Anti-Moesin, clone SPM562

Prediluted in 1X PBS with 0.1 mg/ml BSA (US sourced) and 0.05% sodium azide, *For IHC use only*. Recognizes 78kDa moesin protein. Moesin, a member of the Talin-4.1 superfamily, is a linking protein of the submembraneous actin cytoskeleton. It is expressed in variable amounts in cells of different phenotypes such as macrophages, lymphocytes, fibroblastic, endothelial, epithelial, and neuronal cell lines but not in blood cells. The ERM proteins, ezrin, radixin, and moesin are involved in a variety of cellular functions, such as cell adhesion, migration, and the organization of cell surface structures, and are highly homologous, both in protein sequence and in functional activity, with merlin/schwannomin, a neurofibromatosis-2-associated tumor-suppressor protein. Cell lines of epithelial and mesothelial origin contain both moesin and radixin whereas cells of endothelial and lymphoid origin express moesin. Protein function: Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages. Participates also in immunologic synapse formation (PubMed:27405666). [The UniProt Consortium]