|Detection of Human, Mouse, and Rat Ezrin by Western Blot. Western blot shows lysates of human placenta tissue, mouse placenta tissue, and C6 rat glioma cell line. PVDF membrane was probed with 0.2 µg/mL of Sheep Anti-Human/Mouse/Rat Ezrin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7239) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Ezrin at approximately 81 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
EZRIN (also Cytovillin, Villin2 and p81) is a founding member of the ERM family, Band 4.1 Superfamily of proteins. Although its predicted MW is 69 kDa, it runs anomalously at 77-82 kDa in SDS-PAGE. ERZIN is expressed by epithelial cells where it serves as a linker between the cell membrane and the actin cytoskeleton. Its presence is particularly strong in microvilli where it helps organize this structure. In addition, ERZIN also organizes microtubules in lymphocytes at or near the immunological synapse by interacting with Glg1. Human EZRIN is 585 amino acids (aa) in length. It contains a band 4.1 homology/FERM domain that binds CD44, ICAM-1, EBP50 and ERM family members (aa 1-295), a central alpha -helical region (aa 296-352), and a C-terminal ERM and actin-binding/FERM C domain (aa 353-586). EZRIN exists as either a monomer, or a homo/heterodimer. EZRIN is not constitutively active, but must be phosphorylated and unfolded to bind to cytoplasmic proteins. Over aa 438-562, human EZRIN shares 96% aa identity with mouse EZRIN.