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Cell-free protein synthesis, also known as in vitro protein synthesis or CFPS, is the production of protein using biological machinery in a cell-free system, that is, without the use of living cells. The in vitro protein synthesis environment is not constrained by a cell wall or homeostasis conditions necessary to maintain cell viability. [ 1 ]
[6] [7] The cell extract-based type are susceptible to problems like quick degradation of components outside their host, as shown in a study by Kitaoka et al. where a cell-free translation system based on Escherichia coli (E. coli), of the cell extract-based type, had the mRNA template degrade very quickly and led to the halt of protein ...
Cell-free protein array technology produces protein microarrays by performing in vitro synthesis of the target proteins from their DNA templates. This method of synthesizing protein microarrays overcomes the many obstacles and challenges faced by traditional methods of protein array production [1] that have prevented widespread adoption of protein microarrays in proteomics.
Promega Corporation is a Madison, Wisconsin–based manufacturer of enzymes and other products for biotechnology and molecular biology with a portfolio covering the fields of genomics, protein analysis and expression, cellular analysis, drug discovery, and genetic identity.
The in vitro translation can also be done in a PURE (protein synthesis using recombinant elements) system. PURE system is an E. coli cell-free translation system in which only essential translation components are present. Some components, such as amino acids and aminoacyl-tRNA synthases (AARSs) can be omitted from the system.
Tandem affinity purification (TAP) is an immunoprecipitation-based purification technique for studying protein–protein interactions.The goal is to extract from a cell only the protein of interest, in complex with any other proteins it interacted with.
Epithelial cells in culture grow normally as tight clusters. However, they could be induced to break cell-cell contacts and become elongated and motile after exposure to a "scatter factor" that was secreted by mesenchymal cells such as Swiss 3T3 fibroblasts. [12] This was best described by Julia Gray's group in 1987. [13]
P-gp is a 170 kDa transmembrane glycoprotein, which includes 10–15 kDa of N-terminal glycosylation.The N-terminal half of the protein contains six transmembrane helixes, followed by a large cytoplasmic domain with an ATP-binding site, and then a second section with six transmembrane helixes and an ATP-binding domain that shows over 65% of amino acid similarity with the first half of the ...