Phospho-EZR (Tyr146) Antibody

What is Phospho-EZR (Tyr146) Antibody and what specific epitope does it recognize?

Phospho-EZR (Tyr146) Antibody is a rabbit polyclonal antibody that specifically detects endogenous levels of Ezrin protein only when phosphorylated at tyrosine 146 (Tyr146) . The antibody is generated against a synthesized peptide derived from human Ezrin surrounding the phosphorylation site of Tyr146, specifically within amino acid range 111-160 . This antibody recognizes the phosphorylated form of Ezrin, which is critical for studying the activation state of Ezrin in various cellular processes. The specificity of this antibody makes it an essential tool for researchers investigating phosphorylation-dependent functions of Ezrin in cytoskeletal organization and membrane dynamics .

What are the validated applications for Phospho-EZR (Tyr146) Antibody?

Based on the technical validation data, Phospho-EZR (Tyr146) Antibody has been thoroughly tested and validated for Western Blot (WB) and Enzyme-Linked Immunosorbent Assay (ELISA) applications . For Western blotting applications, the recommended dilution range is 1:500-1:2000, allowing researchers to optimize based on their specific experimental conditions and sample types . For ELISA applications, a much higher dilution of 1:40000 is typically recommended . The antibody has been verified using positive controls such as 293 cells treated with UV for 15 minutes, which induces Ezrin phosphorylation at Tyr146 . Importantly, validation experiments have confirmed specificity by demonstrating that signal detection is blocked when the antibody is pre-incubated with the phospho-peptide, providing researchers with confidence in the antibody's selective recognition of the phosphorylated epitope .

What species reactivity has been confirmed for this antibody?

The Phospho-EZR (Tyr146) Antibody has been validated to react with Ezrin proteins from multiple mammalian species, specifically Human, Mouse, and Rat . This cross-species reactivity is based on the high conservation of the amino acid sequence surrounding the Tyr146 phosphorylation site across these species . The multi-species reactivity makes this antibody particularly valuable for comparative studies and translational research where findings in rodent models can be related to human biology . When designing experiments using this antibody across different species, researchers should consider potential variations in protein expression levels and phosphorylation dynamics, even though the epitope itself is recognized across these species .

What are the optimal storage conditions and stability parameters for Phospho-EZR (Tyr146) Antibody?

For long-term preservation of antibody activity, Phospho-EZR (Tyr146) Antibody should be stored at -20°C for up to one year from the date of receipt . The antibody is supplied in a stabilizing solution containing PBS with 50% glycerol, 0.5% BSA, and 0.02% sodium azide at pH 7.3, which helps maintain its structural integrity and binding capacity during storage . For short-term storage and frequent use, the antibody can be kept at 4°C for up to one month . To maximize antibody longevity and performance, it is critical to avoid repeated freeze-thaw cycles, which can lead to protein denaturation and loss of binding activity . Researchers are advised to prepare small working aliquots upon initial thawing to minimize the need for repeated freezing and thawing of the stock solution .

What are the recommended Western blot protocols for optimal results with Phospho-EZR (Tyr146) Antibody?

For optimal Western blot results with Phospho-EZR (Tyr146) Antibody, researchers should follow this methodological approach: Begin with proper sample preparation by lysing cells in a buffer containing phosphatase inhibitors to preserve the phosphorylation state of Ezrin . Separate proteins using SDS-PAGE, then transfer to a PVDF or nitrocellulose membrane. Block the membrane with 5% BSA in TBST (not milk, which contains phosphatases that could reduce signal) . Incubate with Phospho-EZR (Tyr146) Antibody at a dilution of 1:500-1:2000 in blocking buffer overnight at 4°C . After thorough washing with TBST, incubate with an appropriate HRP-conjugated secondary antibody . The expected molecular weight for the phosphorylated Ezrin protein is approximately 69 kDa . For validation, researchers should include positive controls (e.g., lysates from cells treated with UV for 15 minutes) and negative controls (e.g., samples pre-treated with phosphatase or blots incubated with antibody pre-absorbed with the phospho-peptide) .

