Lane 1: Raji
Lane 2: SH-SY-5Y
Recombinant Rabbit monoclonal primary
Recombinant Moesin Monoclonal Antibody (ET1610-65)
Raji cell lysate, SH-SY5Y cell lysate, Hela, NCCIT, human tonsil tissue, human spleen tissue, human breast carcinoma tissue, mouse lung tissue, mouse placenta tissue, mouse stomach tissue.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A affinity purified.
Epididymis luminal protein 70 antibody; HEL70 antibody; Membrane organizing extension spike protein antibody; Membrane-organizing extension spike protein antibody; MOES_HUMAN antibody; Moesin antibody; Moesin/anaplastic lymphoma kinase fusion protein antibody; Msn antibody; MSN/ALK fusion antibody
In all tissues and cultured cells studied.
Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity). Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization.; S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.
Cell membrane, Apical cell membrane, microvillus membrane, cytoskeleton, microvillus.
Ezrin, Moesin and Radixin belong to a family of highly homologous Actin-associated proteins that are localized just beneath the plasma membrane. These proteins are believed to be involved in the mediation of interactions between cytoskeletal and membrane proteins. Ezrin serves as a major cytoplasmic substrate of various protein-tyrosine kinases, including the epidermal growth factor receptor. Ezrin has also been identified as a cAMP-dependent protein kinase (A-kinase) anchoring protein and designated AKAP78. Moesin and Radixin share more than 70% homology with Ezrin and are co-expressed within various cell types. Despite the high degree of homology, the three proteins exhibit a distinct receptor-specific pattern of phosphorylation.