14:05 KEYNOTE PRESENTATION:
A New Platform for the Rapid Generation of Stable CHO Pools and Clones
Yves Durocher, Ph.D., Protein Expression Team Leader, Life Sciences, NRC Human Health Therapeutics Portfolio, National Research Council Canada
Large-scale transfection of HEK293 cells is a highly valuable tool for the fast generation of mgs to grams quantities of r-proteins required for R&D purpose. More recently, new CHO-based platforms have been developed with some success, even though productivity is often lower compared to HEK293 cells. This is especially problematic when large quantities of difficult-to-express r-proteins are needed for various studies. We will present data describing our new CHO platform that allows the generation of stable pools capable of producing up to 500 mg/L of monoclonal antibodies in less than 5 weeks post-transfection. This platform represents a viable alternative to large-scale CHO transfection or stable cell line development for manufacturing large quantities of r-proteins candidates.
14:35 Total Protein Engineering Solution for GPCRs through Stabilization and Construct Optimization
Markus Koglin, Ph.D., Associate Director, Protein Engineering, Heptares Therapeutics
Here we demonstrate that protein quality when expressed in mammalian or insect cells drastically improves with increasing thermostability. Although this increased quality produces material suitable for biophysical technologies like SPR or NMR, StaR generation alone normally does not provide suitable material for crystallization. Further construct optimization including N- and C-terminal truncations and PTM removal can have a dramatic effect in expression quantities and qualities. The combination of StaR technology and systematic construct design delivers a powerful approach in expression and purification of protein with suitable crystallization qualities.
15:05 Refreshment Break in the Exhibit Hall with Poster Viewing
15:50 Expression and Stabilization of Pathologic GPCR Mutations and Arrestin Complexes for Structural Studies
Joerg Standfuss, Ph.D., Senior Scientist and Group Leader, Biomolecular Researcher, Paul Scherrer Institute, ETH
We have solved GPCR Structures with full and partial agonists to understand the activation mechanism and the pharmacology of GPCRs in detail. Thermostabilization of receptors has enabled biophysics and detailed pharmacological characterization of a number of GPCRs. GPCR structure can now be used for fragment-based drug design.
16:20 Recombinant Expression of Full-Length Complement Protein C1q and its Globular Domains
Uday Kishore, Ph.D., Director, Centre for Infection, Immunity and Disease Mechanisms, Brunel University
C1q is the IgG- and IgM-recognizing subcomponent of the classical complement pathway that is important in a range of conditions including SLE, cancer, allergy, and transplantation and epilepsy. C1q, which is composed of three chains (A, B, C)having N-terminal collagen region and binds a number of self and non self-ligands via C-terminal globular region. To make recombinant forms of full length heterotrimeric C1q as well as globular region has been a real challenge in the field for over decades. Various strategies to express and characterize C1q will be discussed.
16:50 New Tools for Difficult Expression Problems: Endotoxin-Free Proteins, Biotinlyated Proteins, and More
David Mead, CEO, Lucigen Corp.
Lucigen will present novel competent E. coli cells lacking lipopolysaccharide (LPS) for endotoxin-free protein and DNA production, as well as new systems for fast expression and isolation of pure proteins via highly efficient in vivo biotinylation.
17:05 Corynex®: A Novel Protein Expression System that Delivers Better Results
Yoshimi Kikuchi, Ph.D., Principal Researcher, AJINOMOTO CO., INC.
Corynex® is a microbial protein expression system that can secrete active proteins directly into media with high purity. Corynex® has already succeeded in producing numerous difficult-to-express proteins which could hardly be produced in other systems.
17:20 End of Day One
17:20 Short Course Registration*
17:35 – 20:30 Dinner Short Course: Troubleshooting and Engineering of Antibody Constructs
*Separate registration required, see page 2 for details
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