A Single Codon Optimization Enhances Recombinant Human TNF-α Vaccine Expression in Escherichia coli
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Enhanced Expression of Recombinant Activin A in Escherichia coli by Optimization of Induction Parameters
Activin A is a member of the transforming growth factor β super family. Because of its extensive clinical usages, its recombinant production is beneficial. In this study, activin A was expressed in E. coli using the pET 21a expression vector. The optimization of the activin A production in E. coli was done by using the response surface methodology (RSM). At this stage, the effect of IPTG and la...
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Background: Leukemia inhibitor factor (LIF) is a very important pleiotropic cytokine which belongs to interleukin-6 (IL-6) family. LIF exerts multiple effects on different types of cells and tissues with numerous regulatory effects in vivo and in vitro. It is a lymphoid factor, which performs a number of activities including cholinergic neuron differentiation, contro...
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Porcine β-defensin-2 (pBD2) is a cationic antimicrobial peptide that has therapeutic potential. The amount of pBD2 in nature is limited, and the expression of pBD2 in Escherichia coli is low, probably because a different gene codon is used by prokaryotic organisms to that used by eukaryotes. Codon preference optimization is one of the ways to increase heterologous expression of pBD2. To achieve...
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A genetic strategy to enhance recombinant protein production is discussed. A small DNA bending protein, Fis, which has been shown to activate rRNA synthesis upon a nutrient upshift, was overexpressed in E. coli strain W3110 carrying vector pUCR1. Overexpression of Fis during exponential growth was shown to activate rrn promoters to different extents. A 5-fold improvement in chloramphenicol acet...
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ژورنال
عنوان ژورنال: BioMed Research International
سال: 2018
ISSN: 2314-6133,2314-6141
DOI: 10.1155/2018/3025169