Product: Moesin/Ezrin/Radixin Mouse Monoclonal Antibody
Catalog: BF8446
Description: Mouse monoclonal antibody to Moesin/Ezrin/Radixin
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 70kDa; 69kD,68kD(Calculated).
Uniprot: P15311 | P26038 | P35241

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Product Info

Source:
Mouse
Application:
WB 1:500-1:3000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Monoclonal [AFfirm8446]
Conjugate:
Unconjugated.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

Villin 2 ezrin; CVIL; CVL; Cytovillin 2; Cytovillin; DKFZp762H157; Epididymis secretory protein Li 105; EZR; EZRI_HUMAN; Ezrin; FLJ26216; HEL S 105; MGC1584; p81; VIL 2; VIL2; Villin 2 (ezrin); Villin 2; Villin-2; Villin2; Epididymis luminal protein 70; HEL70; Membrane organizing extension spike protein; Membrane-organizing extension spike protein; MOES_HUMAN; Moesin; Moesin/anaplastic lymphoma kinase fusion protein; Msn; MSN/ALK fusion; CB567; CG12537; DFNB24; ESP10; Hh-induced MATH and BTB domain-containing protein; HIB; Moesin-B; Protein roadkill; RADI_HUMAN; Radixin; RDX;

Immunogens

Immunogen:

A synthesized peptide derived from human Moesin/Ezrin/Radixin.

Uniprot:
Gene(ID):
Expression:
P15311 EZRI_HUMAN:

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.

P26038 MOES_HUMAN:

In all tissues and cultured cells studied.

Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL

MPKTISVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWFFGLQYQDTKGFSTWLKLNKKVTAQDVRKESPLLFKFRAKFYPEDVSEELIQDITQRLFFLQVKEGILNDDIYCPPETAVLLASYAVQSKYGDFNKEVHKSGYLAGDKLLPQRVLEQHKLNKDQWEERIQVWHEEHRGMLREDAVLEYLKIAQDLEMYGVNYFSIKNKKGSELWLGVDALGLNIYEQNDRLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQMERAMLENEKKKREMAEKEKEKIEREKEELMERLKQIEEQTKKAQQELEEQTRRALELEQERKRAQSEAEKLAKERQEAEEAKEALLQASRDQKKTQEQLALEMAELTARISQLEMARQKKESEAVEWQQKAQMVQEDLEKTRAELKTAMSTPHVAEPAENEQDEQDENGAEASADLRADAMAKDRSEEERTTEAEKNERVQKHLKALTSELANARDESKKTANDMIHAENMRLGRDKYKTLRQIRQGNTKQRIDEFESM

MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTVGLREVWFFGLQYVDSKGYSTWLKLNKKVTQQDVKKENPLQFKFRAKFFPEDVSEELIQEITQRLFFLQVKEAILNDEIYCPPETAVLLASYAVQAKYGDYNKEIHKPGYLANDRLLPQRVLEQHKLTKEQWEERIQNWHEEHRGMLREDSMMEYLKIAQDLEMYGVNYFEIKNKKGTELWLGVDALGLNIYEHDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILALCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERAQLENEKKKREIAEKEKERIEREKEELMERLKQIEEQTIKAQKELEEQTRKALELDQERKRAKEEAERLEKERRAAEEAKSAIAKQAADQMKNQEQLAAELAEFTAKIALLEEAKKKKEEEATEWQHKAFAAQEDLEKTKEELKTVMSAPPPPPPPPVIPPTENEHDEHDENNAEASAELSNEGVMNHRSEEERVTETQKNERVKKQLQALSSELAQARDETKKTQNDVLHAENVKAGRDKYKTLRQIRQGNTKQRIDEFEAM

