Study protein function more efficiently with standardized clones
Rebecca L. Mullinax Heidi Davis David T. Wong
Kelly Wynne Vilma Nioko
Leonardo DeLeon SanDEe Soares Joseph A. Sorge Edward Marsh
Spencer Stevens Chris Hansen Brian Schilling
Stratagene now offers sequence-validated and expression-tested human cDNA in a single dual- expression vector. These clones eliminate the time spent cloning, sequencing, and expression testing new genes and allow gene analysis experiments to begin immediately. The versatile dual-expression vector permits proteins to be expressed and detected in mammalian cells and proteins to be expressed in and purified from bacterial cells.
In the near future, the human genome will be completely sequenced. The next and more challenging step will be to characterize the biological role of each gene and the way in which the encoded protein functions in the cell. To facilitate this characterization, Stratagene has cloned the open reading frame (ORF) of selected human cDNA into a dual-expression vector. Potential uses for these expressed proteins include analyzing protein function, defining both protein-protein and protein-DNA interactions, elucidating pathways, studying protein degradation, determining the effects of over-expression, and preparing antigen.
The pDual GC expression vector* was designed for high-level
protein expression in mammalian and bacterial cells ( Figure 1). The dominant selectable marker is the neomycin phosphotransferase
gene, which is under the dual control of the b-lactamase
and SV40 promoters in bacterial and mammalian cells, respectively. The
tandemly arranged bacterial Shine-Dalgarno1 and mammalian Kozak