Cited by 236Viral Infectious Diseases and Gene Expression in InsectsRNA Interference and Gene DeliveryTransgenic Plants and Applications

Large-Scale transfection of mammalian cells for the fast production of recombinant protein

Pham, Phuong Lan, Kamen, Amine, Durocher, Yves·2006·Molecular Biotechnology

Abstract

Recombinant proteins (r-proteins) are increasingly important in fundamental research and for clinical applications. As many of these r-proteins are of human or animal origin, cultivated mammalian cells are the host of choice to ensure their functional folding and proper posttranslational modifications. Large-scale transfection of human embryonic kidney 293 or Chinese hamster ovary cells is now an established technology that can be used in the production of hundreds of milligram to gram quantities of a r-protein in less than 1 mo from cloning of its cDNA. This chapter aims to provide an overview of large-scale transfection technology with a particular emphasis on calcium phosphate and polyethylenimine-mediated gene transfer.

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Crossref · 10.1385/mb:34:2:225

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  • When the need for a quick and economical approach prevails, transient expression remains the best choice for protein production.

    “When the need for a quick and economical approach prevails, transient expression remains the best choice for protein production (Rosser et al., 2005;Pham et al., 2006;Geisse, 2009;Chahal et al., 2011;Baldi et al., 2012).”

    From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Pham et al., 2006

  • The production rate in transient transfection relies on many factors including efficiency of the transfection phase, cytotoxicity of the transfection reagent, and extensiveness of the feeding strategy applied post-transfection.

    “However, the production rate relies on many factors including efficiency of the transfection phase, cytotoxicity of the transfection reagent and extensiveness of the feeding strategy applied to the culture post-transfection (Pham et al., 2006;Daramola et al., 2014).”

    From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Pham et al., 2006

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Authors
Pham, P. L., Kamen, A., & Durocher, Y.
Affiliations
  • Université de Montréal (CA)
  • Biotechnology Research Institute (CA)
Corresponding author
Durocher, Yves
Venue
Molecular Biotechnology
Published
2006
Volume
34
Issue
2
Pages
225-238
ISSN
1073-6085 (ISSN-L)
OpenAlex
W2012250005
Cited by
236
References
119
Citations by year
2026: 1 · 2025: 6 · 2024: 10 · 2023: 6 · 2022: 9 · 2021: 7 · 2020: 21 · 2019: 7 · 2018: 11 · 2017: 8 · 2016: 12 · 2015: 11 · 2014: 22 · 2013: 20 · 2012: 23
FWCI
3.38
Type
journal article
Language
en
Open access
closed
Locations
  • Molecular Biotechnology (publishedVersion)
  • PubMed (publishedVersion)
  • NPARC (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Interference and Gene Delivery
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
Keywords
recombinant protein expression, mammalian cell expression systems, HEK293 cells, CHO cells, calcium phosphate transfection, post-translational modification, cDNA cloning
MeSH terms
Animals, Biotechnology, Calcium Phosphates, Cell Line, Culture Media, Genetic Vectors, Cricetinae, Humans, Polyethyleneimine, Recombinant Proteins, Transfection

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