Biomarker quantification
Measure a biomarker in patient serum or plasma and confirm the signal is real binding, not matrix background.
Concentration and binding behaviour read from the same trace.
active concentration
Measure binding kinetics directly in serum, plasma, and CSF
Crude matrices contain proteins and lipids that often generate non-specific binding and false signals. Combined with an antifouling hydrogel surface that minimizes these interactions, the inQuiQ measures affinity, kinetics, and active concentration directly in the sample, in real time, without labeling either binding partner.
Where label-free helps in bioanalysis of complex matrices
Binding measured directly in serum, plasma, CSF, or urine, with no tag on either partner.
Drug concentration and PK-style work
Follow drug-target binding in matrix over time instead of reading a single endpoint value.
Two samples at the same level can behave very differently once you watch them.
kon, koff
Anti-drug antibodies
Characterise an ADA response as kinetics, not only as titre.
Measured in the matrix the sample arrived in, with no tag on either partner.
ADA kinetics
Cytokine and multi-marker panels
Run a target with its controls and related markers from one small sample.
16 sensors on a single chip carry the panel, spotter required.
16 sensors
Diagnostic assay development
Screen capture reagents and surface chemistries against real matrix early.
Find out what holds up in matrix while the assay design can still change.
capture screening
assay development
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Discuss your assay with one of our application specialists.
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Benefits of the inQuiQ in complex biological matrices
01 / 04
Serum and plasma read as clean traces.
An antifouling hydrogel layer limits adsorption of matrix proteins and lipids, and a reference channel carries what remains, so specific binding is separated from background.
bar length shows non-specific signal, not analyte response
antifouling hydrogelreferencing
what sticks, and what does not
The whole binding event, not one endpoint number.
Endpoint methods report how much analyte is there at a fixed timepoint. The inQuiQ records association and dissociation as they happen, so rate, stability, and active concentration all come from the same trace.
kon, koff, KDactive concentration
four injections, or four endpoint numbers
One small sample covers a marker and its controls.
30 µL is enough for a measurement, and 4-plex runs standard in the inQuiQ. With a spotter, 16 sensors carry a biomarker panel, or a target with its mismatch and off-target controls, from a single injection.
*spotter necessary for 16-sensor immobilisation
30 µL minimumup to 2 mL
four channels, sixteen sensors
Filter, inject, and the run is under way.
Unpurified samples go straight in once they have passed a 0.22 µm filter, undiluted or diluted.
- No extraction or cleanup step between the sample and the sensor
- Five-minute warm-up, against roughly an hour or a 24-hour equilibration
- 30 by 40 cm on the bench, beside the samples it measures
0.22 µm filter5 min warm-up
straight from sample to sensor
From sample to sensorgram
Every measurement follows the same steps, whatever the matrix. A capture reagent is immobilised on the sensor, the filtered sample flows past, and the instrument records the response in real time. An endpoint assay gives you one number. The inQuiQ gives you the full curve.
Immobilisation
The capture reagent is attached to the sensor surface first.
Amine coupling or capture through a tag holds it in place on an antifouling hydrogel layer, which limits serum and plasma from sticking to the surface later. A reference channel is prepared alongside, without capture reagent, so bulk and matrix background can be subtracted from every injection that follows.
- amine coupling
- capture
- antifouling hydrogel
Deactivation
Any activated site left unused is capped before the first sample arrives.
Without it the surface keeps reacting with whatever passes over, and in serum or plasma that means matrix proteins and lipids in the trace instead of the pair being measured. The response settles at a stable level, the immobilised amount.
- deactivation
- blocking
- non-specific binding
Association
The filtered sample flows across the surface and the response climbs.
Serum, plasma, CSF, or urine goes in undiluted or diluted, once it has passed a 0.22 µm filter. Flow between 1 and 100 µL/min sets contact time, up to 300 µL/min for low-viscosity samples, and up to 2 mL can be drawn on when a dilute analyte needs longer at the surface. The rising phase gives the on-rate, kon.
- 0.22 µm filter
- referencing
- kon
Dissociation
Buffer replaces the sample and the response falls as the complex comes apart.
The falling phase gives the off-rate, koff, and 1/koff gives residence time. Fit a concentration series and you get kon, koff, and KD in the matrix the sample arrived in. For an ADA response or a drug-target pair, that is the difference between a titre and a kinetic profile, and what is read is active concentration rather than total mass.
