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A general fluorescent light-up probe for staining and quantifying protein

Proteins are the primary functional agents in all cellular processes, facilitating various functions such as enzymes and structure-forming or signal-transducing molecules. In this work, we report a fluorescent dye, PyMDI-Zn, which could specifically bind with proteins and provide a red-shifted fluor...

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Detalles Bibliográficos
Autores principales: Zou, Jiawei, Chen, Gangyi, Du, Feng, Yuan, Yi, Huang, Xin, Dong, Juan, Xie, Kexin, Cui, Xin, Tang, Zhuo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6731743/
https://www.ncbi.nlm.nih.gov/pubmed/31598246
http://dx.doi.org/10.1098/rsos.190580
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author Zou, Jiawei
Chen, Gangyi
Du, Feng
Yuan, Yi
Huang, Xin
Dong, Juan
Xie, Kexin
Cui, Xin
Tang, Zhuo
author_facet Zou, Jiawei
Chen, Gangyi
Du, Feng
Yuan, Yi
Huang, Xin
Dong, Juan
Xie, Kexin
Cui, Xin
Tang, Zhuo
author_sort Zou, Jiawei
collection PubMed
description Proteins are the primary functional agents in all cellular processes, facilitating various functions such as enzymes and structure-forming or signal-transducing molecules. In this work, we report a fluorescent dye, PyMDI-Zn, which could specifically bind with proteins and provide a red-shifted fluorescent emission. The visual analysis of protein in sodium dodecyl sulfate-polyacrylamide gel electrophoresis could be realized in 5 min by using PyMDI-Zn as a light-up dye. Based on its cell penetration and low toxicity, PyMDI-Zn could also be applied to locate protein-rich regions and organelles in live cell imaging. Moreover, the direct protein quantitation can be realized based on PyMDI-Zn, providing a method of screening for food adulteration by nitrogen-rich compounds.
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spelling pubmed-67317432019-10-09 A general fluorescent light-up probe for staining and quantifying protein Zou, Jiawei Chen, Gangyi Du, Feng Yuan, Yi Huang, Xin Dong, Juan Xie, Kexin Cui, Xin Tang, Zhuo R Soc Open Sci Cellular and Molecular Biology Proteins are the primary functional agents in all cellular processes, facilitating various functions such as enzymes and structure-forming or signal-transducing molecules. In this work, we report a fluorescent dye, PyMDI-Zn, which could specifically bind with proteins and provide a red-shifted fluorescent emission. The visual analysis of protein in sodium dodecyl sulfate-polyacrylamide gel electrophoresis could be realized in 5 min by using PyMDI-Zn as a light-up dye. Based on its cell penetration and low toxicity, PyMDI-Zn could also be applied to locate protein-rich regions and organelles in live cell imaging. Moreover, the direct protein quantitation can be realized based on PyMDI-Zn, providing a method of screening for food adulteration by nitrogen-rich compounds. The Royal Society 2019-08-28 /pmc/articles/PMC6731743/ /pubmed/31598246 http://dx.doi.org/10.1098/rsos.190580 Text en © 2019 The Authors. http://creativecommons.org/licenses/by/4.0/ Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/4.0/, which permits unrestricted use, provided the original author and source are credited.
spellingShingle Cellular and Molecular Biology
Zou, Jiawei
Chen, Gangyi
Du, Feng
Yuan, Yi
Huang, Xin
Dong, Juan
Xie, Kexin
Cui, Xin
Tang, Zhuo
A general fluorescent light-up probe for staining and quantifying protein
title A general fluorescent light-up probe for staining and quantifying protein
title_full A general fluorescent light-up probe for staining and quantifying protein
title_fullStr A general fluorescent light-up probe for staining and quantifying protein
title_full_unstemmed A general fluorescent light-up probe for staining and quantifying protein
title_short A general fluorescent light-up probe for staining and quantifying protein
title_sort general fluorescent light-up probe for staining and quantifying protein
topic Cellular and Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6731743/
https://www.ncbi.nlm.nih.gov/pubmed/31598246
http://dx.doi.org/10.1098/rsos.190580
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