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Cambridge Healthtech Institute’s 17th Annual
Recombinant Protein Expression and Production
Achieving Quality and Quantity
January 21-22, 2015

Biopharmaceuticals currently represent the fastest-growing sector of the pharmaceutical industry, driven by a rapid expansion in the manufacture of recombinant protein-based drugs. To meet the demand, it is crucial to increase the throughput of expression, production and purification processes and systems.

Cambridge Healthtech Institute’s Recombinant Protein Expression and Production conference explores the newest data and innovations relating to the best choices in hosts/systems, as well as ways to revive existing systems and make them work more effectively to produce the quality and quantity of the desired biotherapeutic.

Day 1 | Day 2 | Download Brochure | Speaker Biographies 

Final Agenda 


1:30 pm Conference Registration

BUZZ Sessions png

2:00 BuzZ Session A

3:00 Refreshment Break in the Exhibit Hall with Poster Awards

3:45 BuzZ Session B
(More Details >>)

4:30-5:00 Short Course Registration

5:00-8:00 Dinner Short Courses More Details >> 


7:30 am Conference Registration and Morning Coffee

Enhancing Expression and Production: Process Development

8:15 Chairperson’s Opening Remarks

Stephen R. Hughes, Ph.D., Research Molecular Biologist, Renewable Product Technology Research Unit, U.S. Department of Agriculture, Agricultural Research Service, National Center for Agricultural Utilization Research

Keynote Presentation

8:20 In situ Protein Expression for High-Throughput Protein Microarray Studies

JoshuaLaBaerJoshua LaBaer, M.D., Ph.D., Director, Virginia G. Piper Center for Personalized Diagnostics and Virginia G. Piper Chair, Personalized Medicine, Biodesign Institute, Arizona State University

Self-assembling protein microarrays can be used to study protein-protein interactions and protein-drug interactions, to search for enzyme substrates and as tools to search for disease biomarkers. In particular, recent experiments have focused on using these protein microarrays to search for autoantibody responses in cancer patients. These experiments show promise in finding antibody responses that appear in only cancer patients. New methods using click chemistry-based reagents also allow the application of these arrays for discovering new substrates of post-translational modification.

9:00 Optimizing the Cell Line Development Workflow to Support Accelerated Timelines

ChristineDeMariaChristine DeMaria, Ph.D., Associate Director, Therapeutic Protein Expression, Global Biotherapeutics Development, Sanofi US

To support program timelines, we have further optimized our workflow to generate high-titer CHO cell lines. This included modifying the process for selection and sorting of transfected pools and more stringent 96-well plate based screens. These changes resulted in higher-titer clones being identified sooner, supporting more rapid development and quality assessment of lead clones. Workflow optimization case studies will be presented.

9:30 Hijacking E. coli’s Heat-Shock Response Boosts Protein Production

XinZhangXin Zhang, Ph.D., Burroughs Wellcome–CASI Fellow, Scripps Research Institute

The production of high-yield and high-quality recombinant proteins from Escherichia coli is highly desirable for both academic and industrial settings. In this talk, I will describe a generally applicable method for this purpose, using a transcriptionally reprogrammed E. coli by over expressing a heat-shock response transcription factor. Similar strategies of hijacking stress-responsive pathways should be useful to enhance cellular protein folding capacity and improve recombinant protein production in other cell types.

10:00 Coffee Break in the Exhibit Hall with Poster Viewing

10:50 Effect of Ambient Light on Monoclonal Antibody Product Quality during Small-Scale Mammalian Cell Culture Process in Clear Glass Bioreactors

MaryMallaneyMary Mallaney, Engineer II, Purification Development, Genentech, Inc.

During a monoclonal antibody (mAb) small-scale cell culture process, a larger-than-expected difference was observed in the charge variants profile of the harvested cell culture fluid between the 2L and larger scales. It was determined that ambient laboratory light induces photoreactions causing an increase in acidic variants. Our data clearly indicate that care should be taken when glass bioreactors are used in cell culture studies during mAb production.

11:20 Integrated Automation for Continuous High-Throughput Synthetic Chromosome Assembly and Transformation to Identify Improved Yeast Strains for Industrial Production of Peptide Sweetener Brazzein

StephenHughesStephen R. Hughes, Ph.D., Research Molecular Biologist, Renewable Product Technology Research Unit, U.S. Department of Agriculture, Agricultural Research Service, National Center for Agricultural Utilization Research

We describe a one-step construction of a synthetic yeast artificial chromosome (YAC) containing the optimized ORFs in a polyprotein cassette for expression of multiple genes such as those for enzymes in metabolic pathways or for valuable peptide or protein coproducts behind an optimized promoter with custom expression fusion tags selected for desired expression levels and protein locations inside or outside the industrial strain.

11:50 The Rapid Generation of Multiple Antibody Toxin Conjugates: Expression in Eukaryotic Algae

MillerTranMiller Tran, Ph.D., Senior Scientist, Lead Discovery, Verdant Therapeutics, Inc.

