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Recombinant Protein Expression in Mammalian Cells

Overview of attention for book
Cover of 'Recombinant Protein Expression in Mammalian Cells'

Table of Contents

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    Book Overview
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    Chapter 1 Transient Gene Expression in Suspension HEK293-EBNA1 Cells
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    Chapter 2 Transient Expression of Recombinant Membrane-eGFP Fusion Proteins in HEK293 Cells
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    Chapter 3 PEI-Mediated Transient Gene Expression in CHO Cells
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    Chapter 4 Stable Expression by Lentiviral Transduction of Cells
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    Chapter 5 Inducible Protein Production in 293 Cells Using the piggyBac Transposon System
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    Chapter 6 Recombinant CHO Cell Pool Generation Using piggyBac Transposon System
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    Chapter 7 Genome Engineering of Hybridomas to Generate Stable Cell Lines for Antibody Expression
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    Chapter 8 Protein Expression via Transient Transfection of Mammalian Cells in a WAVE Bioreactor
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    Chapter 9 CHO and HEK293 Cultivation and Transfection in Single-Use Orbitally Shaken Bioreactors
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    Chapter 10 Bench-Scale Stirred-Tank Bioreactor for Recombinant Protein Production in Chinese Hamster Ovary (CHO) Cells in Suspension
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    Chapter 11 Continuous and Integrated Expression and Purification of Recombinant Antibodies
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    Chapter 12 High Throughput Transfection of HEK293 Cells for Transient Protein Production
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    Chapter 13 Microfluidic Transfection for High-Throughput Mammalian Protein Expression
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    Chapter 14 Genome-Wide High-Throughput RNAi Screening for Identification of Genes Involved in Protein Production
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    Chapter 15 Targeting miRNAs with CRISPR/Cas9 to Improve Recombinant Protein Production of CHO Cells
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    Chapter 16 Application of the CRISPR/Cas9 Gene Editing Method for Modulating Antibody Fucosylation in CHO Cells
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    Chapter 17 Scalable Production and Purification of Adeno-Associated Viral Vectors (AAV)
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    Chapter 18 Considerations in the Use of Codon Optimization for Recombinant Protein Expression
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    Chapter 19 Versatile Cell-Free Protein Synthesis Systems Based on Chinese Hamster Ovary Cells
Attention for Chapter 17: Scalable Production and Purification of Adeno-Associated Viral Vectors (AAV)
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Chapter title
Scalable Production and Purification of Adeno-Associated Viral Vectors (AAV)
Chapter number 17
Book title
Recombinant Protein Expression in Mammalian Cells
Published in
Methods in molecular biology, September 2018
DOI 10.1007/978-1-4939-8730-6_17
Pubmed ID
30242692
Book ISBNs
978-1-4939-8729-0, 978-1-4939-8730-6
Authors

Daniel Blessing, Nicole Déglon, Bernard L. Schneider, Blessing, Daniel, Déglon, Nicole, Schneider, Bernard L.

Abstract

Here we describe methods for the production of adeno-associated viral (AAV) vectors by transient transfection of HEK293 cells grown in serum-free medium in orbital shaken bioreactors and the subsequent purification of vector particles. The protocol for expression of AAV components is based on polyethyleneimine (PEI) mediated transfection of a 2-plasmid system and is specified for production in milliliter to liter scales. After PEI and plasmid DNA (pDNA) complex formation the diluted cell culture is transfected without a prior concentration step or medium exchange. Following a 3-day batch process, cell cultures are further processed using different methods for lysis and recovery. Methods for the purification of viral particles are described, including iodixanol gradient purification, immunoaffinity chromatography, and ultrafiltration, as well as quantitative PCR to quantify vector titer.

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X Demographics

The data shown below were collected from the profile of 1 X user who shared this research output. Click here to find out more about how the information was compiled.
 Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 40 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 40 100%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 10 25%
Researcher 6 15%
Student > Bachelor 5 13%
Student > Master 4 10%
Other 3 8%
Other 2 5%
Unknown 10 25%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 12 30%
Agricultural and Biological Sciences 5 13%
Engineering 4 10%
Chemical Engineering 2 5%
Chemistry 2 5%
Other 3 8%
Unknown 12 30%
Attention Score in Context

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 20 March 2019.
All research outputs
#18,649,666
of 23,103,903 outputs
Outputs from Methods in molecular biology
#7,996
of 13,222 outputs
Outputs of similar age
#261,042
of 340,695 outputs
Outputs of similar age from Methods in molecular biology
#150
of 235 outputs
Altmetric has tracked 23,103,903 research outputs across all sources so far. This one is in the 11th percentile – i.e., 11% of other outputs scored the same or lower than it.
So far Altmetric has tracked 13,222 research outputs from this source. They receive a mean Attention Score of 3.4. This one is in the 24th percentile – i.e., 24% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 340,695 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 13th percentile – i.e., 13% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 235 others from the same source and published within six weeks on either side of this one. This one is in the 25th percentile – i.e., 25% of its contemporaries scored the same or lower than it.

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