Resources

Publications, application notes and more

  • Application note16 October 2019

    Quantifying the stoichiometry of protein–protein interactions

    Here the Fluidity One-W is used to experimentally determine the conformation of Protein A and is able to infer its stoichiometry when binding to IgG antibodies.

  • Blog10 October 2019

    Drug Target Review webinar: Q&A session

    Don't worry if you missed our recent webinar with Drug Target Review, we have transcribed the Q&A session with speaker Dr Sean Devenish in this blog.

  • Blog09 October 2019

    Q&A session from BSI 2019

    Fluidic Analytics is proud to be a part of the first French congress of Structural Integrative Biology (BSI-2019), hosted at Paul Sabatier University in Toulouse. In this blog we have transcribed the Q&A part of the presentation that we gave on 8th October.

  • Application note11 September 2019

    Measuring the binding affinity of protein–protein interactions in simple and complex backgrounds

    Here the Fluidity One-W is used to experimentally determine the KD of protein-antibody interactions in both buffer and cell culture medium with high precision.

  • Posters10 September 2019

    Fluidity One-W protein interactions poster

    Poster summarising the work done by our internal applications team using MDS on protein interactions with proteins, lipids and antibodies as well as other published work using MDS to analyse protein interactions.

  • Video10 September 2019

    How does the Fluidity One-W work?

    The Fluidity One-W uses microfluidic diffusional sizing (MDS) technology to determine the binding affinity between proteins and their binding partners; whether they are aptamers, lipids, DNA, small molecules or other proteins. Watch the video to understand how the Fluidity One-W works.

  • Blog23 August 2019

    Looking at the numbers: Why protein stoichiometry matters

    Accurate determination of stoichiometry for a protein complex is critical to our understanding how the complex will react to other proteins or small molecules. Here we look at how stoichiometry not only effects important viral protein-antibody interactions but also disease pathology.

  • Documentation31 July 2019

    Protein labelling procedure using Alexa Fluor 488 NHS ester

    Long form protein labelling protocol using Alexa Fluor 488 NHS Ester from Thermo Fisher Scientific. Includes troubleshooting, purification steps and an example calculation to help with concentration and volume calculations.

  • Documentation30 July 2019

    Quick Guide: Labelling with Alexa Fluor 488 NHS Ester

    Quick guide to label and purify proteins with Alexa Fluor 488 NHS ester for use with the Fluidity One-W.

  • Publication25 July 2019

    Microfluidic diffusional sizing (MDS) in the literature

    Document referencing all the publications where microfluidic diffusional sizing (MDS) has been used.

  • Publication24 July 2019

    Putative interaction site for membrane phospholipids controls activation of TRPA1 channel at physiological membrane potentials.

    Macikova et al use Microfluidic Diffusional Sizing (MDS) along with other techniques to understand the role phosphatidylinositol-4,5-bisphosphate (PIP2) has in the regulation of transient receptor potential ankyrin 1 (TRPA1) channel. The Fluidity One was used to create binding curves of the interactions between two specific peptides (L992-N1008 and T1003-P1034) and model lipid membranes in the presence of PIP2.

  • Brochure27 June 2019

    Fluidity One-W Brochure

    This brochure gives an overview of the capabilities, applications and full technical specifications of the Fluidity One-W

  • Application note03 April 2019

    Determination of KD of aptamer protein interactions by microfluidic diffusional sizing

    Here the Fluidity One-W is used to experimentally determine the KD of two protein aptamer interactions, with results in good agreement with literature values. Importantly the technique required no calibration, complex setup or specialist sample preparation. Furthermore, the interaction is assessed without immobilising or altering either molecule beyond the addition of a standard fluorescent label.