PTMs - P15311/P26038/P35241 As Substrate

Site PTM Type Enzyme
K3 Ubiquitination
K35 Acetylation
K35 Ubiquitination
T57 Phosphorylation
K60 Acetylation
K64 Ubiquitination
S66 Phosphorylation P17612 (PRKACA)
K72 Ubiquitination
K79 Acetylation
K79 Ubiquitination
K83 Ubiquitination
K107 Ubiquitination
S112 Phosphorylation
Y116 Phosphorylation
Y137 Phosphorylation
K139 Acetylation
K139 Ubiquitination
K143 Ubiquitination
S144 Phosphorylation
Y146 Phosphorylation P00533 (EGFR) , P16591 (FER) , P12931 (SRC) , P06239 (LCK)
S149 Phosphorylation
K162 Ubiquitination
R171 Methylation
K184 Acetylation
K184 Ubiquitination
Y191 Phosphorylation
Y201 Phosphorylation
Y205 Phosphorylation
K209 Ubiquitination
K211 Ubiquitination
K230 Sumoylation
K230 Ubiquitination
K233 Sumoylation
K233 Ubiquitination
T235 Phosphorylation Q00535 (CDK5)
K237 Ubiquitination
S243 Phosphorylation
S249 Phosphorylation
K253 Acetylation
K253 Ubiquitination
K254 Ubiquitination
K258 Acetylation
K258 Ubiquitination
K262 Acetylation
K262 Sumoylation
K262 Ubiquitination
K263 Acetylation
K263 Ubiquitination
Y270 Phosphorylation
R273 Methylation
Y291 Phosphorylation
K296 Ubiquitination
T299 Phosphorylation
K306 Methylation
K306 Ubiquitination
T332 Phosphorylation
K337 Ubiquitination
K344 Ubiquitination
Y354 Phosphorylation P16591 (FER) , P00533 (EGFR)
K357 Sumoylation
K357 Ubiquitination
S366 Phosphorylation
R393 Methylation
K412 Acetylation
K412 Ubiquitination
S413 Phosphorylation
Y424 Phosphorylation
T425 Phosphorylation
K427 Ubiquitination
R435 Methylation
K438 Ubiquitination
K450 Ubiquitination
K458 Ubiquitination
T468 Phosphorylation
Y478 Phosphorylation P12931 (SRC) , P16591 (FER)
S482 Phosphorylation
Y483 Phosphorylation
S488 Phosphorylation
T497 Phosphorylation
Y499 Phosphorylation
K523 Ubiquitination
S535 Phosphorylation
S536 Phosphorylation
S539 Phosphorylation
T548 Phosphorylation
Y565 Phosphorylation
T567 Phosphorylation P17252 (PRKCA) , Q5S007 (LRRK2) , P41279 (MAP3K8) , O94804 (STK10) , O95819 (MAP4K4) , P25098 (GRK2) , P31751 (AKT2) , Q13464 (ROCK1) , Q04759 (PRKCQ) , Q9P289 (STK26) , P41743 (PRKCI) , O75116 (ROCK2)
T576 Phosphorylation
Site PTM Type Enzyme
K3 Ubiquitination
K35 Ubiquitination
Y55 Phosphorylation
T66 Phosphorylation
K72 Ubiquitination
K79 Acetylation
K79 Ubiquitination
K83 Ubiquitination
Y128 Phosphorylation
Y134 Phosphorylation
Y137 Phosphorylation
K139 Ubiquitination
K143 Ubiquitination
R151 Methylation
K162 Ubiquitination
K165 Ubiquitination
K209 Ubiquitination
K233 Ubiquitination
K237 Ubiquitination
S243 Phosphorylation
S249 Phosphorylation
K253 Acetylation
K253 Ubiquitination
K254 Ubiquitination
K258 Acetylation
K258 Ubiquitination
K262 Acetylation
K262 Sumoylation
K262 Ubiquitination
K263 Acetylation
K263 Ubiquitination
Y270 Phosphorylation
R273 Methylation
