ProteOn used to rapidly screen for binding affinities of reagents
The University of Toronto has selected the ProteOn XPR36 protein interaction array system from US-based Bio-Rad Laboratories to screen protein-specific affinity reagents, including antibodies and antibody fragments as part of an international consortium pilot study arranged by the Structural Genomics Consortium (SGC) and Human Proteome Resource Center.
The University of Toronto has selected the ProteOn XPR36 protein interaction array system from US-based Bio-Rad Laboratories to screen protein-specific affinity reagents, including antibodies and antibody fragments as part of an international consortium pilot study arranged by the Structural Genomics Consortium (SGC) and Human Proteome Resource Center.
The consortium, whose goal is to generate affinity reagents for exploration of the human proteome, chose the multiplexed surface plasmon resonance (SPR) instrument from Bio-Rad for its ability to rapidly screen biomolecular interactions.
Renee LeMaire-Adkins, marketing manager, Protein Interaction Technology at Bio-Rad, said: "The pilot project will generate a wealth of protein-specific reagents that will require a fast, accurate evaluation of their binding affinities.
"The design of the ProteOn XPR36 is ideal for this purpose as it permits the label-free kinetic analysis of six ligands measured against six analytes for 36 data points per experiment."
The result of a workshop in March 2008, the pilot study seeks to demonstrate the feasibility of a variety of methods to generate better affinity reagents for specific protein targets. Researchers from around the world will be sending their affinity reagents to the University of Toronto for testing on the ProteOn and results are expected to be published in the first half of 2009. A second workshop will be held this month where the initial results will be summarised and evaluated.