How can researchers effectively troubleshoot weak or non-specific signals when using this antibody?

When encountering weak or non-specific signals with Phospho-EZR (Tyr146) Antibody, researchers should systematically address several methodological factors. For weak signals, first verify the phosphorylation status of Ezrin in your samples, as phosphorylation at Tyr146 may be transient or context-dependent . Consider stimulating cells with appropriate treatments known to induce Ezrin phosphorylation . Optimize antibody concentration by testing a range of dilutions (1:500, 1:1000, 1:2000) to determine the optimal signal-to-noise ratio for your specific sample type . Increase protein loading amounts and extend exposure times cautiously to enhance signal detection without introducing background . For non-specific bands, increase blocking stringency using 5% BSA in TBST and consider adding 0.1-0.5% Tween-20 to antibody dilution buffers . Ensure thorough washing steps between antibody incubations . If high background persists, try titrating the secondary antibody to lower concentrations . For confirmation of specificity, perform a peptide competition assay using the phosphorylated peptide immunogen, which should abolish specific binding as demonstrated in validation studies .

What are effective strategies for quantifying Ezrin Tyr146 phosphorylation levels in experimental samples?

For accurate quantification of Ezrin Tyr146 phosphorylation levels, researchers should implement a comprehensive analytical strategy. Begin by running parallel Western blots for both phosphorylated Ezrin (using Phospho-EZR (Tyr146) Antibody) and total Ezrin protein (using a non-phospho-specific Ezrin antibody) . Normalize the phospho-Ezrin signal to the total Ezrin signal to account for variations in total protein expression across samples . Include housekeeping proteins (e.g., GAPDH, β-actin) as loading controls to ensure equal protein loading . For densitometric analysis, use specialized software (ImageJ, Image Lab, etc.) to quantify band intensities within the linear range of detection . Perform biological replicates (n≥3) and calculate the phospho-Ezrin/total Ezrin ratio for each experimental condition . For more precise quantification, consider using ELISA-based approaches with the Phospho-EZR (Tyr146) Antibody at a 1:40000 dilution, which can provide more sensitive and quantitative measurements, particularly for samples with low phosphorylation levels . Statistical analysis should be performed to determine the significance of observed changes in phosphorylation levels across experimental conditions .

How should researchers prepare and validate positive and negative controls for Phospho-EZR (Tyr146) Antibody experiments?

Rigorous experimental design with appropriate controls is essential when working with Phospho-EZR (Tyr146) Antibody. For positive controls, treat cells with known inducers of Ezrin Tyr146 phosphorylation, such as UV exposure (15 minutes), which has been validated in previous studies . Alternative positive controls include treatment with growth factors, oxidative stress inducers, or tyrosine kinase activators that have been documented to increase Ezrin phosphorylation . For negative controls, several approaches are recommended: (1) Pre-treatment of cell lysates with lambda phosphatase to remove phosphate groups from all proteins, which should eliminate the phospho-specific signal ; (2) Peptide competition assay, where the antibody is pre-incubated with the phosphorylated peptide immunogen before application to the blot, which should block specific binding ; (3) Use of Ezrin-knockdown or knockout cell lines, which should show reduced or absent signal for both phosphorylated and total Ezrin ; (4) Use of cell lines known to express low levels of Ezrin or those cultured under conditions that minimize Tyr146 phosphorylation . Implementing these controls systematically will strengthen the validity and interpretability of experimental results with this antibody .

How does Ezrin Tyr146 phosphorylation relate to its functional roles in membrane-cytoskeleton interactions?

