| Products/Services Used | Details | Operation |
|---|---|---|
| Codon Optimization | … 1,302 bp) was extracted from NCBI website (Gene Bank = DQ512735.1), then C + G contents and codon usage of the wild-type BoNT/E-Hcc sequence was optimized according to the E. coli expression system by using websites http://eu.idtdna.com, http://www.genscript.com and … | Get A Quote |
Botulinum neurotoxin type E heavy chain consists of two domains: N-terminal half as a translocation domain and C-terminal half (Hcc) as a binding domain. In this research a synthetic gene fragment encoding the binding domain of botulinum neurotoxin type E (BoNT/E-Hcc) was highly expressed in Escherichia coli by pGEX4T-1 vector. After purification, the recombinant BoNT/E-Hcc was evaluated by SDS-PAGE and western blot (immunoblot) analysis. Average yields obtained in this research were 3.7 mg recombinant BoNT/E-Hcc per liter of bacterial culture. The recombinant protein was injected in mice for study of its protection ability against botulinum neurotoxin type E challenges. The challenge studies showed that, vacci... More
