Binding affinity and kinetics for academic labs and research institutes

Label-free interaction analysis measures binding between unmodified molecules in real time. It returns affinity (K_D), kinetics (k_a and k_d), specificity, and concentration, without a fluorescent or radioactive tag on either partner. inQuiQ measures across an affinity range of 10 pM to 10 mM.

Yes. inQuiQ can be operated by researchers as part of their existing workflow. Application scientists provide support with assay setup and method development, helping researchers get started without requiring a dedicated biophysicist.

inQuiQ uses nanophotonic evanescent field sensing (NES), like SPR, but with a different sensor architecture that integrates 16 sensors on a single photonic chip. This enables more channels and a high sensitivity while keeping instrument and consumable costs low. BLI uses a dip sensor and is generally less sensitive for small molecules and fragments and for measuring off-rates since it's lacking flow, although it can be more tolerant of unfiltered samples. For applications where high sensitivity, throughput, and cost of ownership matter, inQuiQ offers a strong alternative to both approaches. High quality data without traditional BLI and SPR instrument cost.

Yes. Runs return full sensorgrams with association and dissociation phases, k_a, k_d, and K_D from single-cycle or multi-cycle kinetics, with reference channel subtraction and baseline noise typically below 0.1 RU RMS. Raw and fitted data can easily be used for figures and supplementary material.