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Titlebook: NADPH Oxidases; Methods and Protocol Ulla G. Knaus,Thomas L. Leto Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2

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書目名稱NADPH Oxidases
副標題Methods and Protocol
編輯Ulla G. Knaus,Thomas L. Leto
視頻videohttp://file.papertrans.cn/661/660013/660013.mp4
概述Includes cutting-edge techniques.Provides step-by-step detail essential for reproducible results.Contains key implementation advice from the experts
叢書名稱Methods in Molecular Biology
圖書封面Titlebook: NADPH Oxidases; Methods and Protocol Ulla G. Knaus,Thomas L. Leto Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2
描述This detailed volume explores the NADPH oxidase family of enzymes in human physiology and genetic disease, in which early discoveries represent prime examples of the finest translational “from bed to bench and back” studies. Methods are included for testing assembly and function of multicomponent oxidase complexes and for analyzing reactive oxygen species (ROS) generation in different systems by various means, while addressing pitfalls of ROS probes currently being used, as well as protocols on NADPH oxidase regulation and their function in cells. Written in the highly successful .Methods in Molecular Biology. series format, chapters include introduction 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.?.Authoritative and cutting-edge, .NADPH Oxidases: Methods and Protocols. will aid researchers working with the NOX/DUOX family in continuing and expanding upon their vital research..
出版日期Book 2019
關鍵詞NOX/DUOX family; Multicomponent oxidase complexes; Genetic diseases; Reactive oxygen species; Oxidase re
版次1
doihttps://doi.org/10.1007/978-1-4939-9424-3
isbn_softcover978-1-4939-9426-7
isbn_ebook978-1-4939-9424-3Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2019
The information of publication is updating

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Insights into the NOX NADPH Oxidases Using Heterologous Whole Cell Assaysof this family of enzymes. These model systems have been used to analyze the biosynthesis and functional domains of NOX enzyme components as well as their regulation and cellular activities. This chapter provides an overview of the basic principles and applications of heterologous whole cell assays in studying NOX NADPH oxidases.
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HPLC-Based Monitoring of Oxidation of Hydroethidine for the Detection of NADPH Oxidase-Derived Superquired for specific detection of the superoxide radical anion. Here, we provide protocols for HPLC- and LC-MS-based quantitation of 2-hydroxyethidium, among other oxidation products. Also, a protocol for continuous sampling for real-time monitoring of superoxide production using rapid HPLC measurements of 2-hydroxyethidium is described.
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NOX5 Cell-Free Assay for the High-Throughput Screening of Small Moleculeseen debated. Here we describe a NOX5 cell-free assay. We present a method to purify the membranous component of cells stably transduced with NOX5 and to measure O.. in a high-throughput format (96-w or 384-w plates). The experimental description allows high-throughput screening of small molecules with limited cost.
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Soluble Regulatory Proteins for Activation of NOX Family NADPH Oxidasesvation prefers NOXO1 and NOXA1, although Rac is also involved. NOX3 constitutively produces superoxide, which is enhanced by regulatory proteins such as p47., NOXO1, and p67.. Here we describe mechanisms for NOX activation with special attention to the soluble regulatory proteins.
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