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Fusion Proteins
Studies from National Taiwan University yield new data on fusion proteins
September 22nd, 2008
"Expression of recombinant proteins as fusions with SUMO (small ubiquitin-related modifier) protein has significantly increased the yield of difficult-to-express proteins in Escherichia coli. The benefit of this technique is further enhanced by the availability of naturally occurring SUMO proteases, which remove SUMO from the fusion protein," scientists in Taipei, Taiwan report. "Here we have improved the exiting SUMO fusion protein approach for effective production of native proteins. First, a sticky-end PCR strategy was applied to design a new SUMO fusion protein vector that allows directional cloning of any target gene using two universal cloning sites (Sfol at the...
Source: Proteomics Weekly (2008-09-22)
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