Yeast expression systems like Pichia pastoris are preferred tools for high expression of properly folded secretory proteins and limited production of endogenous secretory proteins.
It is a cost-effective eukaryotic expression system that allows both secretion expression and intracellular expression. Post-translational modifications have been documented including glycosylation, phosphorylation, and acylation, that are key for biological activities. It is particularly suitable for the expression and preparation of eukaryotic functional proteins such as defensin, interleukin and cytokines. The often efficient secretion of properly folded proteins into the extracellular medium is often observed and allows production of high purity functional protein.
All services include multiple steps from gene to purified protein as described in the table below.
Leadtime is approximately 9-12 weeks.
|Description||Resulting Material||Average turnaround (*)|
-Cloning in standard pUC plasmid
|Cloned, synthesized and verified gene||2 weeks|
|Subcloning for expression|
-Transformation of Pichia pastoris
-Screening and strain creation.
|Strain with target gene||3-4 weeks|
|-Expression pilot and optimization experiments
-Choice of most suitable strain
-Adjust culture conditions
-Determine yields and protein behavior
|10-50 µg of semi-purified protein||2-3 weeks|
|Expression and purification|
-SDS-PAGE, WESTERN blot
|Purified protein||2-3 weeks|
(*) Average production time for average difficult project. Actual turn around time varies with individual project features.