Y291 Phosphorylation
K296 Ubiquitination
T299 Phosphorylation
K306 Methylation
K306 Ubiquitination
K335 Ubiquitination
K344 Acetylation
K344 Ubiquitination
K352 Ubiquitination
K360 Ubiquitination
T369 Phosphorylation
K400 Ubiquitination
K405 Ubiquitination
K427 Ubiquitination
K435 Ubiquitination
K448 Ubiquitination
K526 Ubiquitination
S533 Phosphorylation
T542 Phosphorylation
K544 Ubiquitination
T545 Phosphorylation
K556 Acetylation
K556 Ubiquitination
Y562 Phosphorylation
T564 Phosphorylation O94804 (STK10) , P41279 (MAP3K8) , Q04759 (PRKCQ) , P25098 (GRK2) , O95819 (MAP4K4) , O75116 (ROCK2) , Q5S007 (LRRK2) , Q13464 (ROCK1)
T573 Phosphorylation
Site PTM Type Enzyme
K3 Ubiquitination
T4 Phosphorylation
K35 Acetylation
K35 Ubiquitination
S56 Phosphorylation
T57 Phosphorylation
K60 Acetylation
K64 Acetylation
K64 Ubiquitination
T66 Phosphorylation P34947 (GRK5)
R71 Methylation
K72 Ubiquitination
S74 Phosphorylation
K79 Acetylation
K79 Ubiquitination
K83 Acetylation
K83 Ubiquitination
T98 Phosphorylation
K107 Ubiquitination
Y116 Phosphorylation
S127 Phosphorylation
S132 Phosphorylation
K133 Acetylation
K139 Acetylation
K139 Ubiquitination
K143 Ubiquitination
S144 Phosphorylation
Y146 Phosphorylation
K151 Acetylation
K151 Ubiquitination
K162 Acetylation
K162 Ubiquitination
K165 Acetylation
K165 Ubiquitination
Y191 Phosphorylation
Y205 Phosphorylation
S207 Phosphorylation
K209 Ubiquitination
K211 Ubiquitination
K212 Ubiquitination
Y228 Phosphorylation
K237 Ubiquitination
S243 Phosphorylation
S249 Phosphorylation
K253 Acetylation
K253 Ubiquitination
K254 Ubiquitination
K258 Acetylation
K258 Ubiquitination
K262 Acetylation
K262 Sumoylation
K262 Ubiquitination
K263 Acetylation
K263 Ubiquitination
Y270 Phosphorylation
R273 Methylation
Y291 Phosphorylation
K296 Ubiquitination
T299 Phosphorylation
K306 Methylation
K306 Ubiquitination
K327 Acetylation
K344 Acetylation
K344 Ubiquitination
K352 Ubiquitination
K360 Ubiquitination
K380 Ubiquitination
S384 Phosphorylation
K388 Acetylation
K388 Ubiquitination
K391 Ubiquitination
K400 Acetylation
K400 Ubiquitination
S407 Phosphorylation
K412 Ubiquitination
T413 Phosphorylation
T425 Phosphorylation
S429 Phosphorylation
S440 Phosphorylation
K448 Ubiquitination
K458 Ubiquitination
K464 Ubiquitination
T465 Phosphorylation
S468 Phosphorylation
T469 Phosphorylation
S491 Phosphorylation
S504 Phosphorylation
K520 Ubiquitination
K523 Ubiquitination
T526 Phosphorylation
S527 Phosphorylation
S536 Phosphorylation
K537 Ubiquitination
K538 Ubiquitination
Y556 Phosphorylation
T558 Phosphorylation O95819 (MAP4K4) , Q5VT25 (CDC42BPA) , P41279 (MAP3K8) , Q04759 (PRKCQ) , O75116 (ROCK2) , Q5S007 (LRRK2) , P25098 (GRK2) , P17612 (PRKACA) , Q13464 (ROCK1) , Q9Y5S2 (CDC42BPB) , O94804 (STK10)
T567 Phosphorylation
S576 Phosphorylation

