特异性
Ezrin/Radixin/Moesin (Phospho Thr567/Thr564/Thr558) Antibody detects endogenous levels of Moesin/Ezrin/Radixin protein only when phosphorylated at Thr567/Thr564/Thr558.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):YKtLR
组成
PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA
来源
Monoclonal, Rabbit,IgG
稀释比例
IHC 1:200-1:1000; WB 1:1000-1:5000; IF 1:200-1:1000; ELISA 1:5000-1:20000; IP 1:50-1:200; Note: For IHC, we suggest antigen retrieval with TE buffer pH 9.0
储存
-15°C to -25°C/1 year(Do not lower than -25°C)
其他名称
MSN ; Moesin ; Membrane-organizing extension spike protein ; RDX ; Radixin ; EZR ; VIL2 ; Ezrin ; Cytovillin ; Villin-2 ; p81
背景
Moesin (for membrane-organizing extension spike protein) is a member of the ERM family which includes ezrin and radixin. ERM proteins appear to function as cross-linkers between plasma membranes and actin-based cytoskeletons. Moesin is localized to filopodia and other membranous protrusions that are important for cell-cell recognition and signaling and for cell movement. [provided by RefSeq, Jul 2008],
功能
Probably involved in connections of major cytoskeletal structures to the plasma membrane.,PTM:Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures.,similarity:Contains 1 FERM domain.,subcellular location:Phosphorylated form is enriched in microvilli-like structures at apical membrane.,subunit:In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation (By similarity). Binds SLC9A3R1.,tissue specificity:In all tissues and cultured cells studied.,
