Expression Systems

Would you like it if someone else did the cloning, expression, and protein purification? If you answer yes, check out our protein purification and expression services! 

Our SUMO-tag expression systems maximize the yield of soluble, functional proteins in E. coli, yeast, insect and mammalian cells. This system features SUMO functioning as both a chaperonin and as an initiator of protein folding to dramatically improve the solubility and level of expression of your protein of interest. Our desumoylases efficiently and precisely remove SUMO tags, releasing your protein with the desired N-terminal amino acid. Both the SUMO tags and the desumoylases have His6 tags making their subsequent removal fast and easy.

 
EColiThumb
E. coli

Bacterial expression is the usual starting point for expression of heterologous proteins. Bacterial fermentations are inexpensive and can reach high cell densities resulting in high volumetric yields of the target protein. Our SUMO fusion technology is ideally suited for this system.

 YeastThumb Yeast

As with bacterial expression systems, yeast offer relatively inexpensive growth media and high density fermentation. Furthermore, yeast offer the capability of carrying out limited post-translational modifications such as disulfide bond formation and glycosylation. We offer two yeast expression systems, one for intracellular expression in S. cerevisiae and the second for extracellular expression in P. pastoris.

InsectThumb Insect

Baculovirus/insect cell systems have found wide application for the expression of highly recalcitrant proteins such as protein tyrosine kinases. We have developed a SUMOstar-based system to support expression studies in this system.

MammalianThumbMammalian

Mammalian cell expression has become the system of choice for production of complex, glycosylated biotherapeutic proteins such as antibodies, growth factors and fertility hormones. Our SUMOstar system has been designed for transient transfection or stable expression in HEK293 or CHO cells.

 

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