A suggested positive control for this product is HeLa cells.
Ezrin, radixin and moesin (ERM) proteins are widely distributed proteins located in the cellular cortex, in microvilli and adherens junctions. They are mediate linkage of actin cytoskeleton to plasma membrane in many cells. ERM proteins contain an N-terminal FERM (4.1/ezrin/radixin/moesin) domain that binds to phosphatidylinositol-(4,5)phosphate and cellular membrane proteins. The ERM, particularly ezrin, is important for reconstructing cell-surface architecture during T cell activation. Despite the high degree of homology, the three proteins exhibit a distinct receptor-specific pattern of phosphorylation. ERM activity is regulated in part by phosphorylation at a C-terminal threonine (ezrin-Thr567, radixin-Thr564, moesin-Thr558).
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Protein Aliases: ESP10; Radixin; radixin isoform; RDX
Gene Aliases: AA516625; DFNB24; RDX