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
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Benefits of the inQuiQ in antibody research
01 / 04
One injection, four channels, sixteen sensors.
Four independently addressable flow channels, each carrying four sensors, with the sample flowing through the channels in series.
30 µL minimumsequential flow paths
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.
one 0.22 µm filter step
crude sample reaches the sensor
How does antibody binding analysis work?
Every antibody binding measurement follows the same five steps. One partner is captured on the sensor, the other flows past, and the binding response is recorded in real time. An ELISA gives one endpoint. The inQuiQ gives the whole curve.
Immobilisation
One partner is captured on the sensor surface first.
Antigen coupled directly, or antibody held by a capture reagent. A captured bivalent IgG meets surface-bound antigen with both arms, so the result reflects avidity. Immobilise the antigen instead and you read monovalent affinity.
- immobilisation
- capture
- avidity vs affinity
Deactivation
Any activated site left unused is capped before the sample arrives.
Without capping, the surface keeps reacting with whatever passes over and non-specific binding appears in the trace, unrelated to the pair measured. The response settles at 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 can both be measured. Flow sets the contact time, which matters for small analytes such as a nanobody or scFv. 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 can be read on its own, so clones can be ranked before purification. Fit a concentration series for kon, koff, and KD: multi-cycle kinetics, or 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 put, so every clone in an affinity maturation series meets the same surface. Inject, read, regenerate, repeat, unattended. Every sensor reads the same injection: up to sixteen targets or cross-reactivity controls from one sample.
- regeneration
- automated cycling
- affinity maturation
Response (RU)
Time
What the 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
Epitope binning and affinity ranking
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 of bispecific antibodies
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 increase your throughput for library screens.
2×96 wells
2×384 wells
Application notes, publications, and data
From antibody affinity to small molecule kinetics, explore real binding data generated on the inQuiQ. Each application note pairs a sensorgram with the affinity and kinetic values behind it.
Start A conversation
See the 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.