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Production, characterization, and epitope mapping of monoclonal antibodies of ribosomal protein S3 (rpS3)

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dc.contributor.authorAhn, Woo-Sung-
dc.contributor.authorKim, Tae-Sung-
dc.contributor.authorPark, Yong Jun-
dc.contributor.authorPark, Young Kwang-
dc.contributor.authorKim, Hag Dong-
dc.contributor.authorKim, Joon-
dc.date.accessioned2022-02-21T13:42:44Z-
dc.date.available2022-02-21T13:42:44Z-
dc.date.created2022-02-08-
dc.date.issued2021-09-03-
dc.identifier.issn1976-8354-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/136388-
dc.description.abstractRibosomal protein S3 (rpS3), a member of 40S small ribosomal subunit, is a multifunctional protein with various extra-ribosomal functions including DNA repair endonuclease activity and is secreted from cancer cells. Therefore, antibodies with high specificity against rpS3 protein could be useful cancer biomarkers. In this study, polyclonal antibody (pAb) and monoclonal antibodies (mAbs) were raised against rpS3 protein and epitope mapping was performed for each antibody; the amino acid residues of rpS3 were scanned from amino acid 185 to 243 through peptide scanning to reveal the epitopes of each mAb. Results showed that pAb R2 has an epitope from amino acid 203 to 230, mAb M7 has an epitope from amino acid 213 to 221, and mAb M8 has an epitope from amino acid 197 to 219. Taken together, novel mAbs and pAb against rpS3 were raised and mapped against rpS3 with different specific epitopes.-
dc.languageEnglish-
dc.language.isoen-
dc.publisherTAYLOR & FRANCIS LTD-
dc.subjectGENOMIC STRUCTURE-
dc.subjectCANCER-
dc.subjectANTIGENS-
dc.subjectTHERAPY-
dc.subjectBINDING-
dc.subjectGENE-
dc.titleProduction, characterization, and epitope mapping of monoclonal antibodies of ribosomal protein S3 (rpS3)-
dc.typeArticle-
dc.contributor.affiliatedAuthorKim, Joon-
dc.identifier.doi10.1080/19768354.2021.1980100-
dc.identifier.scopusid2-s2.0-85116478287-
dc.identifier.wosid000704277500001-
dc.identifier.bibliographicCitationANIMAL CELLS AND SYSTEMS, v.25, no.5, pp.323 - 336-
dc.relation.isPartOfANIMAL CELLS AND SYSTEMS-
dc.citation.titleANIMAL CELLS AND SYSTEMS-
dc.citation.volume25-
dc.citation.number5-
dc.citation.startPage323-
dc.citation.endPage336-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.identifier.kciidART002771755-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.description.journalRegisteredClasskci-
dc.relation.journalResearchAreaCell Biology-
dc.relation.journalResearchAreaZoology-
dc.relation.journalWebOfScienceCategoryCell Biology-
dc.relation.journalWebOfScienceCategoryZoology-
dc.subject.keywordPlusANTIGENS-
dc.subject.keywordPlusBINDING-
dc.subject.keywordPlusCANCER-
dc.subject.keywordPlusGENE-
dc.subject.keywordPlusGENOMIC STRUCTURE-
dc.subject.keywordPlusTHERAPY-
dc.subject.keywordAuthorRibosomal protein subunit small 3-
dc.subject.keywordAuthorconformational epitope-
dc.subject.keywordAuthordirect ELISA-
dc.subject.keywordAuthorepitope mapping-
dc.subject.keywordAuthorimmunoprecipitation-
dc.subject.keywordAuthorlinear form epitope-
dc.subject.keywordAuthormAb-
dc.subject.keywordAuthorpeptide synthesis-
dc.subject.keywordAuthorsandwich ELISA-
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