Biomolecular Interaction Analysis with the ProteOn™ XPR36 System





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Published on Dec 10, 2012

For more info, visit http://www.bio-rad.com/yt/7proteonxpr36.
Surface plasmon resonance (SPR) is employed as an excellent technology for measuring biomolecular interactions in real-time in a label-free manner. Using this method, one of the interacting partners (ligand) is immobilized to the sensor surface, while the other (analyte) is free in solution and passed over the surface. The kinetic parameters of the interactions are further calculated from association and dissociation sensorgrams. This lecture introduces the ProteOn XPR36 system, an SPR optical biosensor featuring a 6 x 6 interaction array for the simultaneous analysis of up to six ligands with up to six analytes which enables the analysis of up to 36 different protein interactions in one run on a single chip. A protein-protein interaction, of adenylate cyclase toxin (CyaA) with integrin receptor CD11b/CD18, a lipid-protein interaction, of phosphatidylinositol 4,5-bisphosphate (PIP2) with membrane channel TrpV1, and a DNA-protein interaction, of transcription factor FoxO4 with target DNA, are presented to demonstrate the throughput, flexibility, and versatility of this instrument.

Dr. Ladislav Bumba
Institute of Microbiology AVCR
Prague, Czech Republic


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