Collaboration Improves Characterization of Monoclonal Antibodies Targeting Integral Membrane Proteins
Product News Feb 05, 2009
Bio-Rad Laboratories, Inc. has announced collaboration with Integral Molecular, Inc. to offer the first system for reproducibly characterizing the binding affinities of antibodies to diverse integral membrane proteins, including GPCRs and ion channels.
Integral Molecular, a solution provider for scientific research and drug discovery applications involving integral membrane proteins, has developed a technology, the Lipoparticle, that enables integral membrane protein interactions to be measured using Bio-Rad’s label-free, high throughput ProteOnÔ XPR36 Protein Interaction Array System.
Integral Molecular’s proprietary Lipoparticle technology offers scientists working with membrane-bound targets a standardized reagent with higher concentrations of membrane proteins than cell membrane preparations. Lipoparticles exploit the self-assembling machinery of non-infectious viral core proteins to create non-living, stable, homogenous nanoparticles comprising a lipid bilayer incorporating highly concentrated target receptors.
Bio-Rad’s ProteOn XPR36 is a multiplexed 6x6 SPR array that permits the label-free kinetic analysis of 36 different protein interactions in a single experiment, more than any other system. When used in combination, Lipoparticles and the ProteOn will enable scientists to reproducibly screen membrane protein targeting antibodies for binding characteristics.
Integral Molecular offers Lipoparticles as a product for customers to study their own membrane protein interactions, and now also offers services using Bio-Rad’s ProteOn instrument. Customers can submit sequences of integral membrane proteins to Integral Molecular, who will incorporate the proteins into Lipoparticles.
Lipoparticles can then be coupled to the ProteOn sensor surface and customers’ monoclonal antibodies flowed across the chip in order to measure overall binding strength (affinity, KD) and individual molecular association and dissociation rates.