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Ezrin

Ezrin is a cytoskeletal linker protein that plays a crucial role in the organization and regulation of the cell membrane.
It serves as a crosslink between the plasma membrane and the actin cytoskeleton, enabling important cellular processes such as cell motility, cell-cell adhesion, and signal transduction.
Ezrin's expression and localization are closely linked to various physiological and pathological conditions, making it a valuable target for research in areas like cancer, inflammation, and neurological disorders.
Optimizing Ezrin research can be achieved by leveraging the latest protocols and methods identified through AI-driven comparisons across literature, preprints, and patents.
This approach helps ensure the accuracy and reproducibility of Ezrin-related studies, ultimately enhancing the quality and impact of your research in this important field.

Most cited protocols related to «Ezrin»

1
Purification and Characterization of ERMAD and EBP50 Proteins
Cited 12 times
The cDNA sequences encoding the human ezrin and moesin N-ERMADs (amino acids 1–296) were amplified by PCR from clones F6 (Gould et al., 1989 (link)) and HEBA06 (a gift from Dr. Stachowitz, Gezentrum, Munich, Germany), respectively, using primers which generated EcoRI and HindIII sites at their ends. These products were then subcloned into the expression vector pQE16 (QIAGEN Inc., Chatsworth, CA). The cDNA sequence encoding residues 1-357 of ERM-binding phosphoprotein 50 (EBP50) was amplified by PCR with SphI and HindIII sites at the ends and subcloned into pQE70 (QIAGEN Inc.). Vector sequences coding for the six histidine tags were absent in all of the final constructs. To make the EBP50 COOH-terminal construct, the cDNA sequence encoding residues 241–357 was amplified by PCR using primers that created HindIII and BglII sites at the ends. This product was joined with the 0.99-kb BglI/HindIII fragment of pQE50 (QIAGEN Inc.) and the 2.42-kb BglI/BglII fragment of pQE16 in a three-arm ligation reaction to create the final His-tagged fusion construct. All recombinant sequences were determined to be free of PCR errors by nucleotide sequence analysis. Recombinant plasmids were propagated in the JM109 strain of Escherichia coli (Stratagene, La Jolla, CA).
For protein expression, plasmid constructs were transformed into the E. coli strain M15[pRep4] (QIAGEN, Inc.). Saturated overnight cultures were inoculated at 1:20 dilution in LB medium containing 100 μg/ml ampicillin and 25 μg/ml kanamycin, and grown for 90 min at 37°C. Isopropyl β-d-thiogalactopyranoside was added to 2 mM and cells were grown for an additional 180 min. Cells were harvested by centrifugation at 8,000 g for 15 min. Total bacterial lysates were prepared from cells resuspended in 1 vol of Laemmli buffer (Laemmli, 1970 (link)), boiled 2 min, and then passed through a 28-gauge needle to reduce viscosity.
To purify bacterially expressed ezrin or moesin N-ERMAD, induced cells were resuspended in 6 vol of 180 mM KH2PO4, pH 7.0, at 4°C, containing 50 μg/ml PMSF and 75 μg/ml benzamidine, lysed by sonication (Branson Ultrasonics Corp., Danbury, CT), clarified at 45,000 g for 10 min, and then loaded onto a preequilibrated hydroxyapatite column (HA–Ultragel; Pharmacia Fine Chemicals, Piscataway, NJ). The column was developed using a six-column volume linear gradient of 180–800 mM KH2PO4, and fractions were monitored by SDS-PAGE on 15% gels. Fractions rich in N-ERMAD were pooled, dialyzed against 20 mM MES, 150 mM NaCl, pH 6.7, at 4°C, centrifuged at 45,000 g for 10 min, applied to a preequilibrated S-Sepharose column (Pharmacia Fine Chemicals, Piscataway, NJ), and developed with a five-column volume linear gradient of 0.15–1.0 M NaCl. Homogenous N-ERMAD eluted at ∼490 mM NaCl.
