of O-glycosylation
    • F.G. Hanisch, T.R.E. Stadie, F. Deutzmann, and J. Peter-Katalinc MUC1 glycoforms in breast cancer-cell line T47D as a model for carcinoma-associated alterations of O-glycosylation Eur. J. Biochem. 236 1996 318 327
    • (1996) Eur. J. Biochem. , vol.236 , pp. 318-327
    • Hanisch, F.G.1    Stadie, T.R.E.2    Deutzmann, F.3    Peter-Katalinc, J.4
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 7 1976 248 254
    • (1976) Anal. Biochem. , vol.7 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 0037047012 scopus 로고    scopus 로고
    • Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface
    • W. Vranken, D. Tolkatchev, P. Xu, J. Tanha, Z. Chen, S. Narang, and F. Ni Solution structure of a llama single-domain antibody with hydrophobic residues typical of the VH/VL interface Biochemistry 41 27 2002 8570 8579
    • (2002) Biochemistry , vol.41 , Issue.27 , pp. 8570-8579
    • Vranken, W.1    Tolkatchev, D.2    Xu, P.3    Tanha, J.4    Chen, Z.5    Narang, S.6    Ni, F.7
  • 27
    • 0030767656 scopus 로고    scopus 로고
    • Selection and identification of single domain antibody fragments from camel heavy-chain antibodies
    • M. Ghahroudi, A. Desmyter, L. Wyns, R. Hamers, and S. Muylderman Selection and identification of single domain antibody fragments from camel heavy-chain antibodies FEBS Lett. 414 1997 521 526
    • (1997) FEBS Lett. , vol.414 , pp. 521-526
    • Ghahroudi, M.1    Desmyter, A.2    Wyns, L.3    Hamers, R.4    Muylderman, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.