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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 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.
The expression may be constitutive, meaning that the protein is produced constantly in the background, or it may be inducible whereby the protein is expressed only under certain condition, for example when a chemical inducer is added. These two different types of expression depend on the types of promoter and operator used.
Proteins that can result from the expression of recombinant DNA within living cells are termed recombinant proteins. When recombinant DNA encoding a protein is introduced into a host organism, the recombinant protein is not necessarily produced. [1] Expression of foreign proteins requires the use of specialized expression vectors and often ...
DNA recombinases are widely used in multicellular organisms to manipulate the structure of genomes, and to control gene expression.These enzymes, derived from bacteria (bacteriophages) and fungi, catalyze directionally sensitive DNA exchange reactions between short (30–40 nucleotides) target site sequences that are specific to each recombinase.
Cre recombinase plays important roles in the life cycle of the P1 bacteriophage. Upon infection of a cell the Cre-loxP system is used to cause circularization of the P1 DNA. In addition to this Cre is also used to resolve dimeric lysogenic P1 DNA that forms during the cell division of the phage. [7]
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]
As a eukaryote, they have several important functions not present in the yeast and bacterial systems, including protein modification, processing, and eukaryotic transport system. Because they can be propagated in very high concentrations, it simplifies the process of obtaining large amounts of recombinant proteins.