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dc.contributor.authorMiller, EA
dc.contributor.authorTraxlmayr, MW
dc.contributor.authorShen, J
dc.contributor.authorSikes, HD
dc.date.accessioned2021-10-27T20:28:54Z
dc.date.available2021-10-27T20:28:54Z
dc.date.issued2016
dc.identifier.urihttps://hdl.handle.net/1721.1/135706
dc.description.abstractThis journal is © The Royal Society of Chemistry. Antibodies have traditionally served as the affinity reagents of choice in point-of-care diagnostic biosensors. However, this class of proteins is not ideally suited for this use, being poorly characterized and prone to thermal denaturation. Here, we present an activity-based assessment of an alternative engineered binding protein in a cellulose-based assay.
dc.language.isoen
dc.publisherRoyal Society of Chemistry (RSC)
dc.relation.isversionof10.1039/C6ME00032K
dc.rightsCreative Commons Attribution-Noncommercial-Share Alike
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.sourcePMC
dc.titleActivity-based assessment of an engineered hyperthermophilic protein as a capture agent in paper-based diagnostic tests
dc.typeArticle
dc.identifier.citationMiller, E. A., et al. "Activity-Based Assessment of an Engineered Hyperthermophilic Protein as a Capture Agent in Paper-Based Diagnostic Tests." Mol Syst Des Eng 1 4 (2016): 377-81.
dc.relation.journalMolecular Systems Design and Engineering
dc.eprint.versionAuthor's final manuscript
dc.type.urihttp://purl.org/eprint/type/JournalArticle
eprint.statushttp://purl.org/eprint/status/PeerReviewed
dc.date.updated2019-09-11T16:30:41Z
dspace.orderedauthorsMiller, EA; Traxlmayr, MW; Shen, J; Sikes, HD
dspace.date.submission2019-09-11T16:30:42Z
mit.journal.volume1
mit.journal.issue4
mit.metadata.statusAuthority Work and Publication Information Needed


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