Product Pathways - Cytoskeletal Signaling
Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (48G2) Rabbit mAb (ELISA Specific) #3726
|E-P||H (M) (R) (B)||Endogenous||Rabbit IgG|
Reactivity Key: H=Human M=Mouse R=Rat B=Bovine
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (41A3) Rabbit mAb (ELISA Specific) is phospho-specific by Peptide-ELISA and exhibits a large signal to noise window. The antibody does not recognize the non-phosphorylated peptide in peptide based ELISA (see figure below).
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr567 of human ezrin protein.
The ezrin, radixin, and moesin (ERM) proteins function as linkers between the plasma membrane and the actin cytoskeleton and are involved in cell adhesion, membrane ruffling, and microvilli formation (1). ERM proteins undergo intra or intermolecular interaction between their amino- and carboxy-terminal domains, existing as inactive cytosolic monomers or dimers (2). Phosphorylation at a carboxy-terminal threonine residue (Thr567 of ezrin, Thr564 of radixin, Thr558 of moesin) disrupts the amino- and carboxy-terminal association and may play a key role in regulating ERM protein conformation and function (3,4). Phosphorylation at Thr567 of ezrin is required for cytoskeletal rearrangements and oncogene-induced transformation (5). Ezrin is also phosphorylated at tyrosine residues upon growth factor stimulation. Phosphorylation of Tyr353 of ezrin transmits a survival signal during epithelial differentiation (6).
- Tsukita, S. and Yonemura, S. (1999) J. Biol. Chem. 274, 34507-34510.
- Mangeat, P. et al. (1999) Trends Cell Biol. 9, 187-192.
- Matsui, T. et al. (1998) J. Cell Biol. 140, 647-657.
- Gautreau, A. et al. (2000) J. Cell Biol. 150, 193-203.
- Tran Quang, C. et al. (2000) EMBO J. 19, 4565-4576.
- Gautreau, A. et al. (1999) Proc. Natl. Acad. Sci. USA 96, 7300-7305.
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