Expression and detection of ScFvB9 and its mutant in recombinant phage antibody system

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dc.contributor.authorEun Ju Yang-
dc.contributor.authorJu Won Kwak-
dc.contributor.authorHae Choon Chang-
dc.date.accessioned2017-04-19T08:58:45Z-
dc.date.available2017-04-19T08:58:45Z-
dc.date.issued2001-
dc.identifier.issn1536-8599-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5724-
dc.description.abstractRecombinant single-chain antibody (ScFvB9) and its mutant (ScFvB9-6) were generated by using a polymerase chain reaction (PCR) from the Fab fragment of the murine monoclonal antibody (MAb) B9, MabB9 (γ2b, κ), which is specific for human plasma apolipoprotein (apo) B-100 of low density lipopreotein (LDL). In the recombinant phage antibody system (RPAS), the constructed ScFvB9 and ScFvB9-6 antibody genes were cloned into the pCANTAB5E phagemid vector and expressed in E. coli. The active forms of single-chain antibodies (ScFvB9 and ScFvB9-6) were produced as phage-displayed recombinant antibodies or soluble antibody forms in E. coli. The activities of ScFvB9 and ScFvB9-6 were confirmed by enzyme-linked immunosorbent assay (ELISA) and Western blotting analysis; the generated mutant ScFvB9-6 showed slightly higher antigen binding activity than native ScFvB9 as a soluble antibody in this RPAS.-
dc.publisherMary Ann Liebertko
dc.titleExpression and detection of ScFvB9 and its mutant in recombinant phage antibody system-
dc.title.alternativeExpression and detection of ScFvB9 and its mutant in recombinant phage antibody system-
dc.typeArticle-
dc.citation.titleHybridoma and Hybridomics-
dc.citation.number6-
dc.citation.endPage375-
dc.citation.startPage369-
dc.citation.volume20-
dc.contributor.affiliatedAuthorJu Won Kwak-
dc.contributor.alternativeName양은주-
dc.contributor.alternativeName곽주원-
dc.contributor.alternativeName장해춘-
dc.identifier.bibliographicCitationHybridoma and Hybridomics, vol. 20, no. 6, pp. 369-375-
dc.identifier.doi10.1089/15368590152740770-
dc.description.journalClassN-
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