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Protein Chromatography

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Cover of 'Protein Chromatography'

Table of Contents

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    Book Overview
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    Chapter 1 A Synopsis of Proteins and Their Purification.
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    Chapter 2 Gel-Filtration Chromatography.
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    Chapter 3 Immunoaffinity Chromatography: Concepts and Applications.
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    Chapter 4 Avoiding Proteolysis During Protein Purification.
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    Chapter 5 Scale-Up of Protein Purification: Downstream Processing Issues.
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    Chapter 6 Phage Display: A Powerful Technology for the Generation of High-Specificity Affinity Reagents from Alternative Immune Sources.
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    Chapter 7 Protein Stability: Enhancement and Measurement.
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    Chapter 8 Tagging Recombinant Proteins to Enhance Solubility and Aid Purification.
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    Chapter 9 Storage and Lyophilization of Pure Proteins.
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    Chapter 10 Differential Precipitation and Solubilization of Proteins.
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    Chapter 11 Ion-Exchange Chromatography: Basic Principles and Application.
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    Chapter 12 Protein Quantitation and Analysis of Purity.
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    Chapter 13 Purification of Proteins Fused to Maltose-Binding Protein.
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    Chapter 14 Purification of Polyhistidine-Tagged Proteins.
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    Chapter 15 Purification of Antibodies Using Affinity Chromatography.
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    Chapter 16 Optimized Generation of High-Affinity, High-Specificity Single-Chain Fv Antibodies from Multi-Antigen Immunized Chickens.
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    Chapter 17 Measuring Protein-Protein Interactions Using Biacore.
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    Chapter 18 Hydrophobic Interaction Chromatography.
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    Chapter 19 Fast Protein Liquid Chromatography.
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    Chapter 20 Clinical Proteomics: Liquid Chromatography-Mass Spectrometry (LC-MS) Purification Systems.
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    Chapter 21 Strategies for the Purification of Membrane Proteins.
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    Chapter 22 Antimicrobial Peptide Production and Purification.
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    Chapter 23 Lectin Affinity Chromatography (LAC).
Attention for Chapter 14: Purification of Polyhistidine-Tagged Proteins.
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Chapter title
Purification of Polyhistidine-Tagged Proteins.
Chapter number 14
Book title
Protein Chromatography
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-6412-3_14
Pubmed ID
Book ISBNs
978-1-4939-6410-9, 978-1-4939-6412-3
Authors

Sinéad T. Loughran, Ronan T. Bree, Dermot Walls

Editors

Dermot Walls, Sinéad T. Loughran

Abstract

His-tagging is the most widespread and versatile strategy used to purify recombinant proteins for biochemical and structural studies. Recombinant DNA methods are first used to engineer the addition of a short tract of poly-histidine tag (His-tag) to the N-terminus or C-terminus of a target protein. The His-tag is then exploited to enable purification of the "tagged" protein by Immobilized Metal Affinity Chromatography (IMAC). Here, we describe efficient procedures for the isolation of highly purified His-tagged target proteins from an E. coli host using IMAC.

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Mendeley readers

The data shown below were compiled from readership statistics for 120 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 120 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 36 30%
Student > Ph. D. Student 12 10%
Other 8 7%
Student > Master 8 7%
Professor 3 3%
Other 11 9%
Unknown 42 35%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 41 34%
Agricultural and Biological Sciences 14 12%
Engineering 5 4%
Chemistry 4 3%
Neuroscience 3 3%
Other 8 7%
Unknown 45 38%