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Titlebook: Electrophoretic Separation of Proteins; Methods and Protocol Biji T. Kurien,R. Hal Scofield Book 2019 Springer Science+Business Media, LLC,

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發(fā)表于 2025-3-21 18:19:50 | 只看該作者 |倒序?yàn)g覽 |閱讀模式
書(shū)目名稱(chēng)Electrophoretic Separation of Proteins
副標(biāo)題Methods and Protocol
編輯Biji T. Kurien,R. Hal Scofield
視頻videohttp://file.papertrans.cn/307/306513/306513.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: Electrophoretic Separation of Proteins; Methods and Protocol Biji T. Kurien,R. Hal Scofield Book 2019 Springer Science+Business Media, LLC,
描述This volume expands upon?.Protein Electrophoresis. (2012) and provides readers with easy-to-follow and reproducible methods to study electrophoresis. The chapters in this book cover topics such as the Cydex Blue assay; cellulose-acetate electrophoresis of hemoglobin; cationic electrophoresis; tricine-SDS-Page; identification of proteins on archived 2-D gels; cell surface protein biotinylation of SDS-PAGE analysis; and artifacts and common errors in protein gel electrophoresis. 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..Practical and thorough, .Electrophoretic Separation of Proteins: Methods and Protocols. is a valuable resource for researchers who are interested in learning and experimenting with this field..
出版日期Book 2019
關(guān)鍵詞gel-electrophoresis; homogenization; Lysis Buffer; PAGE; PEGylated Proteins
版次1
doihttps://doi.org/10.1007/978-1-4939-8793-1
isbn_ebook978-1-4939-8793-1Series 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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Measuring Protein Concentration with Absorbance, Lowry, Bradford Coomassie Blue, or the Smith Bicinn procedures. Decisions on the usefulness of any protein isolation procedure depend on knowing the concentration of proteins before and after a procedure. Protein concentration in solution is generally measured with spectrophotometry in the UV range or in the presence of dyes or copper interacting w
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Concentrating Proteins by Salt, Polyethylene Glycol, Solvent, SDS Precipitation, Three-Phase Partitd undesirable molecules, to separate protein fractions, or to increase protein concentrations. Proteins can be concentrated by precipitation from solution with ammonium sulfate, polyethylene glycol, organic solvents, trichloroacetic acid, potassium chloride/sodium dodecyl sulfate thermal denaturatio
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Lysis Buffer Choices Are Key Considerations to Ensure Effective Sample Solubilization for Protein Eocal adhesion protein Kindlin-2 and the transcriptional repressor Snail from choriocarcinoma cells using NP-40 and RIPA lysis buffer. We also show the use of a more denaturing urea/thiourea lysis buffer for solubilization, by comparing its effectiveness with the often utilized RIPA lysis buffer for
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The Cydex Blue Assay: A One-Step Protein Assay for Samples Prior to SDS Electrophoresis,d reducers in the buffers used for protein extraction. Reducers interfere with the copper-based assays, while SDS interferes with the dye-binding assays. The combined use of cyclodextrins with a commercial Bradford reagent concentrate, described in this chapter, allows to determine protein concentra
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Cellulose Acetate Electrophoresis of Hemoglobin,t other than electrophoresis apparatus and the cellulose acetate strip. Here we describe a modified version of cellulose acetate membrane electrophoresis for hemoglobin separation from blood sample. Sharp, clear bands without tailing effects can be obtained with this method. The method and apparatus
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Native Polyacrylamide Gels,) reducing conditions. The most commonly used detergent is sodium dodecyl sulfate (SDS). The major function of SDS is to shield the respective charge of the proteins present in the mixture to be analyzed and to provide all proteins with a negative charge. As a consequence, the proteins will be separ
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Isoelectric Focusing on Non-Denaturing Flatbed Gels,ody clonotype changes. Here we discuss the use of a sensitive native flatbed isoelectric focusing method to analyze specific antibody clonotype changes in a patient with systemic lupus erythematosus, who developed autoantibodies to the Ro 60 autoantigen under observation. Patient sera samples collec
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Determination of Protein Molecular Weights on SDS-PAGE,odium dodecyl sulfate (SDS) separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). This method was established around 1969 and has been utilized substantially even today because of its simplicity. During the following half a century, although it has been reported that man
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