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Day 1 | Day 2 Although therapeutic antibodies have come a long way in the past several years, many problems still exist in the production and use of these complex molecules. The negative qualities of these proteins, including immunogenicity, delivery difficulties, and the high cost of production, among others, have made the outcomes of their production and use less than satisfactory. In order to improve or eliminate these negatives, it is critical to find new ways to engineer antibodies, new antibody alternatives (such as mimetics, fragments, etc.) and novel ways to scale up production to provide large amounts of these proteins in a cost-effective way. This conference will present the latest data on how to achieve these improved results and the research data necessary to apply the solutions to your laboratory’s efforts.
WEDNESDAY, 7 OCTOBER 13:00 Conference Registration 14:00-14:05 Chairperson’s Remarks Overcoming Bottlenecks 14:05-14:35 Production of Recombinant Antibody Fragments in Cold Adapted Bacteria: An Alternative to Conventional Microbial Systems Maria Giuliani, Organic Chemistry and Biochemistry, University of Naples “Federico II” Inclusion body formation is a major limiting factor for recombinant antibody fragment production in conventional prokaryotic expression systems. The solubility of recombinant proteins can be successfully improved by reducing the temperature of the production process. We developed a novel expression system for recombinant antibody fragment production at low temperatures based on the use of a psychrophilic bacterium as the recombinant expression host. The new cold expression system has been tested for recombinant production of several antibody formats (Fab, scFv, Vhh) and all of them were recovered in soluble form correctly secreted in the bacterial periplasm. 14:35-15:05 An XBP-1 Dependent Bottle-Neck in Production of IgG Subtype Antibodies in Chemically Defined Serum-Free Chinese Hamster Ovary (CHO) Fed-Batch Processes Hitto Kaufmann, Ph.D., Boehringer Ingelheim Pharma GmbH & Co. KG, BP Process Science 15:05-15:35 TBA 15:35-16:00 Refreshment Break
Sponsored by Hidetaka Seo, Ph.D., Senior Director, Research & Development, ADLib® (Autonomously Diversifying Library) System could be a platform technology to identify monoclonal antibodies quickly and efficiently in vitro against multiple targets, even tough antigens, which couldn’t be obtained by the conventional methods. 16:15-16:30 Sponsored Presentation (Opportunity Available) 16:30-17:00 ImmunoRNase Fusion Proteins Thomas Schirrmann, Ph.D., Department of Biotechnology, “ImmunoRNases” represent a class of immunoenzymes that employ ribonucleases (RNases) as cytotoxic effector component. They do not show appreciable immunogenicity or non-specific toxicity, and are expected to not cause severe adverse effects known from many classical immunotoxins and their plant or bacterial toxin domains. Recently, we developed a novel immunoRNase design by fusing a CD30 specific single chain Fv (scFv) fragment to the IgG1 Fc moiety and the pancreatic RNase. This immunoRNase construct was very efficiently produced in mammalian cells as homodimeric protein that specifically bound to CD30+ lymphoma cells and inhibited tumor growth at low nanomolar concentrations. 17:00-17:30 Spotlight Poster Presentations 18:30 BIOTECHNICA Night: Beer Hall, full dinner reception, a traditional German band
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