Advances in animal cell recombinant protein production: GS-NS0 expression system
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The production of recombinant proteins using mammalian cell expression systems is of growing importance within biotechnology, largely due to the ability of specific mammalian cells to carry out post-translational modifications of the correct fidelity. The Glutamine Synthetase-NS0 system is now one such industrially important expression system.Glutamine synthetase catalyses the formation ofglutamine from glutamate and ammonia. NS0 cellscontain extremely low levels of endogenous glutaminesynthetase activity, therefore exogenous glutaminesynthetase can be used efficiently as a selectablemarker to identify successful transfectants in theabsence of glutamine in the media. In addition, theinclusion of methionine sulphoximine, an inhibitor ofglutamine synthetase activity, enables furtherselection of those clones producing relatively highlevels of transfected glutamine synthetase and henceany heterologous gene which is coupled to it. Theglutamine synthetase system technology has been usedfor research and development purposes during thisdecade and its importance is clearly demonstrated nowthat two therapeutic products produced using thissystem have reached the market place.
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Murine myeloma cells (NS0 and Sp2/0) are used to produce commercial monoclonal antibodies such as Cetuximab and Palivizumab.
“Murine myeloma cells (NS0 and Sp2/0), derived from tumor cells that no longer produce their original immunoglobulins, also are being used to produce some commercial monoclonal antibodies such as Cetuximab (ERBITUX ® ) and Palivizumab (SYNAGIS ® ) (Barnes et al., 2000;Dumont et al., 2015).”
From Therapeutic glycoprotein production in mammalian cells (2017) · cites this paper as Barnes et al., 2000
The ‘Products generated using the GS-NS0 system’ section identifies Synagis (palivizumab) as a marketed monoclonal antibody produced using the GS-NS0 system. The ‘NS0 cell history’ section also describes NS0 as a non-secreting murine myeloma line. Our copy does not identify Sp2/0 or Cetuximab, so it does not support those parts of the attributed claim. (LLM, conf=0.89)
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Cites
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Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032 · see citing works
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296 · see citing works
Guidelines to cell engineering for monoclonal antibody production
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Mouse cell line authentication
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- Authors
- Barnes, L. M., Bentley, C. M., & Dickson, A. J.
- Affiliations
- University of Manchester (GB)
- ORCID
- Dickson, Alan J.
- Venue
- Cytotechnology
- Published
- 2000-02
- Volume
- 32
- Issue
- 2
- Pages
- 109-123
- ISSN
- 0920-9069 (ISSN-L)
- 1573-0778
- PMC
- PMC3449689
- OpenAlex
- W1498699116
- Cited by
- 129
- References
- 2
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 1 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 7 · 2017: 6 · 2016: 7 · 2015: 6 · 2014: 6 · 2013: 9 · 2012: 6
- FWCI
- 1.09
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cytotechnology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Directorate for Biological Sciences
- Biotechnology and Biological Sciences Research Council
- 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 › Genetics › Animal Genetics and Reproduction
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Transgenic Plants and Applications
- Keywords
- recombinant protein expression, mammalian cell expression systems, NS0 cells, glutamine synthetase, methionine sulfoximine, post-translational modification, therapeutic proteins
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