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Please use this identifier to cite or link to this item: https://doi.org/10.1021/ja0265963
DC FieldValue
dc.titleIntein-mediated biotinylation of proteins and its application in a protein microarray
dc.contributor.authorLesaicherre, M.-L.
dc.contributor.authorLue, R.Y.P.
dc.contributor.authorChen, G.Y.J.
dc.contributor.authorZhu, Q.
dc.contributor.authorYao, S.Q.
dc.date.accessioned2014-06-23T05:42:11Z
dc.date.available2014-06-23T05:42:11Z
dc.date.issued2002-07-31
dc.identifier.citationLesaicherre, M.-L., Lue, R.Y.P., Chen, G.Y.J., Zhu, Q., Yao, S.Q. (2002-07-31). Intein-mediated biotinylation of proteins and its application in a protein microarray. Journal of the American Chemical Society 124 (30) : 8768-8769. ScholarBank@NUS Repository. https://doi.org/10.1021/ja0265963
dc.identifier.issn00027863
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/76388
dc.description.abstractWe report here the first example using an intein-mediated expression system to generate biotinylated proteins suitable for immobilization onto avidin-functionalized glass slides. With this novel array, proteins are site-specifically immobilized on the glass surface and are able to retain their native activity. The advantage of the avidin/biotin linkage over his-tag/Ni-NTA strategies for protein immobilization is highlighted by its ability to withstand a variety of chemical conditions, which makes this new protein array compatible with most biological assays. Copyright © 2002 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/ja0265963
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentPAEDIATRICS
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1021/ja0265963
dc.description.sourcetitleJournal of the American Chemical Society
dc.description.volume124
dc.description.issue30
dc.description.page8768-8769
dc.description.codenJACSA
dc.identifier.isiut000177074400003
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