Ezrin Tyr146 phosphorylation represents a critical regulatory mechanism that influences membrane-cytoskeleton interactions in several important ways. Ezrin functions as a linker between the plasma membrane and actin cytoskeleton, particularly in epithelial cells where it is required for the formation of microvilli and membrane ruffles on the apical pole . Phosphorylation at Tyr146 is one of several post-translational modifications that regulate Ezrin's conformational state and activity . When Ezrin is in its inactive form, it adopts a closed conformation due to intramolecular interactions between its N-terminal FERM domain and C-terminal actin-binding domain . Phosphorylation at Tyr146 disrupts these interactions, promoting an open, active conformation that enables simultaneous binding to membrane proteins and the actin cytoskeleton . In contrast to phosphorylation at threonine 567 (Thr567), which has been more extensively studied, Tyr146 phosphorylation may regulate distinct aspects of Ezrin function or exhibit cell type-specific effects . Research using Phospho-EZR (Tyr146) Antibody has revealed that this modification affects Ezrin's participation in macropinocytosis, a process requiring coordination between the plasma membrane and underlying cytoskeleton . Understanding the spatiotemporal regulation of Tyr146 phosphorylation is essential for elucidating Ezrin's role in dynamic cellular processes like cell migration, adhesion, and morphogenesis .

What experimental approaches can be used to study the relationship between Ezrin Tyr146 phosphorylation and PLEKHG6 in macropinocytosis?

To investigate the functional relationship between Ezrin Tyr146 phosphorylation and PLEKHG6 in macropinocytosis, researchers should employ a multi-faceted experimental approach. Begin with co-immunoprecipitation assays using Phospho-EZR (Tyr146) Antibody to determine whether phosphorylated Ezrin preferentially interacts with PLEKHG6 compared to non-phosphorylated Ezrin . Complement this with reverse co-IP using PLEKHG6 antibodies and blotting with Phospho-EZR (Tyr146) Antibody . For functional studies, establish cell models with either knockdown/knockout of Ezrin using siRNA/CRISPR technologies, or expression of phospho-mimetic (Y146E) and phospho-deficient (Y146F) Ezrin mutants . In these models, assess macropinocytosis efficiency using fluorescent dextran uptake assays while manipulating PLEKHG6 expression levels . Live-cell imaging with fluorescently tagged Ezrin and PLEKHG6 constructs will reveal their spatiotemporal dynamics during macropinocytosis events . For mechanistic insights, investigate downstream signaling pathways using phospho-specific antibodies against components of Rho GTPase signaling, which are known to be regulated by both Ezrin and PLEKHG6 . Finally, perform structured illumination or super-resolution microscopy with Phospho-EZR (Tyr146) Antibody to visualize the precise localization of phosphorylated Ezrin relative to PLEKHG6 and membrane ruffles during various stages of macropinocytosis .

How can phosphorylation at Tyr146 be distinguished from other Ezrin phosphorylation sites in experimental analyses?

Distinguishing Ezrin phosphorylation at Tyr146 from other phosphorylation sites requires precise methodological approaches. The Phospho-EZR (Tyr146) Antibody has been specifically developed to recognize Ezrin only when phosphorylated at the Tyr146 position, making it an essential tool for site-specific phosphorylation analysis . To confirm this specificity, researchers should perform peptide competition assays with phospho-Tyr146 peptides versus peptides phosphorylated at other sites (e.g., Thr567, Tyr353) . For comprehensive phosphorylation profiling, combine Western blotting with multiple phospho-specific antibodies targeting different Ezrin phosphorylation sites and compare their dynamics under various stimuli . Mass spectrometry-based phosphoproteomic analysis offers the most definitive approach for distinguishing multiple phosphorylation sites simultaneously . Using this technique, researchers can identify the exact residues that are phosphorylated and their relative abundance after immunoprecipitation with total Ezrin antibodies . For functional studies, express site-specific phospho-mimetic (Y146E) and phospho-deficient (Y146F) Ezrin mutants in Ezrin-depleted cells and compare their effects on cellular processes with mutants of other phosphorylation sites . Lastly, use computational modeling to predict how phosphorylation at different sites might distinctly affect Ezrin's three-dimensional structure and protein-protein interaction interfaces .

