Luminescent terbium protein labels for time-resolved microscopy and screening.
Brilliance of terbium: Heterodimeric conjugates of trimethoprim covalently linked to sensitized terbium chelates bind to Escherichia coli dihydrofolate reductase fusion proteins with nanomolar affinity (see picture). Terbium luminescence enables sensitive and time-resolved detection of labeled proteins in vitro and on the surface of living mammalian cells.
Rajapakse
Harsha E
HE
Department of Chemistry, University of Illinois at Chicago, 845 W. Taylor St., Chicago, IL 60607, USA.
Reddy
D Rajasekhar
DR
Mohandessi
Shabnam
S
Butlin
Nathaniel G
NG
Miller
Lawrence W
LW
D000818:Animals; D002460:Cell Line; D031541:Fluorescence Resonance Energy Transfer; D005456:Fluorescent Dyes / Q000737:chemistry*; D051379:Mice; D008856:Microscopy, Fluorescence; D041681:NIH 3T3 Cells; D011993:Recombinant Fusion Proteins / Q000032:analysis* / Q000737:chemistry; D013725:Terbium / Q000737:chemistry*; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry* / Q000235:genetics; D014295:Trimethoprim / Q000737:chemistry
D005456:Fluorescent Dyes; D011993:Recombinant Fusion Proteins; D013725:Terbium; D014295:Trimethoprim; D013762:Tetrahydrofolate Dehydrogenase