FluoSpheres™ Biotin-Labeled Microspheres, 0.04 μm, yellow-green fluorescent (505/515), 1% solids - Citations

FluoSpheres™ Biotin-Labeled Microspheres, 0.04 μm, yellow-green fluorescent (505/515), 1% solids - Citations

View additional product information for FluoSpheres™ Biotin-Labeled Microspheres, 0.04 μm, yellow-green fluorescent (505/515), 1% solids - Citations (F8766)

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Citations & References
Abstract
Nanoparticles as fluorescence labels: is size all that matters?
AuthorsSwift JL, Cramb DT,
JournalBiophys J
PubMed ID18390610
'Fluorescent labels are often used in bioassays as a means to detect and characterize ligand-receptor binding. This is due in part to the inherently high sensitivity of fluorescence-based technology and the relative accessibility of the technique. There is often little concern raised as to whether or not the fluorescent label ... More
Selective aluminum passivation for targeted immobilization of single DNA polymerase molecules in zero-mode waveguide nanostructures.
AuthorsKorlach J, Marks PJ, Cicero RL, Gray JJ, Murphy DL, Roitman DB, Pham TT, Otto GA, Foquet M, Turner SW,
JournalProc Natl Acad Sci U S A
PubMed ID18216253
Optical nanostructures have enabled the creation of subdiffraction detection volumes for single-molecule fluorescence microscopy. Their applicability is extended by the ability to place molecules in the confined observation volume without interfering with their biological function. Here, we demonstrate that processive DNA synthesis thousands of bases in length was carried out ... More
A contiguous compartment functions as endoplasmic reticulum and endosome/lysosome in Giardia lamblia.
AuthorsAbodeely M, DuBois KN, Hehl A, Stefanic S, Sajid M, DeSouza W, Attias M, Engel JC, Hsieh I, Fetter RD, McKerrow JH,
JournalEukaryot Cell
PubMed ID19749174
The dynamic evolution of organelle compartmentalization in eukaryotes and how strictly compartmentalization is maintained are matters of ongoing debate. While the endoplasmic reticulum (ER) is classically envisioned as the site of protein cotranslational translocation, it has recently been proposed to have pluripotent functions. Using transfected reporter constructs, organelle-specific markers, and ... More
Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics.
AuthorsBedoukian MA, Weeks AM, Partin KM
JournalJ Biol Chem
PubMed ID16793768
Stargazin is an accessory protein of AMPA receptors that enhances surface expression and also affects the biophysical properties of the receptor. AMPA receptor domains necessary for either of these two processes have not yet been identified. Here, we used confocal imaging and electrophysiology of heterologously expressed, fluorophore-tagged GluR1, GluR2, and ... More