Recombinant Human Moesin protein is a Human Fragment protein, in the 410 to 577 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation (PubMed:27405666).
Moesin, Membrane-organizing extension spike protein, MSN
Recombinant Human Moesin protein is a Human Fragment protein, in the 410 to 577 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE.
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.79% Tris HCl, 0.29% Sodium chloride, 0.00385% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.00174% PMSF
Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton (PubMed:10212266). Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement (PubMed:10212266). These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction (PubMed:12387735, PubMed:15039356). The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs (PubMed:9298994, PubMed:9616160). Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation (PubMed:27405666).
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.
Moesin also known as MSN or moesin protein is part of the ERM (ezrin radixin moesin) family which links the actin cytoskeleton to the plasma membrane. It weighs around 68 kDa. This protein is widely expressed in various tissues notably in endothelial cells and other cells with high cytoskeletal dynamics. Moesin plays an essential role in maintaining cell shape polarity and enabling cellular processes like migration and adhesion.
This protein serves as a crosslinker between the plasma membrane and the actin cytoskeleton influencing signal transduction pathways. Moesin participates significantly in cellular processes like cytokinesis and microvilli formation by binding actin filaments. It is part of several functional complexes ensuring proper cytoskeletal organization and cellular dynamics. Moesin's interactions with other proteins like Rho GTPases regulate its functions aiding cellular morphology and polarity.
Moesin is actively involved in the RhoA-ROCK pathway. This pathway is fundamental to actin cytoskeletal reorganization and cell contraction. Moesin interacts with proteins such as radixin and ezrin ensuring cohesion in cytoskeletal rearrangements. Through these interactions Moesin contributes to cell motility and various signaling cascades necessary for cellular responses.
Moesin is associated with conditions such as cancer and immune system disorders. Aberrant expression of moesin can contribute to enhanced cellular migration and invasion which are mechanisms seen in cancer metastasis. Moesin's interaction with proteins like ezrin in cancer progression has been documented. Also in immune disorders altered moesin activity can affect leukocyte transmigration disrupting efficient immune responses.
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ab64309 on SDS-PAGE, MW 50kDa.
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