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The non-lytic system has been used to give higher protein yield and quicker expression of recombinant genes compared to baculovirus-infected cell expression. [24] Cell lines used for this system include: Sf9 , Sf21 from Spodoptera frugiperda cells, Hi-5 from Trichoplusia ni cells, and Schneider 2 cells and Schneider 3 cells from Drosophila ...
The T7 expression system is used in the field of microbiology to clone recombinant DNA using strains of E. coli. [1] It is the most popular system for expressing recombinant proteins in E. coli. [2] By 2021, this system had been described in over 220,000 research publications. [3]
Enzyme activity analysis requires various expression systems to classify enzyme variants. As opposed to other animals, the expression of functional recombinant proteins is a costly process for mammalian cells specifically, due to low expression levels of enzymes contributing to drug metabolism.
The expression of a protein may be tightly controlled, and the protein is only produced in significant quantity when necessary through the use of an inducer. In some systems, however, the protein may be expressed constitutively. Escherichia coli is commonly used as the host for protein production, but other cell types may also be used.
This system has allowed researchers to manipulate a variety of genetically modified organisms to control gene expression, delete undesired DNA sequences and modify chromosome architecture. The Cre protein is a site-specific DNA recombinase that can catalyse the recombination of DNA between specific sites in a DNA molecule.
The mechanism of these recombination events was known to be unique as they occurred in the absence of bacterial RecA and RecBCD proteins. The components of this recombination system were elucidated using deletion mutagenesis studies. These studies showed that a P1 gene product and a recombination site were both required for efficient ...
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