Ezrin Peptide | EZR peptide

Ezrin (Thr567), Radixin (Thr564), Moesin (Thr558), phosphorylated, Blocking Peptide

Cat. Num. AAA657935

• Gene Names: EZR; CVL; CVIL; VIL2
• Applications: Immunohistochemistry
• Purity: Purified
• Synonyms: Ezrin; Ezrin (Thr567); Radixin (Thr564); Moesin (Thr558); phosphorylated; Blocking Peptide; EZR peptide

• Purity/Purification: Purified

• Applicable Applications for EZR peptide: Immunohistochemistry (IHC)
• Application Notes: Use as a blocking reagent to evaluate the specificity of antibody reactivity in immunohistochemistry protocols.
• Quality Control: The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) Rabbit mAb by immunohistochemistry.
• Preparation and Storage: May be stored at 4 degree C for short-term only. For long-term storage, store at -20 degree C. Aliquots are stable for at least 6 months at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Immunohistochemistry (IHC)

(Immunohistochemical analysis of paraffin-embedded human breast carcinoma using Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (41A3) Rabbit mAb in the presence of control peptide (left) or Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) (41A3) Blocking Peptide (right).)

Related Product Information for EZR peptide

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 their 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).

This peptide is used to block Phospho-Ezrin (Thr567)/Radixin (Thr564)/Moesin (Thr558) Rabbit mAb reactivity.

Product Categories/Family for EZR peptide

Molecular Biology; MB-Peptides

NCBI and Uniprot Product Information

• NCBI GI #: 21614499
• NCBI GeneID: 7430
• NCBI Accession #: NP_003370.2
• NCBI GenBank Nucleotide #: NM_003379.4
• UniProt Accession #: P15311; P23714; Q4VX75; Q96CU8; Q9NSJ4; E1P5A8
• Molecular Weight: 69,413 Da
• NCBI Official Full Name: ezrin
• NCBI Official Synonym Full Names: ezrin
• NCBI Official Symbol: EZR
• NCBI Official Synonym Symbols: CVL; CVIL; VIL2
• NCBI Protein Information: ezrin; p81; villin-2; cytovillin 2; villin 2 (ezrin)
• UniProt Protein Name: Ezrin
• Protein Family: Ezrin
• UniProt Gene Name: EZR
• UniProt Synonym Gene Names: VIL2
• UniProt Entry Name: EZRI_HUMAN

NCBI Description

The cytoplasmic peripheral membrane protein encoded by this gene functions as a protein-tyrosine kinase substrate in microvilli. As a member of the ERM protein family, this protein serves as an intermediate between the plasma membrane and the actin cytoskeleton. This protein plays a key role in cell surface structure adhesion, migration and organization, and it has been implicated in various human cancers. A pseudogene located on chromosome 3 has been identified for this gene. Alternatively spliced variants have also been described for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

Function: Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. Ref.17 Ref.19 Ref.20

Enzyme regulation: A head-to-tail association, of the N-terminal and C-terminal halves results in a closed conformation (inactive form) which is incapable of actin or membrane-binding

By similarity.

Subunit structure: Interacts with MPP5 and SLC9A3R2. Found in a complex with EZR, PODXL and SLC9A3R2

By similarity. Interacts with MCC, PLEKHG6, PODXL, SCYL3/PACE1, SLC9A3R1 and TMEM8B. Interacts (when phosphorylated) with FES/FPS. Interacts with dimeric S100P, the interaction may be activating through unmasking of F-actin binding sites. Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21

Subcellular location: Apical cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection. Cell projection › microvillus membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cell cortex. Cytoplasm › cytoskeleton. Note: Localization to the apical membrane of parietal cells depends on the interaction with MPP5. Localizes to cell extensions and peripheral processes of astrocytes

By similarity. Microvillar peripheral membrane protein (cytoplasmic side). Ref.18

Tissue specificity: Expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. Weakly expressed in brain stem and diencephalon. Stronger expression was detected in gray matter of frontal lobe compared to white matter (at protein level). Component of the microvilli of intestinal epithelial cells. Preferentially expressed in astrocytes of hippocampus, frontal cortex, thalamus, parahippocampal cortex, amygdala, insula, and corpus callosum. Not detected in neurons in most tissues studied. Ref.15

Developmental stage: Very strong staining is detected in the Purkinje cell layer and in part of the molecular layer of the infant brain compared to adult brain. Ref.15

Post-translational modification: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding

By similarity. Ref.9 Ref.10 Ref.18 Ref.19

Sequence similarities: Contains 1 FERM domain.

Sequence caution: The sequence AAA61278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.The sequence CAB82418.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.