Site-Specific Labeling of Surface Proteins on Living Cells Using Genetically Encoded Peptides that Bind Fluorescent Nanoparticle Probes

2009 ◽  
Vol 20 (8) ◽  
pp. 1482-1489 ◽  
Author(s):  
Mark A. Rocco ◽  
Jae-Young Kim ◽  
Andrew Burns ◽  
Jan Kostecki ◽  
Anne Doody ◽  
...  
2021 ◽  
Vol 179 ◽  
pp. 113084 ◽  
Author(s):  
Sylvie Egloff ◽  
Nina Melnychuk ◽  
Andreas Reisch ◽  
Sophie Martin ◽  
Andrey S. Klymchenko

2014 ◽  
Vol 50 (94) ◽  
pp. 14724-14727 ◽  
Author(s):  
Ming Cheng ◽  
Wei Zhang ◽  
Jinghe Yuan ◽  
Wangxi Luo ◽  
Nan Li ◽  
...  

Single-molecule dynamics of the transforming growth factor type II receptor (TβRII) labeled by an unnatural amino acid.


2020 ◽  
Author(s):  
Katsuya Noguchi ◽  
Takashi Shimomura ◽  
Yuya Ohuchi ◽  
Munetaka Ishiyama ◽  
Masanobu Shiga ◽  
...  

The ability to detect cell surface proteins using fluorescent dye-labeled antibodies is crucial for the reliable identification of many cell types. However, the different types of cell surface proteins used to identify cells are currently limited in number because they need to be expressed at high levels to exceed background cellular autofluorescence, especially in the shorter wavelength region. Herein, we report on a new method (CLAMP: quinone methide-based <u>c</u>atalyzed signa<u>l</u> <u>amp</u>lification) in which the fluorescence signal is amplified by an enzymatic reaction that strongly facilitates the detection of cell surface proteins on living cells. We used β-galactosidase as an amplification enzyme and designed a substrate for it, called MUGF, which contains a fluoromethyl group. Upon removal of the galactosyl group in MUGF by β-galactosidase labeling of the target cell surface proteins, the resulting quinone methide group-containing product was found to be both cell membrane permeable and reactive with intracellular nucleophiles, thereby providing fluorescent adducts. Using this method, we successfully detected several cell surface proteins including programmed death ligand 1 protein, which is difficult to detect using conventional fluorescent dye-labeled antibodies.


2019 ◽  
Vol 14 (8) ◽  
pp. 1836-1844 ◽  
Author(s):  
Ross W. Cheloha ◽  
Zeyang Li ◽  
Djenet Bousbaine ◽  
Andrew W. Woodham ◽  
Priscillia Perrin ◽  
...  

2005 ◽  
Vol 2 (2) ◽  
pp. 99-104 ◽  
Author(s):  
Irwin Chen ◽  
Mark Howarth ◽  
Weiying Lin ◽  
Alice Y Ting

1971 ◽  
Vol 124 (5) ◽  
pp. 921-927 ◽  
Author(s):  
J J. Marchalonis ◽  
R E. Cone ◽  
V Santer

1. Radioactive iodide was covalently bound to living cells from normal mouse spleen and a variety of lymphoid tumours by a system consisting of lactoperoxidase, hydrogen peroxide and iodide. 2. About 3×105-6×105 molecules of [125I]iodide/cell could be incorporated without affecting cell viability. 3. Electron-micrographic radioautography showed that the radioactive label was associated with the outer surfaces of the cells. 4. Radioiodinated proteins were solubilized in 9m-urea–0.2m-mercaptoethanol and analysed by gel-filtration and disc electrophoresis. 5. Comparison of distinct tumour lines by disc electrophoresis showed qualitative and quantitative differences in protein distribution patterns.


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