Benefits of a recombinant expression system include control over the expressed protein sequence, control over extent of posttranslational modifications, and reproducibility of culturing conditions and hence protein composition [ 11– 16].
All G-protein chimeras were expressed at comparable levels in the recombinant expression system (Figure 4C, D).
Earlier work demonstrated that the HT1080 fibrosarcoma cell line endogenously expresses this suite of enzymes, producing correctly modified collagen from a recombinant expression system [ 17].
A prerequisite for such an approach is a recombinant expression system.
The results of SDS-PAGE for the recombinant protein indicated that the recombinant expression system was successfully structured.
In this report the optimization of a bacterial recombinant expression system is described, resulting in the high yield production of pacifastin-like inhibitors of the desert locust.
Single and double mutations at residues Q20 and D43 were made in a recombinant expression system that corresponded to Gox2181-D43Q and Gox2181-Q20R&D43Q, respectively.
On the other hand, Escherichia coli (E. coli) is known to be the simplest, fastest and most cost-effective recombinant expression system, which usually achieves higher protein yields than mammalian cells.
