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Human MSN ELISA Kit for Sandwich ELISA - ABIN418327
Ciregia, Giusti, Molinaro, Niccolai, Agretti, Rago, Di Coscio, Vitti, Basolo, Iacconi, Tonacchera, Lucacchini: Presence in the pre-surgical fine-needle aspiration of potential thyroid biomarkers previously identified in the post-surgical one. in PLoS ONE 2013
Show all 5 Pubmed References
Data show that Moesin upregulation influences extra-centrosome behavior and robust bipolar spindle formation.
Btsz and Moesin guide luminal membrane morphogenesis through organizing actin.
The conserved C-terminal coiled-coil domain of Slik, which is necessary and sufficient for apical localization of the kinase in epithelial cells, is not required for Moesin phosphorylation but is critical for the growth-promoting function of Slik.
Early endocytosis maintains normal steady-state levels of Crumbs, which recruits apical phosphorylated (active) Moesin, which in turn regulates seamless tube shape through modulation of cortical actin filaments.
Moesin interacts with an unusual RhoGAP (show ARHGAP1 ELISA Kits), Conundrum (Conu), and recruits it to the cell cortex to negatively regulate RhoA (show RHOA ELISA Kits) activity.
Moesin stabilizes microtubules via a direct interaction at the cell cortex.
Wgn-Moe signaling cascade plays a key role in photoreceptor target field innervations through cell autonomous and non-cell autonomous mechanisms.
Drosophila melanogaster protein phosphatase type 1 beta (flapwing) co-regulates dephosphorylation and altered activity of both Merlin (show NF2 ELISA Kits) and Moesin.
This study revealed a novel mechanism for controlling salivary gland lumen size, namely through Rho1-dependent actin (show ACTB ELISA Kits) polymerization and distribution and downregulation of apical phosphorylated moesin.
the Pp1 (show PPYR1 ELISA Kits)-87B phosphatase restricts high Moesin activity to early mitosis and down-regulates Moesin at the polar cortex, after anaphase onset.
suggest that Ve-cadherin (show CDH5 ELISA Kits) and Moesin1 function to establish and maintain apical/basal polarity during multicellular lumen formation in the intersegmental vessels
results suggest a new role for moesin, acting in a signalling pathway facilitating the differentiation of extraembryonic endoderm
The Ano1 (show ANO1 ELISA Kits)-moesin interaction limits Ano1 (show ANO1 ELISA Kits) lateral membrane mobility and contributes to microvilli scaffolding, therefore stabilizing larger membrane structures. Collectively, these results reveal a newly identified role for Ano1 (show ANO1 ELISA Kits) in shaping the plasma membrane during oogenesis, with broad implications for the regulation of microvilli in epithelia.
These results indicate that loss of miR (show MLXIP ELISA Kits)-200c, as a consequence of p53 (show TP53 ELISA Kits) mutation, can upregulate Moesin oncogene (show RAB1A ELISA Kits) and thus promote carcinogenesis in breast cancer
the administration of 10(-6) M retinoic acid (10-20 min) induces the activation of the migration-related proteins Moesin, FAK (show PTK2 ELISA Kits), and Paxillin (show PXN ELISA Kits) in T-47D breast cancer cells.
Up-regulation of moesin expression in glioblastoma cells correlated with increases in cell proliferation, invasion and migration, suggesting moesin's role in glioblastoma progression.
this study identifies X-linked primary immunodeficiency associated with hemizygous mutations in the moesin gene
These results of this study may pave the way for exploiting moesin as a novel target for intervention in muscular dystrophy.
The present study showed over-expression of ezrin (show EZR ELISA Kits) and moesin in colorectal carcinoma
These results indicate that the Thr (show TRH ELISA Kits) 558 phosphorylation in moesin mediates endothelial angiogenesis. Advanced glycation end products promoted human umbilical vein endothelial cell angiogenesis by inducing moesin phosphorylation via RhoA (show RHOA ELISA Kits)/ROCK pathway.
Phospho-Ezrin/Radixin/Moesin (ERM) inhibit cell adhesion, and therefore, dephosphorylation of ERM proteins is essential for cell adhesion.Phospho-ERM induce formation and/or maintenance of spherical cell shape.
Moesin was required in HMGB1-induced F-actin rearrangement, hyperpermeability, and inflammatory responses. HMGB1 increased Thr558 phosphorylation of moesin. Moesin was elevated in sepsis.
results indicate Moesin may regulate cell motility through its interactions with MT1-MMP (show MMP14 ELISA Kits) and E-cadherin (show CDH1 ELISA Kits)/p120-catenin (show CTNND1 ELISA Kits) adhesion complex and cytoplasmic expression of Moesin correlates with nodal metastasis and poor prognosis of OSCCs
Moesin is an important regulator of the surface abundance and stability of TbetaRII and is important in facilitating the efficient generation of iTregs.
The expression of moesin was upregulated in cardiomyocytes under inflammation, inducing protrusion formation in a phosphorylation-dependent fashion.
this study shows that low neutrophil rolling in inflamed venules was impaired in moesin-deficient mice
High blood moesin levels were also observed in cecal ligation and puncture (CLP)-induced sepsis in mice. Administration of blocking moesin antibodies attenuated CLP-induced septic death.
An increase in moesin expression may contribute to the increased expression of P-gp (show ABCB4 ELISA Kits) in blood brain barrier endothelial cells, leading to the development of morphine analgesic tolerance.
phosphorylation-regulated (show PHAX ELISA Kits) interaction between the cytoplasmic tail of cell polarity protein crumbs and the actin-binding protein (show PFN1 ELISA Kits) moesin
both moesin-mediated inhibition and its localized deactivation by myosin phosphatase are essential for neutrophil polarization and effective neutrophil tracking of pathogens.
A novel role for moesin in regulating clathrin-dependent S1PR1 internalization through clathrin-coated vesicles formation.
Moesin may be a potential drug target for inhibiting corneal fibrosis, and the details of moesin-related signaling pathways would be critical for understanding corneal fibrosis.
Moesin (for membrane-organizing extension spike protein) is a member of the ERM family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons. Moesin is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement.
, membrane-organizing extension spike protein