The ProteOn XPR36 protein interaction array system is a surface plasmon resonance (SPR) biosensor that is used to monitor, in real-time, the affinity, specificity, and interaction kinetics of biomolecular interactions on the surface of a sensor chip. Depending on their surface chemistry, different sensor chips can be used for various applications, such as protein-protein interaction analysis, protein-small molecule interaction analysis, and protein-lipid interaction analysis.
The ProteOn HTG sensor chip is functionalized with tris-NTA and is specifically designed for capturing histidine-tagged proteins. Jay Duffner, a senior scientist at Momenta Pharmaceuticals, recently presented his work measuring the binding kinetics of antibodies to histidine-tagged protein targets using the ProteOn system, at the Society for Laboratory Automation and Screening (SLAS) conference in San Diego.
In this tutorial below, Duffner describes in detail how to optimize the analysis of antibody binding to histidine-tagged proteins captured to the HTG sensor chip. Duffner initially encountered several issues such as loss of analyte response and nonspecific binding in his experiments. Duffner utilized the high throughput capabilities of the ProteOn system and was quickly able to develop a viable assay for measuring antibody binding kinetics against histidine-tagged targets.