abstract: Recombinant protein expression is essential to biotechnology and molecular medicine, but facile methods for obtaining significant quantities of folded and functional protein in mammalian cell culture have been lacking. Here I describe a novel 37-nucleotide in vitro selected sequence that promotes unusually high transgene expression in a vaccinia driven cytoplasmic expression system. Vectors carrying this sequence in a monocistronic reporter plasmid produce >1,000-fold more protein than equivalent vectors with conventional vaccinia promoters. Initial mechanistic studies indicate that high protein expression results from dual activity that impacts both transcription and translation. I suggest that this motif represents a powerful new tool in vaccinia-based protein expression and vaccine development technology. / Dissertation/Thesis / M.S. Biochemistry 2012
| Identifer | oai:union.ndltd.org:asu.edu/item:14728 |
| Date | January 2012 |
| Contributors | Flores, Julia Anne (Author), Chaput, John C (Advisor), Jacobs, Bertram (Committee member), Labaer, Joshua (Committee member), Arizona State University (Publisher) |
| Source Sets | Arizona State University |
| Language | English |
| Detected Language | English |
| Type | Masters Thesis |
| Format | 63 pages |
| Rights | http://rightsstatements.org/vocab/InC/1.0/, All Rights Reserved |
Page generated in 0.0026 seconds