To purify recombinant EBP50, induced bacterial lysates were prepared in TBS (50 mM Tris, 0.15 M NaCl, pH 7.4, at 4°C) in the presence of protease inhibitors, according to the method described above, and EBP50 affinity purified using N-ERMAD–coupled beads in a manner analogous to that used in the affinity binding assay. After washing the beads in TBS made up to 0.5 M NaCl, bound EBP50 was eluted with 2 M NaI, or by boiling the beads in Laemmli buffer.
The His-tagged EBP50 COOH-terminal fusion product was purified on nickel nitrilo-triacetic acid resin (QIAGEN) under denaturing conditions in 8 M urea, according to the manufacturer's protocol.
Reczek D., Berryman M, & Bretscher A. (1997). Identification of EBP50: A PDZ-containing Phosphoprotein that Associates with Members of the Ezrin-Radixin-Moesin Family. The Journal of Cell Biology, 139(1), 169-179.
Publication 1997
2
Establishment and Characterization of Patient-Derived Organoids
Cited 11 times
Upon resected sample receipt, fatty and necrotic tissues were removed macroscopically. Remaining tissue was rinsed with HBSS (Gibco), minced, and digested by Collagenase IV (Sigma-Aldrich), DNaseI (AppliChem, Germany) and Dispase (StemCell Technologies, Germany) at 37 °C for 60 min, followed by pelleting the suspension at 300 g for 3 min, re-suspension in medium and filtration steps as in Konno et al.71 (link). The 40–100 μm aggregates were centrifuged at 300 g for 3 min. After depletion of red blood cells using Red Blood Cell Lysis Solution (Miltenyi, Germany), cells were mixed with phenol-red free growth factor-reduced Matrigel (Corning) and seeded into 24-well plates. Solidified droplets were carefully overlaid with 500 μl of culture medium as in Sato et al.72 (link). During the first week 1.25 μg ml−1 Amphotericin B and 10 μM of the ROCK-II inhibitor Y27632 (Sigma-Aldrich) were added to cultures. The cultures were passaged when the aggregates reached a diameter of approximately 800 μm. Cellular aggregates were released from Matrigel by adding 5 ml Advanced DMEM/F12 followed by centrifugation. Pellets were digested with TrypLE (Gibco). Trypsinization was stopped with 5 ml Advanced DMEM/F12 and cell clusters were re-plated on a 24-well plate. PDO cell cultures were generated from 41 patient tumours and 5 xenografts (Supplementary Data 1). The cell cultures were routinely tested for Mycoplasma contamination and found to be negative.
For immunohistochemistry, 2 μm de-paraffinized FFPE tissue sections of donor tumours or PDO cultures grown for five days were stained using the primary antibodies anti-CK7 (clone OV-TL12/30, Dako, Germany), anti-CK20 (clone KS20.8, Dako), anti-CDX2 (clone CDX2-88, BioGenex, USA) and anti-KI67 (clone MIB-1, Dako) for 32 min at 37 °C, ultraView DAB detection kit (Ventana, USA) on the BenchMark XT instrument (Ventana). Counterstaining was performed with Hematoxylin II Counterstain and Blueing Reagent (Ventana) for 4 min. For immunofluorescence imaging, PDO cell aggregates were fixed and permeabilized with 4% PFA/1% Triton X for 30 min, followed by treatment with 1% Triton X overnight at 4 °C. PDO aggregates were then washed in PBS with 10% FCS. Primary anti-Ezrin antibody (clone 3C12, Thermo Scientific) was incubated at 4 °C for 48 h and removed by washing in PBS with 10% FCS. Secondary antibody (Alexa Fluor488, Invitrogen) was added at 4 °C overnight and removed by washing in PBS. Nuclei were stained with DAPI (Sigma-Aldrich) for 30 min. F-actin was stained accordingly with TRITC-labelled Phalloidin (Sigma-Aldrich). Microscopy was performed with a Zeiss Axiovert 400 microscope (Zeiss, Germany).
