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Expression Systems


Add your protein of interest to the growing bibliography of SUMO-expressed proteins!

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.

Enhanced Expression and Solubility Using SUMO vs. Other Commonly-used Fusion Tags



Figure legend. GDF8 (myostatin), a secreted TGFβ family member and difficult-to-express protein, was expressed in E. coli either as a His6, Ub, SUMO, MBP, GST, TRX, or NUS A fusion. Protein fractions were resolved by SDS-PAGE and stained with Coomassie. Arrowheads indicate expected/observed positions of respective protein bands. Of all tags tested, SUMO was the only fusion tag that provided high-level expression of soluble protein.


Express your protein the first time and every time with SUMO. Choose your preferred expression system below and get started with SUMO today!


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Expression Systems

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.
Expression Systems

Mammalian

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 studies in HEK293 or CHO cells.
Expression Systems

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.
Expression Systems

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.
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HEADLINES

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LifeSensors Awarded U.S. Patent for Novel Ubiquitin Pathway Enzyme Substrates
LifeSensors, Inc., a biotech company developing cutting-edge technologies for studying the ubiquitin pathway, has been awarded a U.S. patent for the development of novel, fluorescent di- and poly-ubiquitin deubiquitinase (DUB) substrates (US 8,518,660).
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LifeSensors is a proud sponsor of the 5th Annual Ubiquitin Drug Discovery & Diagnostics Conference
This year's conference will be held at the Four Seasons Hotel in Philadelphia, July 22-24 and will once again highlight the latest research taking place in the ubiquitin field. We are excited to learn about all of the latest discoveries and technical advances and hope to see you there!
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LifeSensors presented an overview of ubiquitin proteomics at the 3rd GTC Conference, Ubiquitin Research and Drug Discovery, Las Vegas, February 25-26th, 2013.
Complexity of ubiquitin pathways leads to frequent questions related to identification of ubiquitin pathway enzymes (E3s and DUBs) and their substrates. An overview of biochemical proteomics for drug discovery applications including Ubiquitin Protein Microarray Services from LifeSensors was presented by Christian Loch, Assistant Director, R&D. Visit our website to find additional information about our Ubiquitin Protein Microarrays.
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