A synthetic phospho-specific peptide corresponding to residues surrounding Tyr353 of human Ezrin was used as an immunogen. The antibody only detects Ezrin phosphorylated on Tyrosine 353.
Buffer
50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.
Erzin, a member of the Ezrin, Radixin, Moesin (ERM) family, is a linker protein located between cell surface receptors, adhesion molecules, and actin cytoskeleton (1-2). Ezrin activity is regulated by intramolecular interactions between N- and C-terminal ERM association domains (3). Phosphorylation at threonine 567 is a critical regulator of Ezrin function allowing the active protein to link target molecules to the actin cytoskeleton (4). Erzin tyrosine phosphorylation can also be induced by EGF, PDGF and HGF stimulation. Erzin interacts with PI3-K protein kinase A and Rho (5).
Related Pathway
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Western blot analysis on 293 cell lysates using anti-Phospho-Ezrin (pY353), 1:200,000 dilution. Cells were either (A) untreated (B) treated with pervanadate.
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