Phospho-Ezrin/Radixin/Moesin (Thr567/Thr564/Thr558)抗体;Phospho-Ezrin/Radixin/Moesin (Thr567/Thr564/Thr558) Antibody—艾普蒂 新品

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     Western blot analysis of Phospho-Ezrin (Thr567)/ Radixin (Thr564)/ Moesin (Thr558) in 3T3, 3T3+PDGF lysates using Phospho-Ezrin/Radixin/Moesin (Thr567/Thr564/Thr558) antibody.    

  
  

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     Western blot analysis of Ezrin (Phospho-Thr567)/ Radixin (Phospho-Thr564)/ Moesin (Phospho-Thr558) in Hela, CHO-K1, C6 lysates using Ezrin (Phospho-Thr567)/ Radixin (Phospho-Thr564)/ Moesin (Phospho-Thr558) antibody.    

  
  

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     Immunohistochemistry analysis of paraffin-embedded Human tonsil using Ezrin (Phospho-Thr567)/ Radixin (Phospho-Thr564)/ Moesin (Phospho-Thr558) antibody. High-pressure and temperature Sodium Citrate pH 6.0 was used for antigen retrieval.    

  
  

Phospho-Ezrin/Radixin/Moesin (pERM) antibodies specifically detect the activated forms of the ERM protein family—Ezrin, Radixin, and Moesin—which link the plasma membrane to the actin cytoskeleton, regulating cell shape, motility, and signaling. These proteins share structural homology, with a conserved C-terminal threonine residue (Ezrin Thr567. Radixin Thr564. Moesin Thr558) whose phosphorylation is critical for their activation. Phosphorylation at these sites induces a conformational shift from a closed, inactive state to an open state, enabling ERM proteins to bind both membrane-associated proteins (e.g., CD44. ICAMs) and actin filaments.

The pERM antibody serves as a key tool for studying ERM activation dynamics in processes like cell polarization, membrane protrusion, and epithelial-mesenchymal transition. It is widely used in techniques such as Western blotting, immunofluorescence, and flow cytometry to assess ERM involvement in pathological conditions, including cancer metastasis, immune cell trafficking, and inflammatory responses. Dysregulated ERM phosphorylation is associated with tumor invasiveness and immune dysfunction, making this antibody valuable for both basic research and translational studies. Its specificity for the phosphorylated state allows researchers to distinguish active ERM proteins from their inactive forms, providing insights into Rho GTPase signaling pathways that regulate cytoskeletal remodeling.