- residence time
- koff
- KD
- active concentration
Regeneration
A regeneration buffer strips what remains and returns the sensor to baseline, ready for the next sample.
The immobilised capture reagent stays in place, so every sample in a series meets the same surface. Inject, read, regenerate, repeat, unattended. Each injection is read by every sensor on the chip, so one small sample can cover a marker panel, or a target with its mismatch and off-target controls.
- regeneration
- automated cycling
- saveable sequences
Response (RU)
Time
What the inQuiQ does for work in complex matrices
Six capabilities, one modular benchtop instrument, no label on either binding partner.
Clean signal from dirty samples
An antifouling hydrogel layer limits non-specific binding, so serum, plasma, and CSF can be measured without extensive cleanup.
antifouling hydrogel
serum, plasma, CSF
Real-time ADA and PK-style data
Full on and off rates in matrix, so immunogenicity and drug binding are characterised as kinetic profiles rather than single endpoint values.
kon, koff, KD
Active concentration, not total mass
Binding activity is measured directly, which separates functional analyte from material that is present but not working.
active concentration
A target and its controls from one small sample
25 µL is enough for a measurement, and with a spotter 16 sensors carry a biomarker panel, or a target plus its specificity controls, on one chip.
30 µL minimum
16 sensors (spotter required)
Contact time you control
Flow speed runs from 1 to 100 µL/min, and up to 300 µL/min for low-viscosity samples, to tune resolution for the interaction you are following.
1 to 300 µL/min
Fast to start, small on the bench
A five-minute warm-up replaces the hour, or the 24-hour equilibration, that conventional SPR needs.
5 min warm-up
30 × 40 cm
Application notes, publications, and data
From small molecule kinetics to antibody affinity, explore real binding data generated on inQuiQ. Each application note pairs a sensorgram with the affinity and kinetic values behind it.
Small Molecule Kinetics on inQuiQ
This white paper showcases the high sensitivity of ring resonator technology for measuring low-molecular-weight interactions, using Carbonic Anhydrase II (CAII) and two small-molecule binders as a model system.
APPLICATION NOTE
Antibody interaction analysis
Kinetic characterisation of antibodoes and whatnot
APPLICATION NOTE
Small molecule interactions
Ka and Kd for very tiny small biomolecules.
APPLICATION NOTE
Small molecule interactions
Ka and Kd for very tiny small biomolecules.
Start A conversation
Talk to an application scientist
Bring us a matrix that has been giving you trouble. We will look at the assay design with you.
Ready to see the inQuiQ in action?
Talk to an application scientist
Thirty minutes to discuss your assay design, before anyone mentions an instrument.
Download the inQuiQ brochure
Sensitivity, channel layout, footprint, and consumable formats in a couple of pages.
Delta Life Science
info@deltalifescience.nl
Send us an email, and we will get back to you as soon as possible.
info@deltalifescience.nl
Send us an email, and we will get back to you as soon as possible.
Questions researchers ask
Immobilise a capture reagent on an antifouling sensor surface, then inject filtered serum and follow binding in real time. The antifouling hydrogel limits non-specific adsorption from matrix proteins and lipids. Reference channels correct for bulk effects, so the remaining signal reflects specific binding, giving KD, kon, and koff directly in serum.
Three things do most of the work: surface chemistry that resists adsorption, referencing against a control channel to subtract bulk and background effects, and filtering the sample through a 0.22 µm filter. The antifouling hydrogel layer on the inQuiQ chips handles the first, and the 4-channel chip supports the second.
MSD is an endpoint electrochemiluminescence method: it reports how much ADA is present at one timepoint, with a tag on the detection reagent. Label-free measurement adds real-time association and dissociation with no tag, so an ADA response can be described by its kinetics and stability, not only its level.
No. Unpurified samples run directly once filtered through a 0.22 µm filter, and there are no buffer constraints to match beforehand. Minimum sample volume is 30 µL, and up to 2 mL can be used when a low-concentration analyte needs longer contact time with the sensor surface.
The standard 4-channel photonic chip supports up to 4-plex with no extra hardware. With a microarray spotter, the chip carries 16 sensors, so a biomarker panel or a target plus mismatch and off-target controls can be read from a single small sample injection.