MP-SPR NAVI™ 410A Kauris

• 4 independent fluidic channels for simultaneous measurements on a single sensor

• Fully automated operation for efficient and unattended measurements

• High sensitivity for studying a wide range of molecular interactions

• Real-time, label-free measurement of binding affinity and kinetics

• KineticTitration™ for faster affinity and kinetic measurements, particularly for interactions where surface regeneration is difficult

• Two wavelengths per measurement channel for detecting layer thickness and conformational changes

• Wide angular range of 40°–78°, enabling analysis of small molecules, proteins, nanoparticles, and living cells

• Integrated buffer degasser and precision syringe pumps

• 7-vial liquid autosampler for automated measurements

• Supports PureKinetics™ for determining true binding kinetics without requiring a reference channel

• Temperature control from 15 to 45°C

• Compatible with a wide range of sensor surfaces, including Au, SiO₂, CMD, BND, NTA, and regenerable avidin

The MP-SPR Navi™ 410A KAURIS is a fully automated, high-sensitivity 4-channel Multi-Parametric Surface Plasmon Resonance (MP-SPR) instrument designed for real-time, label-free analysis of molecular interactions and biological systems. The system simultaneously measures four channels on a single sensor, enabling efficient analysis of multiple samples or experimental conditions. With two wavelengths in each measurement channel, the 410A KAURIS can provide information on binding interactions, layer thickness, and conformational changes. Its wide angular measurement range of 40°–78° allows researchers to investigate a broad range of analytes, from small organic molecules and proteins to nanoparticles and living cells. The integrated 7-vial autosampler, degasser, and precision syringe pumps support fully automated and unattended measurements. The KineticTitration™ feature enables faster affinity and kinetic measurements by allowing analyte concentrations to be introduced sequentially, making it particularly useful for interactions where regeneration of the sensor surface is difficult or may affect the ligand.

Molecular Interaction Studies Real-time analysis of molecular binding, affinity, and kinetic interactions without fluorescent or radioactive labels. Biophysics Investigation of molecular binding mechanisms, conformational changes, and surface interactions. Drug Discovery & Biopharmaceutical Research Characterization of interactions involving small molecules, peptides, proteins, antibodies, membrane receptors, and other biological molecules. KineticTitration™ can accelerate affinity and kinetic measurements. Biosensor Development Evaluation of receptor–analyte interactions and functionalized surfaces for label-free biosensing. Biomaterials & Biocompatibility Study of molecular and cellular interactions with biomaterial surfaces and coatings. Living Cell Research Real-time investigation of cell adhesion and cell–surface interactions using suitable flow-cell configurations. Nanoparticle & Extracellular Vesicle Research Characterization of interactions involving nanoparticles and extracellular vesicles, including affinity, kinetics, size, and concentration studies with appropriate sensor surfaces and analysis tools.