MoBiTec
P.O. Box 2157
Marco Island, FL, 34146-2157
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Dual Expression Vector System
New pPICHOLI shuttle vector system has been constructed for efficient protein expression both in Escherichia coli and Pichia pastoris making subcloning experiments superfluous. The well-studied, commonly used bacterium E. coli is simple to handle and enables cost-effective high-level production of recombinant proteins. However, the expression of many (mainly eukaryotic) genes, often results in the production of aggregated and denatured proteins, accumulated in inclusion bodies. In contrast, the yeast P. pastoris is ideally suited for synthesis of soluble heterologous target proteins with post-translational modifications which can be used, for example, for the production of monoclonal antibodies or native protein chips, crystallization and NMR structure analysis. Its rapid growth at high cell density combined with a strong, inducible promotor on pPICHOLI allows for expression of recombinant proteins in high yields. Genes cloned in pPICHOLI are expressed in E. coli and P. pastoris as fusion proteins with HIS-, HA- and biotin tags enabling a simple, fast and reproducible purification via affinity chromatography and detection by commercially available specific antibodies.
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