Schütte M., Risch T., Abdavi-Azar N., Boehnke K., Schumacher D., Keil M., Yildiriman R., Jandrasits C., Borodina T., Amstislavskiy V., Worth C.L., Schweiger C., Liebs S., Lange M., Warnatz H.J., Butcher L.M., Barrett J.E., Sultan M., Wierling C., Golob-Schwarzl N., Lax S., Uranitsch S., Becker M., Welte Y., Regan J.L., Silvestrov M., Kehler I., Fusi A., Kessler T., Herwig R., Landegren U., Wienke D., Nilsson M., Velasco J.A., Garin-Chesa P., Reinhard C., Beck S., Schäfer R., Regenbrecht C.R., Henderson D., Lange B., Haybaeck J., Keilholz U., Hoffmann J., Lehrach H, & Yaspo M.L. (2017). Molecular dissection of colorectal cancer in pre-clinical models identifies biomarkers predicting sensitivity to EGFR inhibitors. Nature Communications, 8, 14262.
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Publication 2017
Amphotericin B Antibodies Antibodies, Anti-Idiotypic Cell Culture Techniques Cell Nucleus Cells Centrifugation Clone Cells Collagenase Culture Media DAPI dispase Erythrocytes ezrin F-Actin Filtration Fluorescent Antibody Technique Growth Factor Hematoxylin Hemoglobin, Sickle Immunoglobulins Immunohistochemistry Ki-67 Antigen KRT20 protein, human matrigel Microscopy Mycoplasma Necrosis Neoplasms Patients Pellets, Drug ROCK2 protein, human Stem Cells tetramethylrhodaminylphalloidine Tissue Donors Tissues Xenografting Y 27632
3
Detecting Endothelial NO Bioavailability
Cited 7 times
Bioavailable NO• produced by confluent endothelial cells was detected using electron spin resonance (ESR) as we previously published [27, 28].
Youn J.Y., Wang T, & Cai H. (2008). An Ezrin/Calpain/PI3K/AMPK/eNOSs1179 Signaling Cascade Mediating VEGF-dependent Endothelial Nitric Oxide Production. Circulation research, 104(1), 50-59.
Publication 2008
Electron Spin Resonance Spectroscopy Endothelial Cells
4
Apoptosis Analysis in Tumor Model
Cited 7 times
Tumor volumes, body weights and percentage of apoptotic cells were represented as mean±s.d. Statistical analyses were performed using the two-tailed Student's t test. P<0.05 (*) or P<0.01 (**) were considered significant.
Li G., Zhou T., Liu L., Chen J., Zhao Z., Peng Y., Li P, & Gao N. (2013). Ezrin dephosphorylation/downregulation contributes to ursolic acid-mediated cell death in human leukemia cells. Blood Cancer Journal, 3(4), e108-.
Publication 2013
Apoptosis Body Weight Cells
5
Conditional Knockout of LRRK2 in Mice
Cited 7 times
A genomic DNA fragment carrying the first two coding exons of LRRK2 was isolated from the RPCI-22 (129S6/SvEvTac) Mouse BAC Library (BACPAC Resources Center). One copy of a LoxP site was inserted into intron 1 followed by an insertion of a FRT-flanked neomycin expression cassette and the second copy of LoxP site into intron 2 of LRRK2. The targeting vector was linearized and transfected into 129/SvJ ES cells, which were later subjected to G418 selection for 7 days. The G418 resistant ES clones were picked and screened by Southern blot analysis for the correctly targeted clones. Two positive ES clones were expanded and injected into blastocysts. The resulting male chimera mice were bred with wild-type C57BL/6J female mice to obtain LRRK2+/neo mice. LRRK2+/neo mice were then crossed with Cre transgenic mice (Lakso et al., 1996 (link)) to generate LRRK2+/- mice in which exon 2 was deleted by Cre-mediated DNA recombination, resulting in a premature stop codon in exon 3. The heterozygous LRRK2+/- mice were intercrossed to generate the homozygous LRRK2-/- mice.
Parisiadou L., Xie C., Cho H.J., Lin X., Gu X.L., Long C.X., Lobbestael E., Baekelandt V., Taymans J.M., Sun L, & Cai H. (2009). Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis. The Journal of Neuroscience, 29(44), 13971-13980.
