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Affinity Tag Protein Purification - Day 1



Affinity Tag Protein Purification Banner

Day 1  |  Day 2 

Affinity tags are highly efficient tools for purifying proteins from crude extracts. To maintain a competitive edge, it is important to choose the right tag for the job and to address issues such as quality, efficiency and cost effectiveness. This conference address key questions such as: Which resins are optimal for which procedure? Do tags need to be removed and if so, how? What are possible validation steps to show that tags are not in the final product? What are the newest tagging technologies? Self cleaving vs. proteases, what are the differences and advantages? Is there an optimal way to ensure high yields, high speed and low costs?


Monday, August 23

12:00pm Conference Registration

 

Tags – New and Improved

1:30 Chairperson’s Opening Remarks

1:40 FEATURED PRESENTATION

Tag Technologies: Opportunities and Challenges in the Biopharmaceutical Industry

David Wood, Ph.D., Associate Professor, Dept. of Chemical & Biomolecular Engineering, Ohio State University

Although affinity tag technologies have been ubiquitous in the laboratory for decades, they have yet to make a significant impact in large-scale protein manufacturing.  This is primarily due to the requirement for tag removal from the purified product, which leads to a number of complex processing and regulatory issues.  Recently, several new technologies have been developed to address these limitations, ranging from novel self-cleaving tags, to improved ligands and resins.  This talk will examine the remaining obstacles to the more general adoption of these platform methods, and showcase some of the newer technologies available.

2:10 A Closer Look at Different Protein Tags - Exploring the Pluses and Minuses

Demetrios Vavvas, M.D., Ph.D., Instructor, Ophthalmology, Massachusetts Eye & Ear Infirmary, Harvard University 

2:40 Extensive Crosstalk between O-GlcNAcylation and Phosphorylation is Revealed by Novel Photocleavable Tags Combined with Electron Transfer Dissociation Mass Spectrometry

Gerald W. Hart, Ph.D., Professor & Director, Department of Biological Chemistry, Johns Hopkins University, School of Medicine

Ser(Thr)-O-linked beta-D-N-acetylglucosamine (O-GlcNAc) is an abundant and dynamic modification of nuclear and cytoplasmic proteins. O-GlcNAc regulates signaling and transcription in response to nutrients and stress (for reviews, Nature 446, 1017-1022; Am J Physiol Endocrinol Metab 295:17-28; J. Cell Sci. 123, 13-22). O-GlcNAcylation underlies glucose toxicity and impaired insulin signaling in diabetes, regulates oncogene and tumor suppressor proteins, and plays important roles in neurodegenerative disease. Progress in the study of O-GlcNAcylation has been severely hampered by difficulty in its detection and in mapping sites of attachment. Recently, chemico-enzymatic tagging of O-GlcNAc, combined with Click chemistry to attach photocleavable biotin moieties, and affinity enrichment of tagged-O-GlcNAc-peptides, have allowed highly sensitive detection and site mapping of O-GlcNAc via electron transfer dissociation (ETD) mass spectrometry (Molec Cell. Proteomics 9: 153-160; Science Signaling 3 (104), ra2). These methods have revealed that O-GlcNAc is not only surprisingly highly abundant on nuclear and cytoplasmic proteins, but also that it has an unexpected degree of extensive crosstalk or interplay with protein phosphorylation to regulate cellular processes.

Sponsored by
Forte Bio
3:10 Rapid Detection and Screening of HIS-tagged Proteins Using Simple, Label-Free Dip and Read Assay
Sriram Kumaraswamy, Ph.D., Product Manager, ForteBio, Inc.
Methods currently used for the quantitation of His-tagged proteins have limitations such as interference from other sample components, need for slow and laborious sample purification, multiple assay steps and lack of sufficient throughput.  ForteBio’s anti-penta HIS biosensors have been developed as a simple, one-step, Dip and Read method on the Octet label-free detection platform for the quantitation and detection of His-tagged proteins.  The system is especially suited for high-throughput expression screening and the optimization of protein expression systems where sample purification needs to be avoided.  The assay utilizes the Octet optical biosensing platform and involves direct, label-free detection and quantitation of his-tagged proteins that bind to highly specific penta-HIS antibody pre-immobilized on Octet biosensors.  The anti-penta HIS biosensors complement other pre-fabricated and custom biosensors on the Octet platform to provide a comprehensive set of tools for use in the entire bioprocess workflow from cell line development to production monitoring and quality analysis.

3:30 Networking Refreshment Break With Exhibit and Poster Viewing

4:15 Moderated Small Group Breakout Discussions

Join an informal, facilitated discussion group, designed to discuss important and challengeing topics related to affinity tags and protein purification. This unique session allows confrerence participants to exchange ideas, brainstorm, and have an incteractive problem solving discussion. Furthermore, these breakout groups bring together scientists who share a common interest in specific topics to develop future collaborations around a focused topic.
These forums are open for discussion of scientific challenges and are not sales opportunities. We emphasize that this breakout session is for an interactive exchange amongst scientists and is not meant to be in any way a corporate or product discussion.

5:15 Breakout Group Discussion Summaries

The facilitators of the breakout group discussions will present a brief synopsis of the discussions.

5:30 Reception in Exhibit Hall

6:30 End of Day One

Day 1  |  Day 2



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