Moesin Proteins, Antibodies, cDNA Clones Research Reagents

MSN (Moesin, also known as HEL70; IMD50), located on Xq12, is conserved in Rhesus monkey, dog, cow, mouse, rat, fruit fly, mosquito, C.elegans, and frog. The gene produces a 67820 Da protein composed of 577 amino acids. Moesin (for membrane-organizing extension spike protein) is a member of the ERM family which includes ezrin and radixin. Diseases such as Immunodeficiency 50 and Verrucous Carcinoma are associated with MSN. The related pathways of MSN include Blood-Brain Barrier and Immune Cell Transmigration: VCAM-1/CD106 Signaling and Actin Nucleation by ARP-WASP Complex.

Moesin Protein (1)

    Moesin Antibody (2)

      Moesin cDNA Clone (28)


      クローニングベクター cDNA 製品

      In lentiviral vector


      クローニングベクター cDNA 製品

      In lentiviral vector

      Moesin qPCR Primer (1)

      Moesin の背景知識

      Moesin is a member of the ERM family which includes ezrin and radixin. ERM proteins, highly related members of the larger protein 4.1 superfamily, can exist in an active or inactive conformation. It seems that ERM proteins function as cross-linkers between plasma membranes and actin-based cytoskeletons. The sole Drosophila ERM protein, moesin, functions to promote cortical actin assembly and apical-basal polarity. As a result, cells lacking moesin lose epithelial characteristics and adopt invasive migratory behavior. It is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and cell movement. Moesin contains 1 FERM domain and is expressed in all tissues and cultured cells studied. Moesin has been shown to interact with CD43, Neutrophil cytosolic factor 1, VCAM-1, Neutrophil cytosolic factor 4, ICAM3, and EZR.

      Moesin の参考文献

      • Lankes WT, et al. (1991) Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Proc Natl Acad Sci. 88(19):8297-301.
      • Serrador, J M, et al. (1998) CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. Blood. 91(12):4632-44.
      • Barreiro Olga, et al. (2002) Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes. J Cell Biol. 157(7):1233-45.

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