Moesin (for membrane-organizing extension spike protein) is a member of the ERM protein family which includes ezrin and radixin. The ERM proteins have a crucial role in organizing membrane domains through their ability to interact with transmembrane proteins and the cytoskeleton. The C-terminal domain may form an intramolecular band to the N-terminal four-point-one ERM homology domain or may bind to F-actin depending on the phosphorylation state of a conserved threonine residue (Thr567 in ezrin, Thr564 in radixin, and Thr558 in moesin). An essential role of the 78kD protein Moesin is described for Rho- and Rac-dependent assembly of actin filaments.
Source:
Recombinant corresponding to aa1-577 from human Moesin, fused to N-His tag expressed in E.coli.
Molecular Weight:
~70kD
Storage and Stability:
Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.