Comparative analysis of eukaryotic cell-free expression systems
Author(s) -
Emily M. Hartsough,
Pankti Shah,
Andrew Larsen,
John C. Chaput
Publication year - 2015
Publication title -
biotechniques
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.617
H-Index - 131
eISSN - 1940-9818
pISSN - 0736-6205
DOI - 10.2144/000114327
Subject(s) - reticulocyte , cell free protein synthesis , wheat germ , lysis , protein biosynthesis , hela , cell free system , translation (biology) , recombinant dna , translation system , cell , eukaryotic translation , computational biology , cell culture , messenger rna , biology , microbiology and biotechnology , eukaryotic cell , protein expression , biochemistry , in vitro , gene , genetics
Cell-free protein synthesis (CFPS) allows researchers to rapidly generate functional proteins independent of cell culture. Although advances in eukaryotic lysates have increased the amount of protein that can be produced, the nuances of different translation systems lead to variability in protein production. To help overcome this problem, we have compared the relative yield and template requirements for three commonly used commercial cell-free translation systems: wheat germ extract (WGE), rabbit reticulocyte lysate (RRL), and HeLa cell lysate (HCL). Our results provide a general guide for researchers interested in using cell-free translation to generate recombinant protein for biomedical applications.
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