Monoclonal antibodies and epitope binning
Rank clones by off-rate to find the slowest dissociating binders.
Measure full kinetics and affinity, with epitope binning to map binding sites.
ka, kd, KD
epitope binning
Antibody characterization, binding affinity and kinetics across every format
From monoclonals and bispecifics to nanobodies, the inQuiQ measures binding label-free and in real time, including affinity, kinetics, and epitope binning.
Label-free binding data for every antibody format
Each format has its own testing needs. The 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
Antibody developability for Fc-engineered formats
See how Fc changes affect binding to antigen, FcRn in an FcRn binding assay, and 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 tags
the same binding event
Rank affinity maturation of antibodies 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 characterization 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.
Immobilization
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. Immobilize the antigen instead and you read monovalent affinity.
- immobilization
- 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 immobilized 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, ka.
- association
- crude supernatant
- ka
Dissociation
Buffer replaces the sample and the response falls as the complex comes apart.
The dissociation phase gives the off-rate, kd, and can be read on its own, so clones can be ranked before purification. Fit a concentration series for ka, kd, and KD: multi-cycle kinetics, or single-cycle when material is scarce.
- dissociation
- kd
- KD
- SCK and MCK
Regeneration
A regeneration buffer strips the remaining analyte and returns the sensor to baseline, ready for the next run.
The immobilized partner stays in place throughout affinity maturation of antibodies. Inject, read, regenerate, repeat. Sixteen targets or controls from one sample let antibody specificity testing run alongside affinity measurement.
- epitope binning
- automated cycling
- affinity maturation
Response (RU)
Time
What the inQuiQ does for antibody discovery
One benchtop label-free biosensor across the antibody discovery workflow, from antigen binding assays to epitope binning and antibody characterization.
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 kinetics and multi-cycle kinetics 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
Explore the inQuiQ768
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 binding 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
request@deltalifescience.nl
Send us an email, and we will get back to you as soon as possible.
request@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. The inQuiQ records association and dissociation in real time and fits the data to give binding affinity (KD) and kinetics (kon, koff), across a range of 10 pM to 10 mM, without any label. The same antigen binding assay format supports antibody characterization across every antibody format on this page.
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. The 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. That covers the material hybridoma screening, phage display screening and yeast display screening actually deliver.
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. The inQuiQ runs an epitope binning assay by competitive and cross-blocking injection, showing which candidates compete for the same site. Binning narrows a panel before the finer epitope mapping methods, paratope mapping among them, are brought in.
A bispecific must engage both of its targets to work. The 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, supporting antibody specificity testing and antibody developability decisions.
A nanobody (VHH) is small, so binding produces only a small mass change that some label-free platforms miss. The 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.