Recombinant Human Moesin protein
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Recombinant Human Moesin protein is a Human Fragment protein, in the 410 to 577 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
Moesin, Membrane-organizing extension spike protein, MSN
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Moesin protein (AB64309)
ab64309 on SDS-PAGE, MW 50kDa.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
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.
Pathways
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.
Specifications
Form
Liquid
General info
Function
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).
Post-translational modifications
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.
Subcellular localisation
Cytoskeleton
Target data
Product promise
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