What are the key considerations when developing immunofluorescence protocols with Phospho-EZR (Tyr146) Antibody?

Although not explicitly listed among the validated applications in the search results, researchers interested in adapting the Phospho-EZR (Tyr146) Antibody for immunofluorescence studies should consider several critical factors for protocol optimization. First, fixation method is crucial—paraformaldehyde fixation (4%, 15-20 minutes) preserves phospho-epitopes better than methanol, which can lead to phosphate group loss . Include phosphatase inhibitors (sodium orthovanadate, sodium fluoride) in all buffers to prevent dephosphorylation during sample processing . For permeabilization, use a gentle detergent like 0.1% Triton X-100 rather than harsher agents that might disrupt the phospho-epitope . Blocking should be performed with 5% BSA rather than serum-based blockers that might contain phosphatases . Begin antibody titration at higher concentrations than those used for Western blotting (starting at 1:200-1:500) and extend incubation times (overnight at 4°C) . Include critical controls: positive controls (cells treated with UV or growth factors known to induce Tyr146 phosphorylation) and negative controls (lambda phosphatase-treated samples, peptide competition, and secondary-only controls) . For double-labeling experiments, combine with antibodies against proteins known to co-localize with activated Ezrin, such as F-actin or membrane markers of the apical domain . Due to the typically low abundance of phosphorylated proteins, consider signal amplification systems like tyramide signal amplification if conventional detection yields weak signals .

What is the relationship between Ezrin Tyr146 phosphorylation and other post-translational modifications of Ezrin?

Ezrin undergoes complex regulation through multiple post-translational modifications that can interact functionally with Tyr146 phosphorylation. Phosphorylation at threonine 567 (Thr567) by ROCK2 is one of the best-characterized modifications, which suppresses the head-to-tail association of Ezrin's N-terminal and C-terminal domains, resulting in an opened conformation capable of actin and membrane binding . Tyr146 phosphorylation, mediated by tyrosine kinases, may work in concert with or independently from Thr567 phosphorylation to regulate Ezrin activation in a context-dependent manner . Additionally, Ezrin can undergo S-nitrosylation induced by interferon-gamma and oxidatively-modified low-density lipoprotein (LDL(ox)), potentially involving the iNOS-S100A8/9 transnitrosylase complex . This modification may influence Ezrin's ability to be phosphorylated at various sites or alter the functional consequences of phosphorylation . The temporal sequence of these modifications is critical—evidence suggests that in some cellular contexts, Tyr146 phosphorylation might precede and facilitate Thr567 phosphorylation, creating a sequential activation mechanism . Researchers should consider using multiple phospho-specific antibodies to track different modifications simultaneously when studying Ezrin regulation . Mass spectrometry-based approaches can further reveal how the pattern of post-translational modifications changes under different physiological and pathological conditions, providing insights into the combinatorial code that governs Ezrin function .

How can researchers differentiate between specific and non-specific signals when interpreting Western blot results?

Distinguishing specific from non-specific signals when interpreting Western blot results with Phospho-EZR (Tyr146) Antibody requires systematic analytical approaches. First, verify that the detected band appears at the expected molecular weight of approximately 69 kDa for Ezrin . Confirm specificity through peptide competition assays—pre-incubation of the antibody with the phosphorylated peptide immunogen should dramatically reduce or eliminate the specific signal while leaving non-specific bands unchanged, as demonstrated in validation studies . Compare the band pattern obtained with the Phospho-EZR (Tyr146) Antibody to that observed with a total Ezrin antibody; while the intensity may differ based on the phosphorylation state, the molecular weight should be consistent . Assess signal modulation under conditions known to affect Ezrin phosphorylation—treatment with tyrosine kinase activators should increase the signal, while tyrosine phosphatase activators or kinase inhibitors should decrease it . Examine negative control samples, such as Ezrin-knockout or knockdown cells, which should show reduced or absent specific signal . For borderline cases, perform immunoprecipitation with total Ezrin antibodies followed by Western blotting with Phospho-EZR (Tyr146) Antibody to enrich for the protein of interest and confirm identity . Finally, consider cross-validation with alternative detection methods, such as mass spectrometry, to confirm the presence of phosphorylated Tyr146 in your experimental system .

