Resources

Publication: Protein tyrosine phosphatase PTPN22 negatively modulates platelet function and thrombus formation

In platelets, engagement of platelet surface receptors glycoprotein VI (GPVI) or GPIb-IX-IV by their respective ligands collagen or von Willebrand factor exposed from the subendothelial matrix at the site of vascular injury triggers the phosphorylation of several proteins, leading to activation and transduction of intraplatelet signaling pathway. In this study, a BioFlux shear flow system was used to examine platelet adhesion and aggregation to fibrillar collagen in mepacrine-labeled whole blood to assess adhesive mechanisms. The investigators used a BioFlux to help determine that PTPN22 inhibition enhanced aggregation, spreading, and clot retraction, revealing a novel role of PTPN22 in platelet function and arterial thrombosis.

Related Resources

Researchers at Columbia University used the CellRaft AIR System to support the development of precisely engineered human embryonic stem cell (hESC) lines for a study...

In this study, CellRaft AIR was used to isolate, verify, and expand monoclonal cell lines carrying engineered SF3B1 mutations, forming the basis of an isogenic...

In this work, CellRaft arrays were used to generate clonally derived cell populations from single cells prior to sequencing, providing a ground-truth reference for benchmarking...