Cytoskeletal Signaling
Phospho-Ezrin (Thr567)/Radixin (Thr564)/ Moesin (Thr558) Blocking Peptide
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| CSTコード |
包装 |
希望納入価格 (円) |
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| #1047S | 100 μg | 16,000 | |
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Ezrin, Radixin, Moesin抗体製品一覧
| 使用目的 | |
| Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (41A3) Rabbit mAb （#3149）の反応をブロックし、抗体の反応特異性を確認するために使用 |
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (41A3) Rabbit mAb #3149 in the presence of control peptide (left) or Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (41A3) Blocking Peptide (right).
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).
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Tsukita, S. and Yonemura, S. (1999) J. Biol. Chem. 274, 34507-34510.
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Mangeat, P. et al. (1999) Trends Cell Biol. 9, 187-192.
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Matsui, T. et al. (1998) J. Cell Biol. 140, 647-657.
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Gautreau, A. et al. (2000) J. Cell Biol. 150, 193-203.
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Tran Quang, C. et al. (2000) EMBO J. 19, 4565-4576.
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Gautreau, A. et al. (1999) Proc. Natl. Acad. Sci. USA 96, 7300-7305.