What are the technical considerations for using Phospho-EZR (Tyr146) Antibody in studying disease models?

When applying Phospho-EZR (Tyr146) Antibody to disease model research, several technical considerations are essential for generating reliable and translatable data. First, carefully assess the baseline phosphorylation status of Ezrin at Tyr146 in your specific disease model, as altered kinase/phosphatase activities in pathological states may significantly affect this modification . For cancer models, where Ezrin is frequently dysregulated, compare phosphorylation levels between tumor and adjacent normal tissues using consistent sample processing protocols that preserve phospho-epitopes . When working with animal models of human diseases, remember that while the antibody recognizes human, mouse, and rat Ezrin, species-specific differences in regulatory pathways may influence the phosphorylation dynamics . For chronic disease models, temporal analysis is critical—collect samples at multiple time points to track changes in Tyr146 phosphorylation throughout disease progression . In studies involving therapeutic interventions, monitor how treatments affect Ezrin phosphorylation, as this may provide mechanistic insights into drug efficacy . When analyzing clinical specimens, standardize pre-analytical variables (collection, fixation, storage times) to minimize phospho-epitope degradation . For difficult-to-detect phosphorylation events in diseased tissues, consider phospho-enrichment techniques prior to Western blotting . Finally, always incorporate internal controls reflecting disease-relevant conditions in each experiment to account for the potentially altered cellular environments that might influence antibody performance .

How can researchers integrate Phospho-EZR (Tyr146) Antibody data with other phosphoproteomic approaches?

Integrating data obtained with Phospho-EZR (Tyr146) Antibody into broader phosphoproteomic studies requires methodological alignment and complementary analytical strategies. Begin by establishing a clear correlation between antibody-based detection and mass spectrometry-based phosphopeptide identification of Ezrin Tyr146 phosphorylation . This can be achieved by immunoprecipitating Ezrin from experimental samples using total Ezrin antibodies, followed by parallel analysis with Phospho-EZR (Tyr146) Antibody via Western blotting and phosphopeptide identification via LC-MS/MS . For quantitative integration, normalize Western blot band intensities using standard curves generated with synthesized phosphopeptides at known concentrations . When performing pathway analysis, combine Phospho-EZR (Tyr146) antibody data with phosphoproteomic datasets of known Ezrin-interacting proteins to build comprehensive signaling networks . For temporal studies, synchronize sampling time points between antibody-based detection and global phosphoproteomic profiling to enable direct comparisons of Ezrin phosphorylation dynamics relative to the broader phosphoproteome . Consider using multiplexed antibody arrays that include Phospho-EZR (Tyr146) alongside antibodies targeting other components of cytoskeletal regulatory pathways . For systems biology approaches, integrate antibody-derived quantitative data on Ezrin Tyr146 phosphorylation with transcriptomic and proteomic datasets to develop multi-omics models of cytoskeletal regulation . Finally, validate key findings from global phosphoproteomic studies regarding Ezrin phosphorylation using the highly specific Phospho-EZR (Tyr146) Antibody to confirm the mass spectrometry results in targeted experiments .

What are the most common technical challenges when using Phospho-EZR (Tyr146) Antibody and how can they be addressed?

