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Protein Interaction Analyzer for Membrane Proteins Industry-Medical / Health Care - Pharmaceuticals
Fluidity One-M by Fluidic Sciences Ltd. provides an innovative approach to studying membrane proteins without the need for traditional purification processes. This advanced instrument allows for analysis in-solution using single-use microfluidic channels, minimizing the risk of damaging delicate protein structures. It facilitates a more accurate study of protein conformation changes, ligand binding, and protein interactions in their native membrane environment. The instrument's smart assistant, Fluidity Insight, utilizes advanced machine learning for experiment guidance, enhancing your workflow's precision and efficiency. The system supports the measurement of protein expression levels and binding affinities directly within native lipid-bilayer environments. It also eliminates the use of detergents, preventing potential artifacts and preserving the protein's structural integrity. This purification-free method aids in producing significant insights into protein behavior, proving invaluable for drug development targeting membrane proteins.
Challenges in studying membrane proteins
Up to a third of all human genes encode membrane proteins — showing both their variety and significance. Mutations in membrane proteins cause many common human diseases like heart disease, neurological diseases, cancer, and cystic fibrosis, making them an extremely important target for drug development. In fact, over 50% of current small molecule drugs target membrane proteins.
Despite their prevalence and importance, less than 1% of high-resolution protein structures are membrane proteins. Expression, purification and stabilization of membrane proteins is time consuming and difficult, and even if achieved, the immobilization required for many interaction analysis technologies risks damaging the precious protein. This wide array of challenges therefore begs the question of whether it could be possible to study membrane protein structural stability, folding, oligomerization, binding and function all without purification?
A new type of quantitative serum-antibody profiling
When studying the immune response to a drug, a vaccine, or an antigen, established serological technologies, such as ELISA, only provide semi-quantitative outputs such as titer. This can determine the presence of antibodies in blood but lacks the ability to discriminate between a low concentration of strong-binding antibodies and a high concentration of weak-binding antibodies. With multi-step workflows classical serological assays are slow and difficult to develop for new antigens, and the titers obtained cannot be compared between laboratories.
We developed our Seroaffinity and Concentration (SAffCon) assay to overcome these challenges.
By directly measuring antibody affinity and concentration in clinical samples, without the need for purification, immobilization, and external calibrants, we provide universally comparable absolute results to enable accurate correlation of antibody properties with immunogenicity and clinical outcome.