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Our Latest Webinar
All antibodies are NOT created equal: Comprehensive profiling of SARS-CoV-2 antibodies
Detecting antibodies that confer effective immunity is crucially important to understand a patient’s immune response to SARS-CoV-2. In particular, the ability to quantify the virus-neutralizing capacity of the immune system is key to support the development of suitable vaccines and antibody-based treatments such as convalescent plasma therapies.
This talk outlines our efforts in assessing the immune response in COVID-19 patients by use of a novel microfluidic in-solution immunoassay platform. With this new approach, we were able to comprehensively profile SARS-CoV-2 antibodies directly in minimally diluted serum of these patients.
Engage with us on demand
Sign up for an upcoming live webinar or view our archive of previous broadcasts, available to view on demand. All the latest webinars from Fluidic Analytics, covering a range of topics from mesauring antibody affinity in serum to Monitoring of SMALP nanodisc formation, to quantifying the stoichiometry and binding affinity of protein–protein interactions in complex backgrounds.
Accurate solution phase affinity profiling of a SARS-CoV-2 antibody in serum
Mesauring antibody affinity in serum - it's not as trival as it sounds

Affinity vs Avidity — What's the difference?
We explore the differences between Affinity vs Avidity and hopefully dispell the vagueness you feel next time you come across them in a paper

Monitoring of SMALP nanodisc formation by microfluidic diffusional sizing
MDS is an ideal tool to monitor SMALP nanodisc formation discover why in this webinar

Quantifying the stoichiometry and binding affinity of protein–protein interactions in complex backgrounds
The Fluidity One-W;is able to provide insights on structural arrangements of individual proteins and protein complexes

Affinity of PD-1/PD-L1 interaction — a comparison between SPR, MST, ITC and MDS
Determinationn of binding affinity and stoichiometry of protein interactions without prior knowledge of the structure
