Histidine-Tagged Protein Capture Using the ProteOn™ XPR36 System





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Published on Jun 25, 2013

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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


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