protein

Moesin Protein, Human (His)

HY-P73806

20 μg

285 USD

Moesin Protein, Human (His)

proteins

E. coli

20 μg

285 USD

Moesin proteins connect the actin cytoskeleton to the plasma membrane and regulate cell cortical structure and function. Moesin Protein, Human (His) is the recombinant human-derived Moesin protein, expressed by E. coli , with N-His labeled tag. The total length of Moesin Protein, Human (His) is 346 a.a., with molecular weight of ~45 kDa.

Human

Moesin, an Ezrin-radixin-moesin (ERM) family protein, serves as a crucial link between the actin cytoskeleton and the plasma membrane, thereby influencing the structure and function of specific domains in the cell cortex. Functioning as a tether for actin filaments, Moesin undergoes oscillation between a resting and an activated state, establishing transient interactions with the actin cytoskeleton. Upon phosphorylation of its C-terminal threonine, Moesin becomes activated, leading to interactions with F-actin and subsequent cytoskeletal rearrangements. These rearrangements play a pivotal role in regulating various cellular processes, including cell shape determination, membrane transport, and signal transduction. Moesin's significance is particularly pronounced in immunity, impacting both T and B-cell homeostasis and self-tolerance, and regulating lymphocyte egress from lymphoid organs. Additionally, Moesin modulates phagolysosomal biogenesis in macrophages and participates in immunologic synapse formation. The protein adopts a closed conformation (inactive form) through a head-to-tail association of its N-terminal and C-terminal halves, rendering it incapable of actin or membrane-binding in this state.

Moesin; Membrane-organizing extension spike protein; MSN

Greater than 80% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 0.5M NaCl, pH 8.0. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.

Room temperature in continental US; may vary elsewhere.