January 13 - 17, 2014
Renaissance Hotel and Palm Springs Convention Center Palm Springs, California

A Community Dedicated to the
Evolving Field and Future of Biotherapeutics

Archived Content

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Successful engineering and designing of vectors and clone constructs leads to efficient production throughout the protein expression pipeline.  Protein expression bottlenecks frequently arise because functional proteins are difficult to produce as they fail to express, are expressed as insoluble aggregates, or cannot be purified by standard methods.  Thus, protein engineers are forced to return to the drawing board. This usually requires designing new cloning schemes including: lengthy verification and sequence analysis of the gene or protein of interest, moving a gene from one vector to another, transfecting the vector in an alternative host, re-characterizing the expressed protein, or any or all of the above. Researchers view this process as a linear pathway:  make an expression clone, try it out, and if it fails, go back to the beginning and start over--an inefficient, time-consuming and expensive process.  Cambridge Healthtech Institute’s Inaugural Engineering Vectors and Designing Clone Constructs continues the tradition of applying protein discovery research leading to functional products.  Learn from seasoned savvy researchers as they share their real-world experiences, applications, and results.

Thursday, January 14

1:15 pm Registration for Engineering Vectors & Designing Clone Constructs

 

ENGINEERING VECTORS

1:45 Chairperson’s Opening Remarks

Domonic Esposito, Ph.D., Principal Scientist, Protein Expression Laboratory, SAIC-Fredeick, Inc.

1:50 Highly Efficient Production of Diverse Protein Targets from Cell Substrates Engineered with Lentiviral Vectors

Boro Dropulic, Ph.D., Founder, President & Chief Scientific Officer, Lentigen Corp.

Lentiviral vectors are known as the most efficient method to deliver genes stably into cells.  There are several significant advantages for using this technology for protein production: (i) Quality – multiple gram levels of protein production from mammalian cells while maintaining high levels of glycosylation; (ii) Flexibility – applicable to all mammalian cell types, including adherent or suspension cells; (iii) Speed – multiple gram quantities of fully glycosylated protein within 12 weeks of sequence availability; (iv) Robust productivity – high transgene copy number per cell mitigates risk of gene silencing; and (v) Economics – high level of production in supernatant significantly decreases upstream and downstream costs; this technology is well suited for integration with disposable bioreactor systems.

2:20 Improved Physical Delivery Methods in Immune Therapy and Vaccine Models

Kate Broderick, Ph.D., Manager, Product Development, Inovio Biomedical

2:50 Purification and Characterization of a Yeast Endocytic Protein Using the Yeast Expression Plasmid pEG(KT)

B. Daniel Pierce, B.S., Department of Biology, Johns Hopkins University

The purification of proteins in large amounts is required for a variety of biochemical and biophysical experiments. The yeast plasmid pEG(KT), which we have sequenced and made amenable for modification, is particularly useful for purifying proteins that require eukaryotic post-translational modifications or cause problems when bacterially expressed. Using this plasmid, we have purified the yeast endocytic scaffold protein Pan1 for biochemical analysis of its self-interactions and biophysical experiments, such as a characterization of its intrinsic tryptophan fluorescence to obtain structural information.

3:20 Selected Poster Presentation

3:35 Networking Refreshment Break in the Exhibit Hall

4:30 Harnessing The Proteome:  The Center for Personalized Diagnostics at Arizona State

Jason Steel, B.S., Research Scientist, Center for Personalized Diagnostics,The Biodesign Institute, Arizona State University

We have initiated a project to create a sequence-verified collection of full-length cDNAs representing all coding regions for several organisms in a vector system that is protein expression-ready. By using a recombination-based vector system, users are able to execute the automated transfer of 1,000’s of genes into any protein expression vector overnight. We have demonstrated that it is possible to convert the full coding potential of an organism into a single repository of full-length cDNAs that can be used for all aspects
of protein analysis.

5:00 Vector-Based Strategies for Enhanced Protein Expression in the Food Grade Bacterium Lactococcus lactis

David Mills, Ph.D., Professor, Viticulture & Enology, University of California Davis

Lactococcus lactis is a common starter culture used in various dairy fermentations. Because of its long history of food grade use, combined with significant acid tolerance, L. lactis is currently a popular target for oral delivery of various biotherapeutic proteins.
We have developed a series of vectors, fermentation conditions and defined media that significantly increase heterologous protein production in L. lactis. These improvements, along with systems-biology approaches, reveal factors that limit protein production
in this commercially valuable microorganism.

5:30 Panel Discussion

6:00 Close of Day

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Recommended Short Course*

Tuesday, January 12
(SC8) Phage Diplay for Antibody and Peptide - Technical Tips & Guidelines 

* Separate registration required

 

 

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      Premier Sponsors: 

EMD Millipore 

 Novozymes (white) 

PerkinElmer NEW 2009 

 Protein Simple  

  

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Training Seminars 

Mon-Tues, January 13-14 

Biologics Formulation and Delivery  

 


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