Mammalian cell factories for efficient and stable protein expression

2006 ◽  
Vol 17 (4) ◽  
pp. 381-386 ◽  
Author(s):  
Louise M Barnes ◽  
Alan J Dickson
Keyword(s):  
Protein Expression ◽  
Mammalian Cell ◽  
Cell Factories

scholarly journals Special Issue: Recombinant Protein Expression in Microorganisms

2019 ◽  
Vol 7 (9) ◽  
pp. 355
Author(s):  
Trygve Brautaset ◽  
Svein Valla
Keyword(s):  
Recombinant Protein ◽  
Protein Expression ◽  
Recombinant Protein Expression ◽  
Sustainable Production ◽  
Industrial Biotechnology ◽  
Special Issue ◽  
Cell Factories ◽  
Wide Range

Microorganisms are widely used in industrial biotechnology as cell factories for the sustainable production of a wide range of compounds and chemicals [...]

Analysis of Protein Expression and Virus-like Particle Formation in Mammalian Cell Lines Stably Expressing HIV-1 gag and env Gene Products with or without Active HIV Proteinase

Virology ◽  
1993 ◽  
Vol 192 (2) ◽  
pp. 605-617 ◽  
Author(s):  
Hans Georg Kräusslich ◽  
Christina Ochsenbauer ◽  
Anke-Mareil Traenckner ◽  
Klaus Mergener ◽  
Michael Fäcke ◽  
...  
Keyword(s):  
Protein Expression ◽  
Cell Lines ◽  
Mammalian Cell ◽  
Particle Formation ◽  
Gene Products ◽  
Mammalian Cell Lines ◽  
Virus Like Particle ◽  
Hiv 1

scholarly journals Mammalian cell-free protein expression promotes the functional characterization of the tripartite non-hemolytic enterotoxin from Bacillus cereus

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Franziska Ramm ◽  
Srujan Kumar Dondapati ◽  
Lena Thoring ◽  
Anne Zemella ◽  
Doreen Anja Wüstenhagen ◽  
...  
Keyword(s):  
Protein Expression ◽  
Bacillus Cereus ◽  
Mammalian Cell ◽  
Functional Characterization ◽  
Free Protein

Vector and Cell Line Engineering Technologies Toward Recombinant Protein Expression in Mammalian Cell Lines

2018 ◽  
Vol 185 (4) ◽  
pp. 986-1003 ◽  
Author(s):  
Seyedeh Hoda Jazayeri ◽  
Amir Amiri-Yekta ◽  
Salahadin Bahrami ◽  
Hamid Gourabi ◽  
Mohammad Hossein Sanati ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Protein Expression ◽  
Cell Line ◽  
Cell Lines ◽  
Mammalian Cell ◽  
Recombinant Protein Expression ◽  
Mammalian Cell Lines ◽  
Line Engineering

scholarly journals Systems biotechnology of mammalian cell factories

2008 ◽  
Vol 7 (2) ◽  
pp. 95-110 ◽  
Author(s):  
P. M. O'Callaghan ◽  
D. C. James
Keyword(s):  
Mammalian Cell ◽  
Systems Biotechnology ◽  
Cell Factories

Droplet size influences division of mammalian cell factories in droplet microfluidic cultivation

2016 ◽  
Vol 38 (2) ◽  
pp. 305-310 ◽  
Author(s):  
Prem Kumar Periyannan Rajeswari ◽  
Haakan N. Joensson ◽  
Helene Andersson-Svahn
Keyword(s):  
Mammalian Cell ◽  
Droplet Size ◽  
Cell Factories

scholarly journals Placing the RPL32 Promoter Upstream of a Second Promoter Results in a Strongly Increased Number of Stably Transfected Mammalian Cell Lines That Display High Protein Expression Levels

2011 ◽  
Vol 2011 ◽  
pp. 1-11 ◽  
Author(s):  
F. Hoeksema ◽  
K. Hamer ◽  
M. Siep ◽  
J. A. Verhees ◽  
A. P. Otte
Keyword(s):  
Protein Expression ◽  
Cell Lines ◽  
Mammalian Cell ◽  
Small Region ◽  
High Protein ◽  
Expression Levels ◽  
Mammalian Cell Lines ◽  
Selection Systems ◽  
In Cis ◽  
Gene Expression Levels

The use of high stringency selection systems commonly results in a strongly diminished number of stably transfected mammalian cell lines. Here we placed twelve different promoters upstream of an adjacent primary promoter and tested whether this might result in an increased number of colonies; this is in the context of a stringent selection system. We found that only the promoter of the human ribosomal protein, RPL32, induced a high number of colonies in CHO-DG44 cells. This phenomenon was observed when the RPL32 promoter was combined with the CMV, SV40, EF1-α, and the β-actin promoters. In addition, these colonies displayed high protein expression levels. The RPL32 promoter had to be functionally intact, since the deletion of a small region upstream of the transcription start site demolished its positive action. We conclude that adding the RPL32 promoter to an expression cassette in cis may be a powerful tool to augment gene expression levels.

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