Researchers using Phospho-EZR (Tyr146) Antibody may encounter several technical challenges that can be systematically addressed through specific methodological adjustments. One common issue is weak or absent signal despite the presence of phosphorylated Ezrin . This can be addressed by: (1) Ensuring complete inhibition of phosphatases during sample preparation by using fresh phosphatase inhibitor cocktails containing both serine/threonine and tyrosine phosphatase inhibitors ; (2) Optimizing protein extraction conditions by using different lysis buffers (RIPA vs. NP-40) to improve solubilization while preserving phospho-epitopes ; (3) Reducing antibody dilution to 1:500 rather than 1:2000 for samples with low phosphorylation levels . Another frequent challenge is high background or non-specific bands . This can be mitigated by: (1) Increasing blocking stringency (5% BSA in TBST for 2 hours at room temperature) ; (2) Extending washing steps (5-6 washes of 10 minutes each) ; (3) Using alternative membrane types (PVDF vs. nitrocellulose) if background persists . For inconsistent results across experiments, researchers should: (1) Standardize cell culture conditions, as confluence levels and serum factors significantly affect Ezrin phosphorylation ; (2) Use internal loading controls and positive controls in every experiment ; (3) Prepare larger batches of working antibody dilution to use across multiple experiments . Finally, for degradation of signal over time, aliquot the antibody upon first thawing and strictly avoid repeated freeze-thaw cycles .

How can researchers optimize sample preparation to preserve Ezrin Tyr146 phosphorylation for antibody detection?

Preserving Ezrin Tyr146 phosphorylation during sample preparation is critical for reliable detection using Phospho-EZR (Tyr146) Antibody. Begin by harvesting cells rapidly, preferably by direct addition of hot SDS sample buffer to culture plates for immediate protein denaturation and phosphatase inactivation . If this direct approach is not feasible, use ice-cold lysis buffers supplemented with comprehensive phosphatase inhibitor cocktails containing sodium orthovanadate (1-2 mM), sodium fluoride (10-20 mM), sodium pyrophosphate (5-10 mM), and β-glycerophosphate (10 mM) . For tissues, snap-freeze samples in liquid nitrogen immediately upon collection and maintain frozen state during homogenization . Consider using specialized phosphoprotein extraction kits designed to preserve phosphorylation status throughout the isolation process . When quantifying protein concentration, avoid phosphate-based assays (e.g., Bradford) that might interfere with phosphatase inhibitors . Store extracted proteins at -80°C with phosphatase inhibitors and minimize freeze-thaw cycles . Before SDS-PAGE separation, heat samples at 95°C for only 5 minutes, as extended boiling can lead to phosphate group hydrolysis . For complex samples with low abundance of phosphorylated Ezrin, consider enrichment strategies such as immunoprecipitation with total Ezrin antibodies followed by detection with Phospho-EZR (Tyr146) Antibody . Finally, process all experimental samples in parallel under identical conditions to minimize technical variation in phosphorylation preservation .

What are emerging applications of Phospho-EZR (Tyr146) Antibody in cytoskeletal dynamics research?

Recent advances in cytoskeletal research have expanded the applications of Phospho-EZR (Tyr146) Antibody beyond conventional techniques, opening new avenues for understanding Ezrin's role in dynamic cellular processes. Super-resolution microscopy techniques (STORM, PALM, SIM) combined with Phospho-EZR (Tyr146) immunolabeling now enable nanoscale visualization of phosphorylated Ezrin distribution at membrane-cytoskeleton interfaces, revealing previously undetectable spatial organizations . Researchers are increasingly using this antibody in live-cell phospho-sensors, where conformation-sensitive fluorescent proteins are integrated with Ezrin to allow real-time monitoring of Tyr146 phosphorylation dynamics during cellular processes like membrane ruffling, migration, and division . The antibody is proving valuable in organoid research, where 3D epithelial structures better recapitulate the physiological relevance of apical-basal polarity and Ezrin phosphorylation patterns than traditional 2D cultures . Microfluidic-based cellular migration assays coupled with Phospho-EZR (Tyr146) immunostaining are revealing how gradient-dependent Ezrin phosphorylation contributes to directional cell movement . In mechanobiology, researchers are using this antibody to investigate how mechanical forces trigger Ezrin phosphorylation at Tyr146 through mechanosensitive kinase activation, linking physical stimuli to cytoskeletal remodeling . These emerging applications are collectively enhancing our understanding of how site-specific phosphorylation of Ezrin at Tyr146 contributes to the spatiotemporal regulation of membrane-cytoskeleton interactions in diverse cellular contexts .

