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Elucidate binding effects of antibodies within the 2D membrane-constrained cellular environment, taking into account the effects of epitope, steric hindrance, and multivalency.
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Cell Avidity

Revolutionize binding for the future of cell & antibody therapeutics

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Why Cell Avidity?

Keeping up with the complexity of binding mechanisms

Many immunotherapies adapt to solve the field’s most pressing issues (an intricate balance between persistence, potency, and safety) by integrating multiple signaling mechanisms and engaging with more than one domain (e.g., biparatopic and polyvalent antibodies). With that trend, the binding mechanisms between binder and target also complexify. Molecular binding assays like tetramer binding and surface plasmon resonance (SPR) measure preconditions for binding, providing limited insights into actual cell binding. Focusing on isolated ligand-receptor interactions or abundance on a molecular level, they can miss the cellular context and often do not correlate well with functional outcomes.
Overcome these challenges with Cell Avidity:
  • Generate direct, physiologically relevant measurements of binding in its full, dynamic complexity
  • Understand the mechanism of action of your therapeutic products by revealing its complex binding dynamics
  • Balance potency and safety by optimizing binding

Cell Avidity measures true binding of biparatopic antibodies

Mechanistic issues limit the effectiveness of many current cancer-targeting antibody therapies, with monospecific antibodies often hindered by receptor dimerization and activation. Biparatopic antibodies, which bind to two unique non-overlapping epitopes, offer a promising solution with stronger binding, more potent antagonism, and higher specificity. 

Case study

Binder screening & optimization
William Sellers, MD
Professor of Medicine

FGFR2 fusion genes confer sensitivity to FGFR2 kinase inhibitors like Pemigatinib, which saw accelerated FDA approval. However, response rates are hampered by tumor resistance from arising FGRF2 mutations.  The researchers showed that the ECD of FGFR2 is necessary for a full oncogenic transformation by FGFR2 fusion. This makes the ECD a promising target for antibody therapies. Biparatopic antibodies present a promising opportunity for targeting FGFR2 owing to increased binding, specificity, and lower likelihood of inter-protein crosslinking. It was hypothesized that the most effective biparatopic antibodies would show both high affinity and high Cell Avidity.

Binding affinity and avidity screening of biparatopic antibodies candidates. Cell Avidity assay shows increased avidity (% bound beads) of biparatopic antibodies (blue/purple) compared to monospecifi c antibodies B, C and D (grey).

Overview of the experimental setup. Left: Visualization of the monospecific antibody epitope sites (A-F) mapped to the FGFR2 extracellular domain (ECD). Center: workflow representation of the generation of the 15 biparatopic antibodies (A/B to E/F) from their monospecific constituent parts (illustrated by F40SL + K409R) by controlled Fab-arm exchange. Right: Viability assay output comparing the 15 biparatopic antibodies with the 6 monospecific antibodies (and an IgG1 negative control) on their growth inhibition of FGFR2-fusion-driven BaF3 cells.

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Cell Avidity measures true binding of biparatopic antibodies

App Notes

Mechanistic issues limit the effectiveness of many current cancer-targeting antibody therapies, with monospecific antibodies often hindered by receptor dimerization and activation. Biparatopic antibodies, which bind to two unique non-overlapping epitopes, offer a promising solution with stronger binding, more potent antagonism, and higher specificity.

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White Paper
Solutions

Avidion

The next generation Cell Avidity platform

Ideal for cell therapy candidate screening and large characterization studies. Run up to 4 disposable 48-well cartridges a day for a total of 192 measurements with <80 min. hands-on time.
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Avidigo

White glove Cell Avidity services

Full-service contract research from experimental design to data report based on Cell Avidity measurements at high throughput.
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z-Movi

For small sized Cell Avidity studies

A fast and simple solution for single-sample Cell Avidity experiments. Run up to 20 measurements per day.
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Publications

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Text Link

Identification of potent biparatopic antibodies targeting FGFR2 fusion driven cholangiocarcinoma

Chaturantabut et al.,
2025
J. Clin. Investigation
Author Empty
Antibody Therapy
Publication

Relevant resources

Learn as much as you can by reading up on our application notes or marathoning our webinars.

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Unveiling a one-to-one relationship of TCR-dependent T cell function and cellular avidity at single-cell level using acoustic force

Unveiling a one-to-one relationship of TCR-dependent T cell function and cellular avidity at single-cell level using acoustic force

Webinar
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TCR- and BsAb-induced interaction drives avidity-based cellular immunotherapy efficacy

TCR- and BsAb-induced interaction drives avidity-based cellular immunotherapy efficacy

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Cell Avidity screening deployed by T cell pioneers to accelerate the identification of functional TCRs

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Scientific update
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Antibody Therapy

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Cell Avidity measures true binding of biparatopic antibodies

Cell Avidity measures true binding of biparatopic antibodies

Application note
01-01-20
01-01-20

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