In this study, pullulanase gene (pulN) was functionally expressed in E. coli through expression vector replacement and induction expression strategy optimization.
In this study, we obtained a novel pullulanase gene from the strain P. polymyxa Nws-pp2 and the gene was functional expressed in E. coli through expression vector replacement and induction expression strategy optimization.
For vector-based shRNA, improvements can be achieved through manipulating expression strategy, using different types of promoters, modifying shRNA structures, and simultaneously expressing multiple shRNAs in a single vector [ 9– 13].
We obtained a soluble BubR1 construct using a three-step expression strategy.
In this study, we tested a multiple shRNA expression strategy for different shRNAs using repeated promoters in a lentiviral vector.
The expression strategy included using a previously reported modified α-factor preproleader for enhanced secretion and pAOX1, a methanol-responsive promoter.
Maximization of the soluble protein expression in Escherichia coli (E. coli) via the fusion expression strategy is usually preferred for academic, industrial and pharmaceutical purposes.
A broad-host-range expression strategy was successfully developed to exploit the unique metabolic capability for UDP-galactose regeneration during oligosaccharide synthesis.
A novel high-throughput screening method based on the Luminex® xMAP™ bead technology was developed allowing a rapid evaluation of a certain expression strategy.
In the present paper, the general properties, mechanism of action, application value, existing problems, the latest progress and the expression strategy were discussed.
Here, a novel cell-free expression strategy was developed to efficiently produce large amounts of human GNA1(HsGNA1) and HsGNA1-sGFP for throughput inhibitor screening.
