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Protein Expression in Mammalian Cells

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Cover of 'Protein Expression in Mammalian Cells'

Table of Contents

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    Book Overview
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    Chapter 1 Why Proteins in Mammalian Cells?
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    Chapter 2 Large-Scale Transfection of Mammalian Cells
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    Chapter 3 Selection of High Expressing Mammalian Cells by Surface Display of Reporters
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    Chapter 4 Expression of a Secreted Protein in Mammalian Cells Using Baculovirus Particles
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    Chapter 5 Transfection of Difficult-to-Transfect Primary Mammalian Cells
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    Chapter 6 Stable Protein Expression in Mammalian Cells Using Baculoviruses
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    Chapter 7 Protein Expression in Mammalian Cells
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    Chapter 8 Protein Expression in Mammalian Cells
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    Chapter 9 Post-transcriptional Regulatory Elements for Enhancing Transient Gene Expression Levels in Mammalian Cells
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    Chapter 10 Protein Expression in Mammalian Cells
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    Chapter 11 Generation of High-Expressing Cells by Methotrexate Amplification of Destabilized Dihydrofolate Reductase Selection Marker
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    Chapter 12 Protein Expression in Mammalian Cells
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    Chapter 13 Identification and characterization of protein glycosylation using specific endo- and exoglycosidases.
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    Chapter 14 Protein Expression in Mammalian Cells
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    Chapter 15 Methods for Constructing Clones for Protein Expression in Mammalian Cells
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    Chapter 16 Optimizing Transient Recombinant Protein Expression in Mammalian Cells
Attention for Chapter 12: Protein Expression in Mammalian Cells
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Chapter title
Protein Expression in Mammalian Cells
Chapter number 12
Book title
Protein Expression in Mammalian Cells
Published in
Methods in molecular biology, September 2011
DOI 10.1007/978-1-61779-352-3_12
Pubmed ID
Book ISBNs
978-1-61779-351-6, 978-1-61779-352-3
Authors

Zahra Assur, Wayne A. Hendrickson, Filippo Mancia

Editors

James L Hartley

Abstract

Structural and functional studies of many mammalian systems are critically dependent on abundant supplies of recombinant multiprotein complexes. Mammalian cells are often the most ideal, if not the only suitable host for such experiments. This is due to their intrinsic capability to generate functional mammalian proteins. This advantage is frequently countered by problems with yields in expression, time required to generate overexpressing lines, and elevated costs. Coexpression of multiple proteins adds another level of complexity to these experiments, as cells need to be screened and selected for expression of suitable levels of each component. Here, we present an efficient fluorescence marking procedure for establishing stable cell lines that overexpress two proteins in coordination, and we validate the method in the production of recombinant monoclonal antibody Fab fragments. This procedure may readily be expanded to systems of greater complexity, comprising more than two components.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 59 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 59 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 15 25%
Student > Ph. D. Student 12 20%
Student > Bachelor 7 12%
Student > Master 4 7%
Professor > Associate Professor 3 5%
Other 7 12%
Unknown 11 19%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 19 32%
Agricultural and Biological Sciences 16 27%
Engineering 3 5%
Chemistry 3 5%
Medicine and Dentistry 2 3%
Other 5 8%
Unknown 11 19%