Publication 2009
antibiotic G 418 Blastocyst Chimera Clone Cells Cloning Vectors Codon, Nonsense DNA Library Embryonic Stem Cells Exons Females Genome Heterozygote Homozygote Introns LRRK2 protein, human Males Mice, Inbred C57BL Mice, Laboratory Mice, Transgenic Neomycin Recombination, Genetic Southern Blotting

Most recents protocols related to «Ezrin»

1
Silencing Ezrin in Endothelial Cells
RNA interference was involved in present study to silence Ezrin gene in ECs. Log-phase ECs were harvested and seeded in a 75 cm2 culture flask at density of 2×107. When 70-80% confluency was reached, Ezrin siRNA (SignalSilence® Ezrin siRNA I, CellSignaling Technology) was added at a final concentration of 100 nM by siRNA Transfection Reagent (sc-29528; Santa Cruz Biotechnology). After 24 h transfection, cells were harvested for further experiments.
Zhuo D., Mei Y., Lin C., Wu A., Luo Y., Lu H, & Fu J. (2024). Nudifloside, a Secoiridoid Glucoside Derived from Callicarpa nudiflora, Inhibits Endothelial-to-Mesenchymal Transition and Angiogenesis in Endothelial Cells by Suppressing Ezrin Phosphorylation. Journal of Cancer, 15(9), 2448-2459.
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Publication 2024
2
Investigating ARHGAP18-Ezrin Interaction
To determine the interaction between ARHGAP18 and ezrin, pulldown assays were performed using cell lysate from Jeg3 wildtype and Jeg3 LOK-/-SLK-/- cells. Transfections were performed using PEI MAX polyethylenimine reagent (Polysciences; Cat# 24765). After transfection, cells were washed with phosphate-buffered saline (PBS) and harvested with lysis buffer (25 mM Tris, 5% glycerol, 150 mM NaCl, 50 mM NaF, 0.1 mM Na3VO4, 10mM βGP, 0.2% Triton X-100, 250 mM calyculin A, 1 mM DTT, 1× cOmplete Protease Inhibitor Cocktail [Roche; Cat# 11836153001]) by scraping. Lysates were then sonicated, and any insoluble material was centrifuged at 8000 × g for 10 min at 4°C. Before incubating with the cell lysates, SUMO-ARHGAP18 NiNTA or M2-Flag resin beads were equilibrated and washed into lysis buffer. The sample of the supernatant was taken for input, then the rest was added to the SUMO-ARHGAP18 NiNTA or M2-Flag beads and nutated for 3 hr at 4°C. After incubation, the beads were pelleted and washed four times before boiling in 40 µL 2× Laemmli sample buffer.
Lombardo A.T., Mitchell C.A., Zaman R., McDermitt D.J, & Bretscher A. (2024). ARHGAP18-ezrin functions as an autoregulatory module for RhoA in the assembly of distinct actin-based structures. eLife, 13, e83526.
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Publication 2024
3
Ratiometric Actin Filament Visualization
DeAct-GS1—EGFP-caax and Ezrin(abd*) constructs were created using InFusion cloning (Takara Bio) by annealing one DNA fragment into the parent plasmid. The parent plasmid contains a 1.3 kb MBP promoter driving expression of (farnesylated, membrane-bound) EGFP-caax in a pAAV vector backbone and was linearized using NcoI and BglI. The fragment encoding for either human gelsolin segment 1 (GS1, the actin-severing domain; aa 53-176, Addgene # 89445)59 (link) or human Ezrin(abd*) (Ezrin aa 552-586 with T567D constitutively-active mutation, Addgene #155227)61 (link) was cloned with 15 base pair overhangs required for InFusion reactions. This created constructs with the following configuration: pMBP-GS1-EGFP-caax or pMBP-Ezrin(ABD*)-EGFP-caax. pMBP-EGFP-caax AAV vector (Addgene #190155) was previously reported15 (link).
