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.

  • Video15 October 2019

    We are Fluidic

    Fluidic Analytics is made up of a wide range of experts who have come from different scientific backgrounds. Here, we take a look at some of our ever-growing team.

  • Video15 October 2019

    Drug Target Review webinar

    Missed out on our recent Drug Target Review webinar? Don't worry you can watch it here anytime.

  • 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.

  • Blog03 October 2019

    Cancer drugs might not work the way we think they do

    The majority of proposed anticancer treatments do not succeed in advancing to clinical use because of problems with efficacy or toxicity, often for unclear reasons. Lin et al. discovered that a drug candidate in clinical development was effective at killing cancer cells even when its target protein was knocked out, suggesting that its proposed mechanism of action was incorrect

  • 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.

  • Blog06 September 2019

    The role of chaperones

    In this article, we look at what chaperones are, what role they play in the body and how MDS is being utilized to study them.

  • 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.

  • Blog14 August 2019

    Getting to the heart of the matter: GPCRs as therapeutic targets for heart failure

    In this blog post we cover the functions of key GPCRs in the heart and how they are now being targeted for therapeutic treatments to reduce the impact of coronary heart disease

  • Video13 August 2019

    Conference Poster Presentations 2019

    Throughout 2019 we will be attending conferences all over the world and seeking out research topics and poster presetations we really think are worth taking a look at. Check back here regularly for videos of poster presentations that present cutting edge science from around the globe.

  • Video12 August 2019

    Measuring IL2 Stability in different buffers using Microfluidic Diffusional Sizing (MDS)

    In this video we look at how a commercially available human interleukin-2 is assessed by microfluidic diffusional sizing on the Fluidity One across a dilution series. The hydrodynamic radius is observed to increase with increasing concentration, in a way which suggests a monomer-trimer equilibrium with positive cooperativity is established.

  • Publication01 August 2019

    Analysis of αB-crystallin polydispersity in solution through native microfluidic electrophoresis

    In this paper, the authors utilise microfluidic diffusional sizing and electrophoresis to characterise the oligomeric states of the chaperone protein alphaB-crystallin.

  • 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.

  • Publication29 July 2019

    On-chip label-free protein analysis with downstream electrodes for direct removal of electrolysis products

    Saar et al designed and demonstrated a single step lithography approach to fabricate microfluidic devices that can be used to apply high electric fields without the formation of any electrolysis products in the electrophoresis area.

  • Video25 July 2019

    KD video series

    Here is our series of videos that explain what te dissociation constant, KD, is and how to derrive it on a binding curve.

  • Publication25 July 2019

    Gradient-free determination of isoelectric points of proteins on chip

    Lapinska et al. using a microfluidic system built in house design a new technique to determine a protein's isoelectric point (pI) based on microfluidic free-flow electrophoresis (μFFE). The approach exploits temporal rather than spatial pH gradients. To demonstrate the effectiveness of this method the pI of 7 different proteins of known pI were tested; β-lactoglobulin, ribonuclease A, ovalbumin, human transferrin, ubiquitin and myoglobin. The paper shows that this method is successful in determining the pI using this new technique without the requirement of generating and maintaining pH gradients which is often challenging for other techniques. The technique requires low voltages and low sample consumption. The paper also shows that using this technique it is possible to estimate the pI values for a wide range of proteins measuring at only two pH values, suggesting that this technique is rapid and accurate on small volume samples.