How might artificial intelligence and computational approaches enhance research utilizing Phospho-EZR (Tyr146) Antibody?

Artificial intelligence and computational approaches are transforming how researchers can utilize Phospho-EZR (Tyr146) Antibody data in several innovative ways. Machine learning algorithms are being developed to analyze Western blot images obtained with Phospho-EZR (Tyr146) Antibody, improving quantification accuracy and reducing subjective interpretation by automatically identifying specific bands and calculating intensity ratios relative to total Ezrin . Deep learning-based image analysis of immunofluorescence data can now segment and quantify subcellular localization patterns of phosphorylated Ezrin, tracking its redistribution under various experimental conditions with greater precision than traditional methods . Network modeling approaches integrate Phospho-EZR (Tyr146) Antibody data with protein-protein interaction databases to predict how Tyr146 phosphorylation alters Ezrin's interactome and signaling pathway engagement . Molecular dynamics simulations, informed by phosphorylation status detected by the antibody, can predict the three-dimensional conformational changes induced by Tyr146 phosphorylation and their impact on Ezrin's binding affinities for membrane proteins and actin . For experimental design, machine learning algorithms trained on published data can help researchers identify optimal experimental conditions for detecting Tyr146 phosphorylation in specific cell types . In multi-omics integration, computational tools can correlate Phospho-EZR (Tyr146) Antibody-derived data with transcriptomic, proteomic, and phenotypic datasets to reveal broader patterns of cellular regulation involving Ezrin . These computational approaches collectively enhance the extraction of biological insights from experimental data generated using Phospho-EZR (Tyr146) Antibody, accelerating discovery in cytoskeletal biology research .

What potential role does Ezrin Tyr146 phosphorylation play in pathological conditions and how can the antibody advance disease research?

Ezrin Tyr146 phosphorylation is emerging as a critical regulatory event in various pathological conditions, and Phospho-EZR (Tyr146) Antibody offers valuable tools for investigating these disease mechanisms. In cancer biology, aberrant phosphorylation of Ezrin at Tyr146 has been implicated in enhanced tumor cell migration, invasion, and metastatic potential, making this antibody valuable for stratifying tumors based on phosphorylation status and correlating with clinical outcomes . The antibody enables researchers to examine how altered tyrosine kinase activities in cancer cells affect Ezrin phosphorylation and subsequent cytoskeletal reorganization during metastatic progression . In inflammatory disorders, Ezrin phosphorylation at Tyr146 influences immune cell morphology, migration, and function, with the antibody helping to reveal how this modification is dysregulated during chronic inflammation . For infectious diseases, pathogens often manipulate host cytoskeletal components to facilitate invasion, with some bacteria and viruses specifically targeting Ezrin; the Phospho-EZR (Tyr146) Antibody can track these pathogen-induced phosphorylation changes . In neurodegenerative diseases, alterations in cytoskeletal dynamics contribute to pathogenesis, and the antibody can help investigate whether abnormal Ezrin phosphorylation plays a role in neuronal dysfunction . For therapeutic development, the antibody serves as an essential tool for screening compounds that modulate Ezrin phosphorylation, potentially identifying new drugs targeting cytoskeletal dynamics in various diseases . By systematically applying this antibody across different disease models and patient samples, researchers can build a comprehensive understanding of how Ezrin Tyr146 phosphorylation contributes to pathological processes and identify new therapeutic opportunities .