Novel Applications of Histidine-Tagged Protein Capture Using the ProteOn™ XPR36 System
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March 17, 2017
"For more info, visit http://www.bio-rad.com/yt/13/proteonwebinar. Jay Duffner, a senior scientist at Momenta Pharmaceuticals, presents techniques for improving results in the measurement of binding kinetics of antibodies to histidine-tagged protein targets using the ProteOn system. Techniques discussed include capture conditions for histidine-tagged proteins, the reduction of non-specific binding, chip regeneration techniques, and measurement of ligand activity over the course of an assay. The ProteOn HTG sensor chip is functionalized with a novel tris-NTA complex for improved capture of histidine-tagged proteins. This tris-NTA complex is unique to the ProteOn HTG and HTE chips and provides excellent binding stability and regeneration capability in the capture of histidine-tagged proteins. The HTG chip has a compact binding capacity and is most suitable for protein-protein and protein-peptide interaction analysis. Features and Benefits: • Full compatibility with the ProteOn XPR36 protein interaction array system • Improved binding capacity and stability due to the novel tris-NTA formulation • Reduced decay of ligand over time – ensures reliable results and no cumbersome software corrections are needed • Capture of histidine-tagged proteins directly from crude media, reducing work-up labor and required sample volumes • Enhanced efficiency and reduced costs due to surface regeneration ability (typically 10 or more surface regeneration cycles) • Surface regeneration combined with One-shot Kinetics™ technology yields exceptionally high throughput http://www.bio-rad.com/evportal/destination/product?catID=cfcf89c2-a3c9-454d-857c-4bb2f156f924&WT.mc_id=yt-pfd-ww-proteonxpr36-20130624-Nw7-80LlC4M"
Drug Discovery
