Moesin (MSN), a cytoskeletal protein belonging to the ezrin-radixin-moesin (ERM) family, plays a critical role in linking the cell membrane to the actin cytoskeleton, regulating cell shape, adhesion, and motility. It is encoded by the MSN gene and is highly expressed in endothelial, epithelial, and immune cells. Moesin facilitates cellular processes such as membrane ruffling, signal transduction, and immune cell activation by interacting with transmembrane proteins and cytoskeletal components. Dysregulation of moesin has been implicated in various pathologies, including cancer metastasis, viral infections (e.g., HIV), and autoimmune disorders, due to its role in cell migration and inflammatory responses.
MSN antibodies are essential tools for studying these mechanisms. They are widely used in techniques like Western blotting, immunohistochemistry, and flow cytometry to detect moesin expression, localization, and post-translational modifications (e.g., phosphorylation at Thr558. which activates moesin). Researchers utilize these antibodies to explore moesin's involvement in tumor invasiveness, immune cell trafficking, and endothelial barrier integrity. Additionally, MSN antibodies have diagnostic potential, as altered moesin levels correlate with disease progression in cancers and inflammatory conditions. Recent studies also highlight their utility in elucidating moesin's interaction with pathogens, aiding therapeutic development. Overall, MSN antibodies are pivotal in advancing understanding of cellular dynamics and disease pathways linked to ERM protein function.