As a eukaryote, Pichia pastoris has many of the advantages of higher eukaryotic expression systems such as protein processing, protein folding, and posttranslational modification, while being as easy to manipulate as E. coli or Saccharomyces cerevisiae. It is faster, easier, and less expensive to use than other eukaryotic expression systems such as baculovirus or mammalian tissue culture, and generally gives higher expression levels.
Many therapeutic proteins are glycoproteins and require the attachment of sugar structures (i.e. glycosylation) to allow for proper folding, expression and biologic/therapeutic activity. Current manufacturing methods based on mammalian cell culture do not allow for the precise control of glycosylation and produce a mixture of different glycoforms, some of which are beneficial and some of which are problematic or of little benefit. We have a technology that modifies Pichia to make the production of proteins with human-like glycosylation possible.
- Uniform glycosylation
- Minimize aberrant glycosylation
- Customize glycosylation
- Increased homogeneity of bio-pharmaceuticals
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