Specific factors determine successful protein expression in E coli
Specific factors such as host strain, growth temperature, media composition, induction parameters, and fusion tags heavily determine the success and solubility of recombinant protein expression in E. coli.
The claim is specific, empirical, and testable. Multiple retrieved papers explicitly investigate and establish that environmental, genetic, and operational factors govern recombinant protein expression and solubility in Escherichia coli.
Tao-Ho Chang. Protocol for Recombinant Protein Expression in Escherichia coli (BL21) with Variable Antibiotics v1. 2025. https://doi.org/10.17504/protocols.io.5qpvoo579v4o/v1
This protocol outlines specific culture conditions, antibiotics, and induction parameters used to achieve recombinant protein expression in E. coli.
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Harith k. Buniya. Potential E. coli Expression Strategies for Production of Soluble Recombinant Streptokinases. 2022. https://doi.org/10.21203/rs.3.rs-1881858/v1
This study demonstrates how changing culture conditions like optical density, temperature, and media directly affects the soluble expression of recombinant streptokinases.
Igor P. Oscorbin, Maria S. Kunova, Maxim L. Filipenko. Optimization of conditions for production of soluble <i>E. coli</i> polyA-polymerase. 2024. https://doi.org/10.1101/2024.12.01.626206
This research shows that host strain choice, induction temperature, and plasmid copy number significantly dictate the yield and solubility of recombinant E. coli proteins.
Ruizhao Jiang, Shuting Yuan, Yilong Zhou, Yuwen Wei, Fulong Li, Miaomiao Wang, Bo Chen, Huimin Yu. Strategies to overcome the challenges of low or no expression of heterologous proteins in Escherichia coli.. 2024. https://doi.org/10.1016/j.biotechadv.2024.108417
This review highlights the critical role of managing mRNA structure, codon bias, and protein toxicity to overcome challenges in heterologous protein expression.
Christos P Papaneophytou, George Kontopidis. Statistical approaches to maximize recombinant protein expression in Escherichia coli: a general review.. 2014. https://doi.org/10.1016/j.pep.2013.10.016
This review explains that multiple factors such as expression host, fusion tags, and induction temperature and time heavily influence the production of soluble and active proteins.
Christoph Köppl, Nico Lingg, Andreas Fischer, Christina Kröß, Julian Loibl, Wolfgang Buchinger, Rainer Schneider, Alois Jungbauer, Gerald Striedner, Monika Cserjan-Puschmann. Fusion Tag Design Influences Soluble Recombinant Protein Production in Escherichia coli.. 2022. https://doi.org/10.3390/ijms23147678
This study evaluates how different N-terminal fusion tag combinations influence product titer, cell growth, and soluble protein production.
K Friehs, K F Reardon. Parameters influencing the productivity of recombinant E. coli cultivations.. 1993. https://doi.org/10.1007/BFb0007196
This review discusses how a multitude of variables relating to DNA, protein synthesis, and cultivation design determine overall productivity in recombinant E. coli.
Didier Busso, Yoav Peleg, Tatjana Heidebrecht, Christophe Romier, Yossi Jacobovitch, Ada Dantes, Loubna Salim, Edouard Troesch, Anja Schuetz, Udo Heinemann, Gert E Folkers, Arie Geerlof, Matthias Wilmanns, Andrea Polewacz, Claudia Quedenau, Konrad Büssow, Rachel Adamson, Elena Blagova, Julia Walton, Jared L Cartwright, Louise E Bird, Raymond J Owens, Nick S Berrow, Keith S Wilson, Joel L Sussman, Anastassis Perrakis, Patrick H N Celie. Expression of protein complexes using multiple Escherichia coli protein co-expression systems: a benchmarking study.. 2011. https://doi.org/10.1016/j.jsb.2011.03.004
This benchmark study confirms that various experimental factors like vector systems and cultivation conditions heavily influence protein production and solubility profiles.
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