Research Backgrounds

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.

PTMs:

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).

S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex.

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. Cell projection>Microvillus.
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).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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.

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. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity). Detected in a complex composed of at least EZR, AHNAK, PPL and PRX (By similarity). Interacts with PDPN (via cytoplasmic domain); activates RHOA and promotes epithelial-mesenchymal transition. Interacts with SPN, CD44 and ICAM2 (By similarity).

Family&Domains:

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.

Function:

Ezrin-radixin-moesin (ERM) family protein that connects the actin cytoskeleton to the plasma membrane and thereby regulates the structure and function of specific domains of the cell cortex. Tethers actin filaments by oscillating between a resting and an activated state providing transient interactions between moesin and the actin cytoskeleton. Once phosphorylated on its C-terminal threonine, moesin is activated leading to interaction with F-actin and cytoskeletal rearrangement. These rearrangements regulate many cellular processes, including cell shape determination, membrane transport, and signal transduction. The role of moesin is particularly important in immunity acting on both T and B-cells homeostasis and self-tolerance, regulating lymphocyte egress from lymphoid organs. Modulates phagolysosomal biogenesis in macrophages (By similarity). Participates also in immunologic synapse formation.

PTMs:

Phosphorylation on Thr-558 is crucial for the formation of microvilli-like structures. 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). Phosphorylation on Thr-558 by STK10 negatively regulates lymphocyte migration and polarization.

S-nitrosylation of Cys-117 is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) implicating the iNOS-S100A8/9 transnitrosylase complex.

Subcellular Location:

Cell membrane>Peripheral membrane protein>Cytoplasmic side. Cytoplasm>Cytoskeleton. Apical cell membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection>Microvillus membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection>Microvillus.
Note: Phosphorylated form is enriched in microvilli-like structures at apical membrane. Increased cell membrane localization of both phosphorylated and non-phosphorylated forms seen after thrombin treatment (By similarity). Localizes at the uropods of T lymphoblasts.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

In all tissues and cultured cells studied.

Subunit Structure:

In resting T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted upon TCR activation. Interacts with SLC9A3R1. Interacts with PPP1R16B. Interacts with PDZD8. Interacts with SELPLG and SYK; these interaction mediate the activation of SYK by SELPLG. Interacts with PDPN (via cytoplasmic domain); this interaction activates RHOA and promotes epithelial-mesenchymal transition. Interacts with SPN/CD43. Interacts with CD44. Interacts with ICAM2 (By similarity). Interacts with ICAM3 (via C-terminus). Interacts with PDZD8. Interacts with F-actin. Interacts with CD46. Interacts with PTPN6 (By similarity).

(Microbial infection) Interacts with HIV-1 envelope protein gp120.

Family&Domains:

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.

Function:

Probably plays a crucial role in the binding of the barbed end of actin filaments to the plasma membrane.

PTMs:

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).

Subcellular Location:

Cell membrane>Peripheral membrane protein>Cytoplasmic side. Cytoplasm>Cytoskeleton. Cleavage furrow. Cell projection>Microvillus.
Note: Highly concentrated in the undercoat of the cell-to-cell adherens junction and the cleavage furrow in the interphase and mitotic phase, respectively.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Subunit Structure:

Binds SLC9A3R1. Interacts with NHERF1, NHERF2, LAYN, MME/NEP and ICAM2. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain). Interacts with SPN and CD44 (By similarity).

Family&Domains:

The N-terminal domain interacts with the C-terminal domain of LAYN. An interdomain interaction between its N-terminal and C-terminal domains inhibits its ability to bind LAYN. In the presence of acidic phospholipids, the interdomain interaction is inhibited and this enhances binding to LAYN (By similarity).

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Tight junction.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

· Human Diseases > Infectious diseases: Viral > Measles.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Overview > MicroRNAs in cancer.

· Organismal Systems > Immune system > Leukocyte transendothelial migration.   (View pathway)

· Organismal Systems > Digestive system > Gastric acid secretion.

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