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Titlebook: Chaperones; Methods and Protocol Stuart K. Calderwood,Thomas L. Prince Book 2023Latest edition The Editor(s) (if applicable) and The Author

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书目名称Chaperones
副标题Methods and Protocol
编辑Stuart K. Calderwood,Thomas L. Prince
视频videohttp://file.papertrans.cn/224/223941/223941.mp4
概述Includes cutting-edge methods and protocols.Provides step-by-step detail essential for reproducible results.Contains key notes and implementation advice from the experts
丛书名称Methods in Molecular Biology
图书封面Titlebook: Chaperones; Methods and Protocol Stuart K. Calderwood,Thomas L. Prince Book 2023Latest edition The Editor(s) (if applicable) and The Author
描述This second edition volume expands on the previous edition with new discussions on the latest techniques used to study molecular chaperones and the stress response. The chapters in this book cover such as analysis of the initiation and regulation of the stress response; the role of heat shock protein 90 (Hsp90) in gene expression through chromosome-immunoprecipitation; features of chaperone function and biology; the emerging role of the extracellular HSPs; and the use of chaperones as biomarkers. Written in the highly successful .Methods in Molecular Biology. series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls..Cutting-edge and thorough, .Chaperones: Methods and Protocols, Second Edition. is a valuable resource for all researchers who want to learn more about this interesting and developing field. .
出版日期Book 2023Latest edition
关键词FLECS assay; homologous recombination; Hsp90; ChiP assay; protein folding
版次2
doihttps://doi.org/10.1007/978-1-0716-3342-7
isbn_softcover978-1-0716-3344-1
isbn_ebook978-1-0716-3342-7Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightThe Editor(s) (if applicable) and The Author(s), under exclusive license to Springer Science+Busines
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Detecting Posttranslational Modifications of Hsp90 Isoforms,modifications (such as phosphorylation, SUMOylation, and ubiquitination) are important for Hsp90 stability and regulation of its ATPase activity. Both mammalian and yeast cells can be used to express and purify Hsp90 and TRAP1 and also detect post-translational modifications by immunoblotting.
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Book 2023Latest editionps on troubleshooting and avoiding known pitfalls..Cutting-edge and thorough, .Chaperones: Methods and Protocols, Second Edition. is a valuable resource for all researchers who want to learn more about this interesting and developing field. .
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Practical Ajax Projects with Java Technologym isolated nuclei and sheared by sonication. Hsp90-bound loci are immunoprecipitated and the corresponding DNA fragments are purified and sequenced. The described approach revealed that Hsp90 binds close to the transcriptional start site of around one-third of all . coding genes and characterized the role of the chaperone at chromatin.
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