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Heterologous Gene Expression in E.coli

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Cover of 'Heterologous Gene Expression in E.coli'

Table of Contents

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    Book Overview
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    Chapter 1 Recombinant Protein Expression in E. coli : A Historical Perspective
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    Chapter 2 N- and C-Terminal Truncations to Enhance Protein Solubility and Crystallization: Predicting Protein Domain Boundaries with Bioinformatics Tools
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    Chapter 3 Harnessing the Profinity eXact™ System for Expression and Purification of Heterologous Proteins in E. coli
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    Chapter 4 ESPRIT: A Method for Defining Soluble Expression Constructs in Poorly Understood Gene Sequences
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    Chapter 5 Optimizing Expression and Solubility of Proteins in E. coli Using Modified Media and Induction Parameters
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    Chapter 6 Optimization of Membrane Protein Production Using Titratable Strains of E. coli
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    Chapter 7 Optimizing E. coli-Based Membrane Protein Production Using Lemo21(DE3) or pReX and GFP-Fusions
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    Chapter 8 High Yield of Recombinant Protein in Shaken E. coli Cultures with Enzymatic Glucose Release Medium EnPresso B
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    Chapter 9 A Generic Protocol for Purifying Disulfide-Bonded Domains and Random Protein Fragments Using Fusion Proteins with SUMO3 and Cleavage by SenP2 Protease
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    Chapter 10 A Strategy for Production of Correctly Folded Disulfide-Rich Peptides in the Periplasm of E. coli
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    Chapter 11 Split GFP Complementation as Reporter of Membrane Protein Expression and Stability in E. coli: A Tool to Engineer Stability in a LAT Transporter
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    Chapter 12 Acting on Folding Effectors to Improve Recombinant Protein Yields and Functional Quality
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    Chapter 13 Protein Folding Using a Vortex Fluidic Device
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    Chapter 14 Removal of Affinity Tags with TEV Protease
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    Chapter 15 Generation of Recombinant N-Linked Glycoproteins in E. coli
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    Chapter 16 Production of Protein Kinases in E. coli
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    Chapter 17 Expression of Prokaryotic Integral Membrane Proteins in E. coli
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    Chapter 18 Multiprotein Complex Production in E. coli: The SecYEG-SecDFYajC-YidC Holotranslocon
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    Chapter 19 Membrane Protein Production in E. coli Lysates in Presence of Preassembled Nanodiscs
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    Chapter 20 Not Limited to E. coli: Versatile Expression Vectors for Mammalian Protein Expression
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    Chapter 21 A Generic Protocol for Intracellular Expression of Recombinant Proteins in Bacillus subtilis
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    Chapter 22 In Vivo Biotinylation of Antigens in E. coli
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    Chapter 23 Cold-Shock Expression System in E. coli for Protein NMR Studies
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    Chapter 24 High-Throughput Production of Proteins in E. coli for Structural Studies
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    Chapter 25 Mass Spectrometric Analysis of Proteins
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    Chapter 26 How to Determine Interdependencies of Glucose and Lactose Uptake Rates for Heterologous Protein Production with E. coli
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    Chapter 27 Interfacing Biocompatible Reactions with Engineered Escherichia coli
Attention for Chapter 3: Harnessing the Profinity eXact™ System for Expression and Purification of Heterologous Proteins in E. coli
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Chapter title
Harnessing the Profinity eXact™ System for Expression and Purification of Heterologous Proteins in E. coli
Chapter number 3
Book title
Heterologous Gene Expression in E.coli
Published in
Methods in molecular biology, January 2017
DOI 10.1007/978-1-4939-6887-9_3
Pubmed ID
28470597
Book ISBNs
978-1-4939-6885-5, 978-1-4939-6887-9
Authors

Yoav Peleg, Vadivel Prabahar, Dominika Bednarczyk, Tamar Unger

Editors

Nicola A. Burgess-Brown

Abstract

Highly purified recombinant proteins in large quantities are valuable material for biochemical and structural studies. To achieve this goal, versatile tools were developed to increase the expression of the recombinant proteins and to facilitate the purification process. Fusion tags are commonly used for enhancing expression and solubility and some can be used in the purification process. However, these tags may need to be removed by treatment with specific proteases in order to obtain the tag-free protein. The Profinity eXact™ system provides an alternative system for a fusion tag, enhancing expression and purification in one-step. Here we describe a set of new vectors in which the Profinity eXact™ tag, in addition to a 6× His-tag, with or without additional expression-enhancing sequences, could be used in the Profinity eXact™ system. We show that the solubility enhancing tags (Trx, GST, GB1) increase the yield of the purified tested protein compared to the vector containing only a His-tag upstream of the Profinity eXact™ fusion tag.

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Mendeley readers

The data shown below were compiled from readership statistics for 9 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 9 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 3 33%
Student > Ph. D. Student 2 22%
Student > Bachelor 2 22%
Student > Master 1 11%
Unknown 1 11%
Readers by discipline Count As %
Agricultural and Biological Sciences 4 44%
Biochemistry, Genetics and Molecular Biology 2 22%
Pharmacology, Toxicology and Pharmaceutical Science 1 11%
Chemistry 1 11%
Unknown 1 11%

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