OpenSPR Surface Plasmon Resonance (SPR) System

Accelerate your research with binding kinetics & affinity data on your benchtop

OpenSPR Benchtop Surface Plasmon Resonance System OpenSPR Benchtop Surface Plasmon Resonance System

Affordable benchtop SPR system for any lab

The OpenSPR system is an affordable benchtop instrument for in-depth label-free binding kinetics in your own lab. No need for costly & inconvenient core facilities to get that binding affinity data.

User-Friendly

The OpenSPR system is a user-friendly SPR instrument, regardless of the researchers' experience. Save time & optimize with a wide range of affordable sensor chips. No complicated biomolecule labelling required

Real-Time Data with low sample volumes

Publish faster with label-free binding kinetics & affinity data with volumes of 5–100 μL. Real-time data generated by the OpenSPR includes kon, koff, KD, specificity and yes/no binding.

Data accuracy and quality are comparable to Biacore ™ and IBIS ™ SPR systems. Read the application note.

Low Maintenance

Forget about expensive service contracts so you can focus on your research: this benchtop OpenSPR SPR system requires low maintenance.

You can now investigate real-time binding events like on rate (kon), off rate (koff), affinity (KD), specificity and yes/no binding between various biomolecules in your own lab, with results within 1 hour!

Download our free SPR E-book to learn more about the OpenSPR technique.

The affordable, benchtop SPR sytem brings you comparable results to  Biacore ™ and IBIS ™ SPR systems for a much lower price. With 400+ OpenSPR Systems installed worldwide, the number of publications is continuously growing.

Molecule binding curve generated with Nicoya's OpenSPR system. Real-time analyte-ligand association (2-3) & dissociation (4) data give detailed insight into the binding strength and stability of the biomolecule interaction. Molecule binding curve generated with Nicoya's OpenSPR system. Real-time analyte-ligand association (2-3) & dissociation (4) data give detailed insight into the binding strength and stability of the biomolecule interaction.
 
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