Fluidity One-M

Robust results. Simple to run.

MDS is performed in solution, directly in patient serum, without requiring immobilization of antibody or antigen on a solid surface allowing detection of a specific interaction in a complex background like serum.

Vasilis Kosmoliaptsis

Transplant Surgeon, University of Cambridge

Why the Fluidity One-M?

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Multi-attribute results:

Binding affinity (KD), concentration, stoichiometry, and size, all at once

In-solution, purification-free:

Analyze disease-relevant proteins closer to their native environment and avoid non-specific surface binding, avidity, and misfolding.

Small sample volumes:

Meaning more replicates and more material available for orthogonal characterization

Maintenance-free design:

No fluidics in the instrument avoids clogging, priming, or flushing

Plate-based consumables:

Enable quick sample load with multi-channel pipettes. No cross-contamination.

Easy access:

Easy-to-use user interface & guided experimental setup. Enable automated data analysis from sample to publication-ready results.

Complex research in a simple workflow

Preparation

10 minutes

Transfer

3 minutes

Measurement

25 minutes

Analysis

2 minutes

Making protein interaction measurement robust and
hassle-free

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4 µL

Sample volume per data point enables KD determination with as little as 50 µL of sample

1-20 nm

Range for size measurement, covering peptides to multiprotein complexes and fibrillar aggregates

25 minutes

To generate 24 data points, providing a full binding curve and KD value

from pM to µM

Range for affinity measurement, covering high and low affinity systems

Learn how your peers

used the Fluidity One-M

Understand immune response to SARS-CoV-2 variants

Emmenegger et al. from the University Hospital Zurich, report that serum antibodies against the wild-type, delta, and omicron variants of SARS-CoV-2 have similar affinity, indicating a broad cross-clade immune response. Changes in antibody titers were primarily driven by B-cell expansion, rather than affinity maturation, after infection or vaccination.

Emmenegger, Marc, et al. “Both COVID-19 infection and vaccination induce high-affinity cross-clade responses to SARS-CoV-2 variants.” Iscience 25.8 (2022).

Study the mechanism of action of anti-Aβ antibodies

Linse et al. combine kinetic analyses with MDS binding measurements to address the mechanism of action of four clinical stage anti-Aβ antibodies. They quantify the influence of these antibodies on the aggregation kinetics and on the production of oligomeric aggregates and link these effects to the affinity and stoichiometry of each antibody for monomeric and fibrillar forms of Aβ. Their results reveal that, only one of these four antibodies dramatically reduces the flux of Aβ oligomers which is linked to its inhibitory potential.

 

Linse, Sara, et al. “Kinetic fingerprints differentiate the mechanisms of action of anti-Aβ antibodies.” Nature structural & molecular biology 27.12 (2020): 1125-1133.

Fluidic Sciences Ltd