單株抗體

5月 1日 (四)

1:00 - 1:30 pm Registration

1:30 Chairperson's Opening Remarks

KEYNOTE PRESENTATION 
1:40 Discovery of Fv and its Utilization as a Modular Fragment in Constructing Therapeutic Antibodies
David Givol, Ph.D., Professor, Department of Molecular Cell Biology, Weizmann Institute
The discovery of Fv (1972) as the minimal antibody fragment that retains the full binding and specificity completed our understanding of the domain structure of the antibody. The demonstration that Fv can be denatured and refold autonomously to regain its original binding properties made it the ideal candidate for preparation of chimeric antibodies between species (mouse/human) or isotypes (antibody classes). This boosted the industry of therapeutic antibodies in the mid nineties that was not so effective in its original use of mouse monoclonals. The increased stability by making single chain Fv and the technology to increase affinity by mutating or grafting the CDR made the recombinant Fv a basic tool at the foundation of antibody technology. This led to multitude of variants of engineered molecules based on Fv, like minibodies ,diabodies, Di-diabodies, bispecific scFv, T-bodies (redirected T cells) and the list is still increasing.

SELECTION AND CHARACTERIZATION

2:10 Label-Free Antibody Characterization on Arrays 
Voula Kodoyianni, Ph.D., Chief Scientific Officer, R&D, GWC Technologies, Inc.
SPR imaging (SPRi) is a label-free method for monitoring interactions between biomolecules on arrays. SPRi quantifies changes on the whole array in real time. The platform capabilities are especially appealing for antibody analysis, since antibody-antigen interactions can be characterized in different ways, for example: (i) antibody-antigen affinities can be obtained by spotting either purified antibodies or ascites, using either kinetic or equilibrium data (ii) antibody pairs suitable for sandwich immunoassays can be identified, and (iii) immobilization chemistries and how they affect antibody activities can be evaluated and optimized.

2:40 Solutions Showcase I (Sponsorship Available) 

2:55 Solutions Showcase II (Sponsorship Available)

3:10 Refreshment Break in the Exhibit Hall

4:00 To Be Announced

4:30 New Mapped Monoclonal Antibodies for Disaggregation of Fibrils
Elena L. Paley, Ph.D., Department of Urology, Northwestern University Feinberg School of Medicine
The presentation will show the epitope mapping and characteristics of new monoclonal antibodies to protein biosynthesis enzyme (tryptophanyl-tRNA synthetase). The conformation-dependent epitopes for these antibodies have been mapped to amino- and carboxyl-termini of the natural (non-recombinant) enzyme. The antibodies can detect aggregated forms of the enzyme and disaggregate the fibrils self-assembled by the enzyme.

5:00 pm End of Day