ArticleProtein science : a publication of the Protein Society2014
Over-expression of secreted proteins from mammalian cell lines.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
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- Arrhythmogenic Cardiomyopathy: from Preclinical Models to Genotype-phenotype Correlation and Pathophysiology.Stem cell reviews and reports · 2023Review
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- Construction and application of a multifunctional CHO cell platform utilizing Cre/Frontiers in bioengineering and biotechnology · 2023Article
- Venom biotechnology: casting light on nature's deadliest weapons using synthetic biology.Frontiers in bioengineering and biotechnology · 2023Review
- A Bench-Top Approach for Isolation of Single Antibody Producing Chinese Hamster Ovary (CHO) Cells Using a Microwell-Based Microfluidic Device.Micromachines · 2022Article
- Harnessing secretory pathway differences between HEK293 and CHO to rescue production of difficult to express proteins.Metabolic engineering · 2022Article
- Zika Virus Envelope Protein Domain III Produced inDiagnostics (Basel, Switzerland) · 2022Article
- Stabilizing and Anti-Repressor Elements Effectively Increases Transgene Expression in Transfected CHO Cells.Frontiers in bioengineering and biotechnology · 2022Article
- Progress of Transposon Vector System for Production of Recombinant Therapeutic Proteins in Mammalian Cells.Frontiers in bioengineering and biotechnology · 2022Review
- Mammalian Cell Culture as a Platform for Veterinary Vaccines.Methods in molecular biology (Clifton, N.J.) · 2022Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Secreted mammalian proteins require the development of robust protein over-expression systems for crystallographic and biophysical studies of protein function. Due to complex disulfide bonds and distinct glycosylation patterns preventing folding and expression in prokaryotic expression hosts, many secreted proteins necessitate production in more complex eukaryotic expression systems. Here, we elaborate on the methods used to obtain high yields of purified secreted proteins from transiently or stably transfected mammalian cell lines. Among the issues discussed are the selection of appropriate expression vectors, choice of signal sequences for protein secretion, availability of fusion tags for enhancing protein stability and purification, choice of cell line, and the large-scale growth of cells in a variety of formats.
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