To detect actin filaments in live cells, genetically encodable Lifeact93 (link) is the field standard. However, Lifeact has been shown to bind actin monomers. To overcome this issue and visualize only actin filaments, we generated Ratiometric Lifeact (RMLA). RMLA constructs were created using InFusion cloning (Takara Bio) by annealing two DNA fragments into the parent plasmid. The parent plasmid contains a 1.3 kb MBP promoter driving expression of Lifeact-mRuby3 in a pAAV vector and was linearized using BamHI and BglI. Two fragments encoding self-cleaving peptide P2A-T2A94 (link) and mClover3 (cytoplasmic) were PCR-amplified with 15 base pair overhangs required for InFusion reactions and inserted into the backbone. This created constructs with the following configuration: pMBP-Lifeact-mRuby3-P2AT2A-mClover3. This (in principle) results in equimolar production of Lifeact-mRuby3 and cytoplasmic mClover3 in a cell, which can be divided to generate a ratiometric signal specific for actin filaments. All DNA constructs generated for this paper will be made publicly available by AddGene at the time of publication. All correspondence and requests for materials should be addressed to J.B.Z.
Iyer M., Kantarci H., Cooper M.H., Ambiel N., Novak S.W., Andrade L.R., Lam M., Jones G., Münch A.E., Yu X., Khakh B.S., Manor U, & Zuchero J.B. (2024). Oligodendrocyte calcium signaling promotes actin-dependent myelin sheath extension. Nature Communications, 15, 265.
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Publication 2024
4
Molecular Signaling in Vascular Development
NDF (purity ≥ 95%) is product of APExBIO Technology LLC (Houston, Texas). VEGF165 (HY-P7110A) and TGF-β1(HY-P78168) were purchased from MedChemExpress LLC (Shanghai, China). PTK787 (S1101) and TGF-βRI inhibitor SD208 (S7624) were purchased from Selleck (Shanghai, China). Alexa Fluor™ 488 Phalloidin (A12379) was purchased from ThermoFisher Scientific (Shanghai, China). Several primary antibodies were used in present study. Antibodies of Ezrin (ab40839), p-Ezrin (phosphor T567, ab47293), PODXL (ab150358), CD31 (ab9498), α-SMA (ab7817), I-Col(ab138492), III-Col (ab184993), β-Actin (ab8226), VE-Cadherin (ab3136320 and ICAM-1 (ab282575) were the products of Abcam.
Zhuo D., Mei Y., Lin C., Wu A., Luo Y., Lu H, & Fu J. (2024). Nudifloside, a Secoiridoid Glucoside Derived from Callicarpa nudiflora, Inhibits Endothelial-to-Mesenchymal Transition and Angiogenesis in Endothelial Cells by Suppressing Ezrin Phosphorylation. Journal of Cancer, 15(9), 2448-2459.
Full text: Click here
Publication 2024
5
Measuring ARHGAP18-Ezrin/FERM Binding by ITC
Purified ARHGAP18 was produced as described in the antibody production except that the SUMO tag was not cleaved as it was found that the protein was insoluble above 2 mg/mL without it. Purified ezrin and FERM were produced as described in Viswanatha et al., 2012 (link). Ezrin or FERM were diluted to 75–80 µM depending on the purified volume and number of injections needed for ITC. The proteins were then injected into 30 µM SUMO-ARHGAP18 using automated injections on a TA Instruments-Waters LLC (New Castle, DE) Affinity ITC-LV. Injections were performed using ITC run software (TA Instruments) with a minimum pulse time of 200 s and 2–5 μL injections and a stirring rate of 175 rotations per minute. The system was calibrated using the injection of water into water as a negative control and the injection of 0.95 mM CaCl2 into 0.150 mM EDTA as a positive control. Injections were continued until saturation of the binding was observed through a plateau of the released energy per injection or the max volume of the injection syringe was depleted. Collected ITC data were then imported into NanoAnalyze software (TA Instruments), and a baseline linear curve representing the energy from injecting water into water was subtracted leaving a normalized energy injection dataset. Injection points from either the first injection or injections after the binding affinity had plateaued were excluded and the remaining data points were then fit to a single independent binding curve. FL-ezrin or FERM injections that did not show an absorbance curve were not fit to one in the NanoAnalyze program as part of a pre-exclusion criteria.
Lombardo A.T., Mitchell C.A., Zaman R., McDermitt D.J, & Bretscher A. (2024). ARHGAP18-ezrin functions as an autoregulatory module for RhoA in the assembly of distinct actin-based structures. eLife, 13, e83526.
