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Protein Affinity Tags

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Cover of 'Protein Affinity Tags'

Table of Contents

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    Book Overview
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    Chapter 1 1D4: A Versatile Epitope Tag for the Purification and Characterization of Expressed Membrane and Soluble Proteins
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    Chapter 2 Affinity Purification of Heme-Tagged Proteins
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    Chapter 3 Purification of a recombinant protein with cellulose-binding module 3 as the affinity tag.
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    Chapter 4 Purification of E. coli Proteins Using a Self-Cleaving Chitin-Binding Affinity Tag
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    Chapter 5 Simplified Protein Purification Using an Autoprocessing, Inducible Enzyme Tag
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    Chapter 6 SUMO as a Solubility Tag and In Vivo Cleavage of SUMO Fusion Proteins with Ulp1.
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    Chapter 7 Rescuing Aggregation-Prone Proteins in Escherichia coli with a Dual His6-MBP Tag.
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    Chapter 8 Expression, Purification, and Immobilization of Recombinant Tamavidin 2 Fusion Proteins
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    Chapter 9 Use of Tandem Affinity Chromatography for Purification of Cannabinoid Receptor CB 2
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    Chapter 10 Detection of protein-protein interactions using tandem affinity purification.
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    Chapter 11 An Improved In Vivo Biotinylation Strategy Combined with FLAG and Antibody Based Approaches for Affinity Purification of Protein Complexes in Mouse Embryonic Stem Cells
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    Chapter 12 Purification of Recombinant Proteins with a Multifunctional GFP Tag
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    Chapter 13 Targeted Purification of SnAvi-Tagged Proteins
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    Chapter 14 An efficient fluorescent protein-based multifunctional affinity purification approach in Mammalian cells.
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    Chapter 15 Bimolecular Affinity Purification: A Variation of TAP with Multiple Applications
Attention for Chapter 14: An efficient fluorescent protein-based multifunctional affinity purification approach in Mammalian cells.
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Chapter title
An efficient fluorescent protein-based multifunctional affinity purification approach in Mammalian cells.
Chapter number 14
Book title
Protein Affinity Tags
Published in
Methods in molecular biology, June 2014
DOI 10.1007/978-1-4939-1034-2_14
Pubmed ID
Book ISBNs
978-1-4939-1033-5, 978-1-4939-1034-2
Authors

Ma H, McLean JR, Gould KL, McCollum D, Hanhui Ma, Janel R. McLean, Kathleen L. Gould, Dannel McCollum

Abstract

Knowledge of an individual protein's modifications, binding partners, and localization is essential for understanding complex biological networks. We recently described a fluorescent protein-based (mVenus) multifunctional affinity purification (MAP) tag that can be used both to purify a given protein and determine its localization (Ma et al., Mol Cell Proteomics 11:501-511, 2012). MAP purified protein complexes can be further analyzed to identify binding partners and posttranslational modifications by LC-MS/MS. The MAP approach offers rapid FACS-selection of stable clonal cell lines based on the expression level/fluorescence of the MAP-protein fusion. The MAP tag is highly efficient and shows little variability between proteins. Here we describe the general MAP purification method in detail, and show how it can be applied to a specific protein using the human Cdc14B phosphatase as an example.

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The data shown below were compiled from readership statistics for 2 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 2 100%

Demographic breakdown

Readers by professional status Count As %
Professor > Associate Professor 1 50%
Student > Master 1 50%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 1 50%
Agricultural and Biological Sciences 1 50%

Attention Score in Context

This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 13 February 2015.
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