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Titlebook: Galectins; Methods and Protocol Sean R. Stowell,Connie M. Arthur,Richard D. Cummin Book 2022Latest edition Springer Science+Business Media,

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發(fā)表于 2025-3-21 16:18:51 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書(shū)目名稱(chēng)Galectins
副標(biāo)題Methods and Protocol
編輯Sean R. Stowell,Connie M. Arthur,Richard D. Cummin
視頻videohttp://file.papertrans.cn/381/380370/380370.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
叢書(shū)名稱(chēng)Methods in Molecular Biology
圖書(shū)封面Titlebook: Galectins; Methods and Protocol Sean R. Stowell,Connie M. Arthur,Richard D. Cummin Book 2022Latest edition Springer Science+Business Media,
描述.This second edition is dedicated to new and updated methodological approaches designed to study galectin function. Chapters examine salient features of galectin functions. Written in the 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 protocols, and notes on troubleshooting and avoiding known pitfalls...?Authoritative and cutting-edge,?Galectins: Methods and Protocols, Second Eidtion aims to be a?useful practical guide to researches to help further their study in this field.?..?.
出版日期Book 2022Latest edition
關(guān)鍵詞oxidative inactivation; thermodynamics; glycan microarrays; neoplastic disease; cancer cells
版次2
doihttps://doi.org/10.1007/978-1-0716-2055-7
isbn_softcover978-1-0716-2057-1
isbn_ebook978-1-0716-2055-7Series ISSN 1064-3745 Series E-ISSN 1940-6029
issn_series 1064-3745
copyrightSpringer Science+Business Media, LLC, part of Springer Nature 2022
The information of publication is updating

書(shū)目名稱(chēng)Galectins影響因子(影響力)




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書(shū)目名稱(chēng)Galectins網(wǎng)絡(luò)公開(kāi)度




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Rapid Detection and Purification of Galectin-3 by the ,pture and ,lease (CaRe) Method, glycoproteins in those processes, it is essential to detect these proteins in biological samples and purify them to homogeneity. Conventional protein detection and purification techniques are multi-step, time-intensive, and expensive. They often require rigorous trial and error experimentations and
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,Introducing 77Se NMR Spectroscopy to Analyzing Galectin –Ligand Interaction,mer(s) of their ligands in solution. Basically, NMR spectroscopy facilitates respective experiments. Towards developing new and even better approaches for these purposes, extending the range of exploitable isotopes beyond .H, .C, and .N offers promising perspectives. Having therefore prepared seleno
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Evaluation of Galectin Binding by Surface Plasmon Resonance,sensitivity and low sample consumption in the Biacore enables the measurement of rapid kinetics and low affinities characteristics of many biological interactions. This chapter describes the affinity measurement of Galectins-1, -2 and -3 and their glycoside ligands using this approach.
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Mechanism of Mucin Recognition by Lectins : A Thermodynamic Study,stant, binding stoichiometry, heat of binding (enthalpy) and indirectly the entropy, and free energy of binding. ITC has been extensively used to study the binding of lectins to mono- and oligosaccharides, but limitedly in applications to lectin–glycoprotein interactions. Inherent experimental chall
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