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The Versatile Leap-In Transposase Platform: Applications in High Titer Bispecific Antibody Production and Next Generation Cell Therapies

About This Webinar

Sponsored by ATUM

The Leap-In Transposase® Platform was launched by ATUM in 2018 for cost-effective, easily implemented stable CHO cell line development and the robust manufacturing of biologics and vaccines. Through continuous development and optimization, Leap-In Transposase has become the industry standard and saw broad application in the urgent response to SARS-CoV-2, enabling the accelerated generation of clinical materials on a timeline of mere months.

The combination of the platform’s rapid generation of bulk pools that are highly predictive of the final manufacturing clones with ATUM’s deep expertise in protein expression regulation has also been applied to the expression of complex multispecific biologics comprised of three and four chains where chain ratio balancing can be critical for robust, cost-effective manufacturing.

In this webinar, ATUM and Invenra will present a case study on the application of the Leap-In Transposase Platform for the development of stable Invenra B-Body® Bispecific Antibody expressing CHO lines that generated unprecedented antibody titer with minimal side-product though the optimization of chain ratios and a well-considered clone selection approach. The resulting CHO lines for three separate Invenra B-Body bispecifics produced among the highest yields observed for bispecific antibody production and permitted the development of a robust, manufacturing protocol with anticipated final yields near or more than 6g/L and readily scalable to kg levels. Additionally, early-stage pools produced via Leap-In Transposase were of sufficient quality to supply preclinical studies and accelerate development. Details of the cell line development process will be described.

Finally, looking forward, we are exploring the application of the Leap-In Transposase Platform to the generation of novel, cell therapeutics. Because transposases efficiently integrate very large cargo, we are exploring the creation of therapeutics not possible with standard viral transduction methods. We will present our initial data on this topic and thoughts about future directions.

Learning Objective:
• How the leap-In platform works for chain ratio balancing for bispecifics & multispecifics

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Categories:
SCIENCE & TECH
Who can view: Everyone
Webinar Price: Free
Webinar ID: f85802c88980
Featured Presenters
Webinar hosting presenter
Amalgamator of Business and Biology, ATUM
Dr. Oren Beske joined ATUM in 2019 and brings nearly 20 years of industry experience to the team. Notably, Dr. Beske was President of Aragen Biosciences, Inc. where he led a multidisciplinary team to bring value added services to the biologics industry. Most recently, he served as the CEO of Alloy Therapeutics, Inc. a start-up antibody discovery platform company. Dr. Beske received a BS in Physiology and Biochemistry from CSULB and his Ph.D. in Cell Biology from UC San Francisco.
Webinar hosting presenter
Senior Director, Protein Sciences, Invenra
Nicholas Marshall, PhD, adds a diverse background in protein biochemistry, biophysical characterization, protein engineering, and process development to Invenra. As the leader of the Protein Sciences group, Nick oversees production and characterization of R&D phase molecules, including biophysical characterization and developability assessments of lead molecules. Nick brings more than 10 years of experience in therapeutic protein discovery and drug development. Prior to joining Invenra, Nick worked in Process Chemistry Research and Development at Merck (MSD), where he used directed evolution and high throughput methods to develop enzymes needed for biocatalytic synthesis of active pharmaceutical ingredients. Before Merck, Nick worked with Everett Stone and George Georgiou at the University of Texas at Austin to discover therapeutic enzymes for immune oncology. Nick holds a PhD in Chemical Biology from the University of Illinois where he studied electron transfer in proteins.
Attended (54)
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