Monoclonal antibodies
Rank clones by off-rate to find the slowest dissociating binders.
Full kinetics and affinity for every lead candidate.
kon, koff, KD
Characterize antibody affinity and kinetics across every format
Monoclonals, bispecifics, nanobodies. inQuiQ measures how each one binds, label-free and in real time, on your own bench.
Label-free binding data for every antibody format
Each format has its own testing needs. inQuiQ covers them from one platform.
Bispecifics and multispecifics
Confirm that both arms reach their targets.
Sequential and simultaneous assays check each arm separately.
dual engagement
Nanobodies (VHH) and fragments
Clean kinetics from low molecular weight formats.
VHH, scFv, and Fab produce only a small mass change on binding.
low mass
Antibody-drug conjugates
Check that conjugation has not altered target binding.
Compare the ADC against its parent antibody under the same conditions.
parent vs conjugate
Fc-engineered and Fc-fusion proteins
See how Fc changes affect binding to antigen and partner proteins.
A temperature series adds thermodynamic detail.
temperature series
Don't see your application?
Discuss your application with one of our application specialsts.
Talk to a specialist
Why antibody workflows can be challenging
01 / 04
One injection reads sixteen sensors.
Targets and cross-reactivity controls measured together, so the panel moves as a batch instead of a queue.
*spotter necessary for 16-sensor immobilisation
30 µL minimumrun in series
four channels, sixteen sensors
Detection range down to 10 pM.
A small mass change still resolves into a full curve, so VHH, scFv, and Fab return real kinetics.
10 pM to 10 mMkon, koff, KD
weak binder still resolves
Measure in native, label-free conditions.
The binder and its target meet unmodified, and the sensor reads the interaction itself rather than a reporter standing in for it.
- No fluorescent or radioactive tag on either partner
- Binding measured exactly as it happens in solution
the same binding event
Rank straight from crude supernatant.
The sample flows over the sensor after one filter step, and the antifouling hydrogel reduces non-specific binding. Trusted data, fewer purification steps.
no buffer constraints
crude sample reaches the sensor
How an antibody binding run works
Every measurement follows the same five steps, whatever the format. The antigen or the antibody goes on the sensor, the binding partner flows past, and the instrument records the response in real time. An ELISA gives you one number at the end. inQuiQ gives you the full curve.
Immobilisation
The partner that stays put is attached to the sensor surface first.
Antigen coupled directly, or antibody held by a capture reagent. That choice matters for IgG: a captured bivalent antibody meeting surface-bound antigen binds with both arms, so the result reflects avidity rather than monovalent affinity. Immobilise the antigen instead and you read one arm at a time.
- immobilisation
- capture
- avidity vs affinity
Deactivation
Any activated site left unused is capped before the sample arrives.
Without it the surface keeps reacting with whatever passes over, and non-specific binding shows up in the trace as signal that has nothing to do with the pair being measured. The response settles at a stable level, the immobilised amount.
- deactivation
- blocking
- non-specific binding
Association
The sample flows across the surface and the response climbs.
Purified protein or crude hybridoma supernatant after a 0.22 µm filter, both go in the same way. Flow between 1 and 100 µL/min sets contact time, which matters for a nanobody or scFv producing only a small mass change. The rising phase gives the on-rate, kon.
- association
- crude supernatant
- kon
Dissociation
Buffer replaces the sample and the response falls as the complex comes apart.
The falling phase gives the off-rate, koff, and it can be read on its own, which is why clones can be ranked before any of them is purified. Fit a concentration series and you get kon, koff, and KD: separate cycles for multi-cycle kinetics, one uninterrupted series for single-cycle when material is scarce.
- dissociation
- koff
- KD
- SCK and MCK
Regeneration
A regeneration buffer strips the remaining analyte and returns the sensor to baseline, ready for the next run.
The immobilised partner stays in place, so every clone in an affinity maturation series meets the same surface under the same conditions. Inject, read, regenerate, repeat, unattended. And every injection is read by all sixteen sensors at once, so one sample can cover sixteen targets, variants, or cross-reactivity controls.
- regeneration
- automated cycling
- affinity maturation
Response (RU)
Time
What inQuiQ does for antibody characterization
Six capabilities, one benchtop instrument, no labels anywhere in the workflow.
Many candidates, one small sample
4 channels to read a single injection, so targets and controls are measured together.
10 samples
30 µL
Map epitopes and binding sites
Competitive and cross-blocking assays sort a panel into bins.
epitope binning
Full kinetics for every candidate
Single-cycle and multi-cycle runs give the whole curve, not an endpoint.
10 pM to 10 mM
Confirm dual engagement
Sequential and simultaneous assays check that both arms of a bispecific reach their targets.
per-arm kinetics
Add thermodynamic detail
The temperature-controlled flow cell runs a full temperature series.
temp. control from 16 to 40 °C
Modular system for an increased throughput
Simply add an autosampler, and increasy your throughput for library screens.
2×384 wells
Application notes, publications, and data
From antibody affinity to small molecule kinetics, 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
See inQuiQ run your antibody assay
Tell us your panel, your formats, and the binding questions you need answered. We will show you inQuiQ on an assay close to yours.
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
Immobilize the antigen or capture the antibody on the sensor, then inject a concentration series of the binding partner. inQuiQ records association and dissociation in real time and fits the data to give affinity (KD) and kinetics (kon, koff), across a range of 10 pM to 10 mM, without any label.
Off-rate ranking sorts candidates by how slowly they release their target, since a slow off-rate (koff) often signals a stronger, longer-lived interaction. inQuiQ captures each antibody, records dissociation in real time, and ranks the panel by koff, so you can shortlist the slowest dissociating binders early, even from crude supernatant.
Epitope binning groups a panel of antibodies by the region of the antigen they bind. Antibodies that block each other likely share an epitope, while pairs that bind together fall into different bins. inQuiQ runs competitive and cross-blocking assays that reveal these bins and show which candidates compete for the same site.
A bispecific must engage both of its targets to work. inQuiQ confirms this with sequential and simultaneous binding assays: capture the bispecific, inject the first antigen, then the second, and watch whether both bind. You get affinity and kinetics for each arm and confirmation that the molecule bridges both targets.
A nanobody (VHH) is small, so binding produces only a small mass change that some label-free platforms miss. inQuiQ measures binding across an affinity range of 10 pM to 10 mM and returns full kinetics (kon, koff) and affinity (KD) for VHH, scFv, and Fab formats from as little as 30 µL of sample.