The ESP? yeast protein expression and purification system uses the yeast Schizosaccharomyces pombe as the expression host and the glutathione S-transferase (GST) peptide as the protein purification tag. This system provides an easy alternative to protein production in E. coli. Proteins expressed in E. coli may lack proper biological function and antigenicity because of the absence of eukaryotic posttranslational modifications. S. pombe is a single-cell eukaryotic organism with properties similar to higher eukaryotic organisms. These properties, such as chromosome structure and function, cell-cycle control, RNA splicing and codon usage, make S. pombe ideal for the production of eukaryotic proteins. Also, eukaryotic proteins expressed in S. pombe are more likely to be folded properly, which improves the specific activity and can eliminate protein insolubility problems found in E. coli expression systems.

Location of Features

ARS1 origin 65–1270
ampicillin resistance (bla) ORF 1401–2258
pUC origin 2409–3076
yeast LEU2-d (promoter mutant) ORF 5464–6555
S. pombe nmt1 promoter 7001–8165
GST affinity tag 8168–8818
thrombin target 8870–8881
FLAG tag 8828–8845
EK target 8846–8869
multiple cloning site 8855–8869
S. pombe nmt1 terminator 8885–9879
f1 origin 10091–10397