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Laboratory methods in enzymology. Volume 541, Protein, Part C
Title
Laboratory methods in enzymology. Volume 541, Protein, Part C / edited by Jon Lorsch.
ISBN
9780124201781
0124201784
1306540887
9781306540889
9780124201194
0124201199
Publication
Amsterdam : Elsevier/Academic Press, 2014.
Physical Description
1 online resource (xvii, 272 pages) : illustrations (black and white).
Local Notes
Access is available to the Yale community.
Access and use
Access restricted by licensing agreement.
Summary
In this volume we have brought together a number of core protocols concentrating on Protein, carefully written and edited by experts.
Variant and related titles
Protein
Elsevier ScienceDirect All Books. OCLC KB.
Other formats
Print version: Lorsch, Jon. Laboratory Methods in Enzymology. Academic Press 2014
Format
Books / Online
Language
English
Added to Catalog
May 17, 2018
Series
Methods in enzymology, volume 541
Bibliography
Includes bibliographical references and index.
Contents
Front Cover; Laboratory Methods in Enzymology: Protein Part C; Copyright; Contents; Contributors; Miscellaneous; Preface; Section I: Protein Protocols/Protein Precipitation; Chapter One: TCA Precipitation; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions and buffers; 4. Protocol; 4.1. Preparation; 4.2. Duration; 4.3. Caution; 5. Step 1A Trichloroacetic Acid Precipitation; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 5.5. Tip; 6. Step 1B Deoxycholate-Trichloroacetic Acid Precipitation; 6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip; 6.5. Tip; References.
Referenced Protocols in Methods NavigatorSection II: Protein Protocols/Protein Pull-Down Methods; Chapter Two: Coimmunoprecipitation of Proteins from Yeast; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions and buffers; 4. Protocol; 4.1. Duration; 4.2. Preparation; 5. Step 1 Preparation of Whole Cell Lysates; 5.1. Overview; 5.2. Duration; 6. Step 2 Normalization of Cell Lysates; 6.1. Overview; 6.2. Duration; 6.3. Tip; 7. Step 3 Coimmunoprecipitation; 7.1. Overview; 7.2. Duration; 7.3. Tip; 7.4. Tip; 7.5. Tip; 7.6. Tip; 7.7. Tip; 7.8. Tip; 7.9. Note.
8. Step 4 Wash and Elute the Immunoprecipitates8.1. Overview; 8.2. Duration; 8.3. Tip; 8.4. Tip; 9. Step 5 Analysis of Immunoprecipitations; 9.1. Overview; 9.2. Duration; References; Referenced Literature; Related Literature; Referenced Protocols in Methods Navigator; Chapter Three: Coupling Antibody to Cyanogen Bromide-Activated Sepharose; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions and buffers; 4. Protocol; 4.1. Duration; 4.2. Preparation; 5. Step 1 Preparation of Antibody and Resin; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 5.5. Tip; 5.6. Tip.
6. Step 2 Coupling the Antibody to the Resin6.1. Overview; 6.2. Duration; 6.3. Tip; 7. Step 3 Quench the Reaction; 7.1. Overview; 7.2. Duration; 7.3. Tip; 8. Step 4 Wash the Resin; 8.1. Overview; 8.2. Duration; References; Referenced Protocols in Methods Navigator; Chapter Four: Analysis of Protein-Protein Interactions by Coimmunoprecipitation; 1. Theory; 2. Equipment; 3. Materials; 3.1. Solutions and buffers; 4. Protocol; 4.1. Preparation; 4.2. Duration; 5. Step 1 Isolation of the Protein of Interest by Immunoprecipitation; 5.1. Overview; 5.2. Duration; 5.3. Tip; 5.4. Tip; 5.5. Tip.
6. Step 2 Detection of the Binding Partner by Immunoblotting6.1. Overview; 6.2. Duration; 6.3. Tip; 6.4. Tip; References; Referenced Literature; Referenced Protocols in Methods Navigator; Section III: Protein Protocols/Protein Purification; Chapter Five: Use and Application of Hydrophobic Interaction Chromatography for Protein Purification; 1. Theory; 1.1. Latest technology in HIC adsorbents; 1.2. Advantages and disadvantages of using HIC; 2. Equipment; 3. Materials; 3.1. Solutions and buffers; 3.2. Preparation; 4. Protocol; 4.1. Preparation; 4.2. Duration; 5. Step 1 Column Equilibration.
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