Bio-Rad Laboratories's Proteon HTG Sensor Chip provides a alternative for pharmaceutical researchers studying polyhystidine-tagged protein interactions.
Used with Bio-Rad's Proteon XPR36 system, the HTG Sensor Chip's surface chemistry has increased binding stability and specificity for His-tagged proteins compared with chips from other surface plasmon resonance (SPR) system providers, according to the company.
Additionally, the HTG Sensor Chip's ability to regenerate and reuse HTG chips multiple times can significantly reduce the cost of generating data, according to the company.
The Proteon HTG Sensor Chip's Tris-NTA complex contains three NTA molecules for improved binding stability and selectivity to His-tagged molecules.
This results in better data quality and reduced ligand decay.
Furthermore, binding via polyhistidine tag is reversible, so the ligand can be removed from the surface and the chip can be re-used ten times or more.
This increases reproducibility by eliminating chip-to-chip variability decreases cost per data point.
To optimise the polyhistidine-tagged protein interaction workflow, Bio-Rad has also introduced the Proteon HTG Reagent kit for use with the Proteon HTG Sensor Chip.
The kit includes NiSO4 for chip activation and an EDTA solution for chip regeneration.