Over the last decades, targeted antibody therapies, including antibody drug conjugates and recombinant immunotoxins, have garnered increasing attention. However, their production has become increasingly complicated and expensive. To overcome the challenges associated with the production of targeted therapies, eukaryotic algae are being used to produce recombinant immunotoxins that overcome the shortcomings of established technologies. With media cost in the cents per liter, the potential of algae is now being realized.

12:20 pm Taking Protein Production in Escherichia coli to the Next Level

DavidVikstromDavid Vikström, Ph.D., CTO, Xbrane Bioscience

The bacterium Escherichia coli is a widely used host for the production of proteins. However, protein production in E. coli is usually a challenge. Therefore, Xbrane has developed new titratable expression systems. These systems allow optimizing the production of both routine and difficult targets in E. coli. The expression systems in combination with optimization and strain engineering are really taking the protein production in E. coli to the next level.

12:50 Session Break  

1:00 Luncheon Presentation: Best of Both Worlds:
Innovative Microbial System Leverages the Advantages of Both Bacterial and Mammalian Manufacturing

KristinDeFifeKristin DeFife, Ph.D., Director, Biologics Manufacturing, Ajinomoto Althea, Inc.

Reach high expression using a microbial system and overcome challenges associated with E. coli including aggregation, lengthy purification and inefficient refolding processes. The Corynex® system secretes properly folded, biologically active proteins into the extracellular fermentation broth like mammalian cells which eliminates multiple purification steps, lowering cost and speeding time to market.

Difficult Expression and Production: Membrane Proteins

2:00 Chairperson’s Remarks

Ian Hunt, Ph.D., Group Leader, Proteomic Chemistry and Head, Protein Sciences, Novartis

2:05 Designer Surfactant-Like Self-Assembling Peptides for Membrane Protein Purification and Stabilization

SotiriosKoutsopoulosSotirios Koutsopoulos, Ph.D., Research Scientist, Center for Biomedical Engineering, Massachusetts Institute of Technology

Membrane proteins are integral proteins of the cell membrane and are directly involved in the regulation of many biological functions and in drug targeting. However, our knowledge of membrane proteins is limited due to difficulties in producing sufficient quantities of soluble, functional and stable receptors. Designer, surfactant-like peptides may be used to extract the protein from the cell membrane and stabilize the protein outside the membrane bilayer for further studies.

2:35 Production of Human Integral Membrane Proteins in Mammalian Cells

JamesLoveJames D. Love, Ph.D., Director, Technology Development, Biochemistry, Albert Einstein College of Medicine

Integral membrane proteins are key targets in the understanding of health and human disease, yet producing functional material in great enough quantities for structural studies remains a formidable task. This talk highlights the expression technologies under development that will greatly aid high-throughput efforts to produce functional human membrane proteins and complexes, specifically GPCRs, for a plethora of structural techniques.

3:05 Advances for Maximizing Protein Yields in HEK293 and CHO Transient Expression

HenryChiouHenry C. Chiou, Ph.D., Associate Director, Cell Biology, Life Science Solutions, Thermo Fisher Scientific

Increasing focus on complex proteins in advanced research elevates the need for higher yields from mammalian transient expression systems. To achieve this objective while maintaining speed, simplicity and ease-of-use requires coordinated development and synergy between novel high-capacity media, higher productivity HEK293 and CHO cells, and higher performance transfection reagents. This presentation will demonstrate the effectiveness of this “holistic” approach to achieve gram-level protein yields by transient expression.

3:35 The Need for Technology Platforms in USP Development

HugoDeWitHugo de Wit, CEO, Cellca

Are you faced with budget reductions for USP development or even anticipated to do “more with less”? Do you see increasing expectations from market and management regarding reducing timelines and cost of goods attributes? We demonstrate how a robust USP platform can help you meet these challenges.

AbSci3:50 Bypassing Inclusion Body Formation in E. coli: Maximizing Soluble Expression of Complex Multimeric Proteins

Mark Valasek, M.D., Ph.D., Co-founder, AbSci; Assistant Professor, Pathology, University of California, San Diego

Cytoplasmic expression of large complex proteins in E. coli is limited primarily due to protein aggregation and the corresponding refolding process. These costly aggregates form when proteins are expressed too quickly and strongly. AbSci has developed a tightly regulated, dual titratable expression system that is able to homogenously induce high levels of complex multimeric proteins in a soluble and active form.

4:05 Refreshment Break

4:30 Plenary Keynote Session

From Yeast to the Brain: Advances in Proteomics (More Details >>

John YatesJohn R. Yates, Ph.D., Ernest W. Hahn Professor, Chemical Physiology and Molecular and Cellular Neurobiology, The Scripps Research Institute


5:30-7:00 Reception in the Exhibit Hall with Poster Viewing

Day 1 | Day 2 | Download Brochure | Speaker Biographies