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DC Field | Value | Language |
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dc.citation.endPage | 5481 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 5473 | - |
dc.citation.title | ANALYTICAL CHEMISTRY | - |
dc.citation.volume | 92 | - |
dc.contributor.author | Eom, Soomin | - |
dc.contributor.author | Bae, Yoonji | - |
dc.contributor.author | Kim, Sunghwan | - |
dc.contributor.author | Choi, Hyukjun | - |
dc.contributor.author | Park, Jongnam | - |
dc.contributor.author | Kang, Sebyung | - |
dc.date.accessioned | 2023-12-21T17:42:56Z | - |
dc.date.available | 2023-12-21T17:42:56Z | - |
dc.date.created | 2020-04-13 | - |
dc.date.issued | 2020-04 | - |
dc.description.abstract | In general immunoassays, secondary antibodies are covalently linked with enzymes and bind to the Fc region of targetbound primary antibodies to amplify signals of low-abundant target molecules. The antibodies themselves are obtained from large mammals and are further modified with enzymes. In this study, we developed novel recombinant immunoglobulin G (IgG)-binding luciferase-based signal amplifiers (rILSAs) by genetically fusing luciferase (Nluc) with antimouse IgG1 nanobody (MG1Nb) and antibody-binding domain (ABD), individually or together, in a mixand-match manner. We obtained three different highly pure rILSAs in large quantities using a bacterial overexpression system and one-step purification. Mouse-specific rILSA, MG1Nb-Nluc, and rabbit-specific rILSA, Nluc-ABD, selectively bound to target-molecule-bound mouse IgG1 and rabbit IgG primary antibodies, whereas the bispecific rILSA, MG1Nb-Nluc-ABD, mutually bound to both mouse IgG1 and rabbit IgG primary antibodies. All rILSAs exhibited an outstanding signal-amplifying capability comparable to those of conventional horseradish-peroxidase-conjugated secondary antibodies, regardless of the target molecules, in various immunoassay formats, such as enzyme-linked immunosorbent assay, Western blot, and lateral flow assays. Each rILSA was selected for its own individual purpose and applied to various types of target analytes, in combination with a variety of target-specific primary antibodies, effectively minimizing the use of animals as well as reducing the costs and time associated with the production and chemical conjugation of signal-amplifying enzymes. | - |
dc.identifier.bibliographicCitation | ANALYTICAL CHEMISTRY, v.92, no.7, pp.5473 - 5481 | - |
dc.identifier.doi | 10.1021/acs.analchem.0c00222 | - |
dc.identifier.issn | 0003-2700 | - |
dc.identifier.scopusid | 2-s2.0-85088912774 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/31909 | - |
dc.identifier.url | https://pubs.acs.org/doi/abs/10.1021/acs.analchem.0c00222# | - |
dc.identifier.wosid | 000526569200099 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Development of Recombinant Immunoglobulin G-Binding Luciferase-Based Signal Amplifiers in Immunoassays | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Analytical | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.type.docType | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordPlus | EP-CAM | - |
dc.subject.keywordPlus | POINT | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | BINDERS | - |
dc.subject.keywordPlus | MARKER | - |
dc.subject.keywordPlus | MOUSE | - |
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