Method to Assess the Intracellular Fate and Bioavailability of Clusterin Using Live Cell Confocal Microscopy Imaging.
Autor: | Soundararajan A; Department of Ophthalmology, Glick Eye Institute, Indiana University School of Medicine, Indianapolis, IN, USA., Pattabiraman PP; Department of Ophthalmology, Glick Eye Institute, Indiana University School of Medicine, Indianapolis, IN, USA. ppattabi@iu.edu.; Stark Neuroscience Research Institute, Indiana University School of Medicine, Indianapolis, IN, USA. ppattabi@iu.edu. |
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Jazyk: | angličtina |
Zdroj: | Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2024; Vol. 2816, pp. 145-149. |
DOI: | 10.1007/978-1-0716-3902-3_14 |
Abstrakt: | Clusterin, also known as apolipoprotein J, is an ATP-independent holdase chaperone protein. Clusterin is involved in various functions including protein quality control and lipid transport. Though clusterin is secreted upon stress, the intracellular fate of clusterin after a stress response is not well understood. The protocol described here utilizes clusterin tagged to fluorescent proteins like green fluorescent protein and red fluorescent protein to understand the intracellular fate of clusterin. (© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.) |
Databáze: | MEDLINE |
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