Full text: Click here
Publication 2024

Top products related to «Ezrin»

1
Lipofectamine 2000 by Thermo Fisher Scientific
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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.
2
Ezrin by Cell Signaling Technology
Sourced in United States
Ezrin is a recombinant protein produced by Cell Signaling Technology. It is a member of the ezrin-radixin-moesin (ERM) family of proteins, which function as linkers between the actin cytoskeleton and the plasma membrane. Ezrin plays a role in cellular processes such as cell adhesion, cell migration, and signal transduction.
3
Fetal bovine serum (fbs) by Thermo Fisher Scientific
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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.
4
Trizol reagent by Thermo Fisher Scientific
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TRIzol reagent is a monophasic solution of phenol, guanidine isothiocyanate, and other proprietary components designed for the isolation of total RNA, DNA, and proteins from a variety of biological samples. The reagent maintains the integrity of the RNA while disrupting cells and dissolving cell components.
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PVDF membranes are a type of laboratory equipment used for a variety of applications. They are made from polyvinylidene fluoride (PVDF), a durable and chemically resistant material. PVDF membranes are known for their high mechanical strength, thermal stability, and resistance to a wide range of chemicals. They are commonly used in various filtration, separation, and analysis processes in scientific and research settings.
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Bovine serum albumin (BSA) is a common laboratory reagent derived from bovine blood plasma. It is a protein that serves as a stabilizer and blocking agent in various biochemical and immunological applications. BSA is widely used to maintain the activity and solubility of enzymes, proteins, and other biomolecules in experimental settings.
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4 6 diamidino 2 phenylindole (dapi) by Thermo Fisher Scientific
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DAPI is a fluorescent dye used in microscopy and flow cytometry to stain cell nuclei. It binds strongly to the minor groove of double-stranded DNA, emitting blue fluorescence when excited by ultraviolet light.
8
Ezrin by Santa Cruz Biotechnology
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Ezrin is a laboratory equipment product offered by Santa Cruz Biotechnology. Ezrin is a cytoskeletal protein that connects the cell membrane to the actin cytoskeleton. It is involved in the regulation of cell shape, motility, and organization.
9
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DAPI is a fluorescent dye that binds strongly to adenine-thymine (A-T) rich regions in DNA. It is commonly used as a nuclear counterstain in fluorescence microscopy to visualize and locate cell nuclei.

More about "Ezrin"

Ezrin, a crucial cytoskeletal linker protein, plays a pivotal role in organizing and regulating the cell membrane.
It serves as a crucial crosslink between the plasma membrane and the actin cytoskeleton, enabling vital cellular processes such as cell motility, cell-cell adhesion, and signal transduction.
Ezrin's expression and localization are closely associated with various physiological and pathological conditions, making it a valuable target for research in areas like cancer, inflammation, and neurological disorders.
To optimize Ezrin research, researchers can leverage the latest protocols and methods identified through AI-driven comparisons across literature, preprints, and patents.
This approach helps ensure the accuracy and reproducibility of Ezrin-related studies, ultimately enhancing the quality and impact of your research in this important field.
PubCompare.ai, a powerful AI-driven platform, can assist researchers in locating the best protocols for Ezrin research.
By comparing methods from various sources, including scientific literature, preprints, and patents, PubCompare.ai identifies the most accurate and reproducible techniques, improving the quality and reliability of your Ezrin research.
When conducting Ezrin experiments, researchers may utilize various reagents and techniques, such as Lipofectamine 2000 for transfection, FBS (Fetal Bovine Serum) for cell culture, TRIzol reagent for RNA extraction, PVDF membranes for Western blotting, Bovine Serum Albumin (BSA) for blocking, and DAPI for nuclear staining.
Lipofectamine 3000 is another transfection reagent that can be used for Ezrin-related studies.
Optimizing Ezrin research can lead to advancements in our understanding of its role in cellular processes and its potential as a target for various therapeutic applications.
By leveraging the power of AI-driven comparisons and the latest protocols, researchers can ensure the accuracy and reproducibility of their Ezrin-related studies, ultimately enhancing the quality and impact of their research in this important field.