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dc.creatorBurg, L
dc.creatorZhang, K
dc.creatorBonawitz, T
dc.creatorGrajevskaja, V
dc.creatorBellipanni, G
dc.creatorWaring, R
dc.creatorBalciunas, D
dc.date.accessioned2021-01-25T21:44:26Z
dc.date.available2021-01-25T21:44:26Z
dc.date.issued2016-11-28
dc.identifier.issn2045-2322
dc.identifier.issn2045-2322
dc.identifier.doihttp://dx.doi.org/10.34944/dspace/4975
dc.identifier.other27892520 (pubmed)
dc.identifier.urihttp://hdl.handle.net/20.500.12613/4993
dc.description.abstractMany experimental techniques rely on specific recognition and stringent binding of proteins by antibodies. This can readily be achieved by introducing an epitope tag. We employed an approach that uses a relative lack of evolutionary conservation to inform epitope tag site selection, followed by integration of the tag-coding sequence into the endogenous locus in zebrafish. We demonstrate that an internal epitope tag is accessible for antibody binding, and that tagged proteins retain wild type function.
dc.format.extent36986-
dc.language.isoen
dc.relation.haspartScientific Reports
dc.relation.isreferencedbySpringer Science and Business Media LLC
dc.rightsCC BY
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectAntibodies
dc.subjectConserved Sequence
dc.subjectEpitopes
dc.subjectProteins
dc.subjectSequence Alignment
dc.subjectZebrafish
dc.titleInternal epitope tagging informed by relative lack of sequence conservation
dc.typeArticle
dc.type.genreJournal Article
dc.relation.doi10.1038/srep36986
dc.ada.noteFor Americans with Disabilities Act (ADA) accommodation, including help with reading this content, please contact scholarshare@temple.edu
dc.creator.orcidBalciunas, Darius|0000-0003-1938-3243
dc.date.updated2021-01-25T21:44:21Z
refterms.dateFOA2021-01-25T21:44:26Z


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