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). Erzin tyrosine phosphorylation can also be induced by EGF, PDGF and HGF stimulation. Erzin interacts with PI3-K protein kinase A and Rho (4). In response to epidermal growth factor (EGF) the microvillar core protein ezrin is phosphorylated transiently to a high level on tyrosine residues in human epidermoid carcinoma A431 cells. Tyr145, lies in the N-terminal region of homology that is common to the band 4.1-talin-ezrin protein family. This tyrosine residue and its vicinal amino acids are conserved throughout the family members, including radixin, moesin, and the two phosphotyrosine phosphatases, PTP H1 and PTP MEG, but not in band 4.1 or talin (5).
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