Recombinant Human Ezrin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1946

Recombinant Human Ezrin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1946
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His
Host Species Human
Accession P15311
Synonym CVIL, CVL, HEL-S-105, VIL2
Background VIL2, also known as villin-2, belongs to the ERM protein family. It is expressed in cerebral cortex, basal ganglia, hippocampus, hypophysis, and optic nerve. VIL2 contains 1 FERM domain and may be involved in connections of major cytoskel
Description A DNA sequence encoding the mature form of human EZR (P15311) (Pro2-Leu586) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal His
AA Sequence Pro2-Leu586
Molecular Weight The recombinant human EZR consists of 601 a.a. and predicts a molecular mass of 71.2 KDa. It migrates as an approximately 82 KDa band in SDS-PAGE under reducing conditions.
Purity >60% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS 100mM Arg 10% glycerol, 0.1% Twen 20, pH 7.5.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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.
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.
Database References
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

Gene Functions References

  1. detection of Ezrin and E-cadherin expression in cervical smears, could be a potential prognostic marker for identifying cervical lesions with high-risk of progression to invasive cervical cancer, and may help on the selection of an appropriate therapy or avoid unnecessary treatment PMID: 29587669
  2. Ezrin and myosin II play critical roles in enhancing line tension by promoting the formation of an actomyosin ring. PMID: 28643776
  3. these findings suggest that baicalein inhibits the proliferation, migration and invasion and induces apoptosis in Osteosarcoma (OS) cells by activating the miR183/Ezrin pathway, revealing a novel mechanism underlying antiOS effects of baicalein. PMID: 29845278
  4. Ezrin-anchored PKA phosphorylates serine 369 and 373 on connexin 43 to enhance gap junction assembly, communication, and cell fusion. PMID: 29259079
  5. High Ezrin expression is associated with osteosarcoma. PMID: 29656060
  6. L1CAM promotes esophageal squamous cell carcinoma tumorigenicity by upregulating ezrin expression. PMID: 28939985
  7. This is the first study to verify the relationship of the expression of RhoA and Ezrin proteins in vaginal tissue of Postmenopausal atrophic vagina. PMID: 28843271
  8. ezrin facilitates AQP2 endocytosis, thus linking the dynamic actin cytoskeleton network with AQP2 trafficking. PMID: 28754689
  9. FUT4/LeY was critical to the TAMs-mediated EMT; this process might be associated with the up-regulation of Ezrin phosphorylation by FUT4/LeY-mediated fucosylation PMID: 28423676
  10. CPI-17 drives Ras activity and tumorigenesis in melanomas in a two-fold way; inactivation of the tumor suppressor merlin and activation of the growth promoting ERM family. PMID: 27793041
  11. Data suggest that EGF induces colorectal cancer cells to undergo epithelial-mesenchymal transition, enhances their ability to invade/migrate, and promotes phosphorylation of Ezrin at Tyr353. (EGF = epidermal growth factor) PMID: 28535417
  12. Binding of phosphatidylinositol 4,5-biphosphate to ezrin induces a conformational change permitting the insertion of the LOK C-terminal domain to wedge apart the membrane and F-actin-binding domains of ezrin. The N-terminal LOK kinase domain can then access a site 40 residues distal from the consensus sequence that collectively direct phosphorylation of the appropriate threonine residue. PMID: 28430576
  13. The expression pattern and subcellular localization of ezrin and moesin correlate with clinicopathological variables such as patients' age, tumor grade and hormonal status. PMID: 28624994
  14. Ezrin represents a promising target for the development of strategies aimed at preventing the progression of cervical cancer. PMID: 26933912
  15. Ezrin S66 phosphorylation enhances filopodia formation, contributing to the regulation of invasion and metastasis of esophageal squamous cell carcinoma cells PMID: 28504189
  16. The results reveal a supportive role of ERMs in cortical activities during cytokinesis, and also provide insight into the selective mechanism that preferentially associates cytokinesis-relevant proteins with the division site. PMID: 28889652
  17. Ezrin protein expression is a promising biomarker in estimating the outcome of stage II colorectal cancer patients. When combined with microsatellite status its ability in predicting disease outcome is further improved PMID: 28953975
  18. Ezrin is down-regulated during cholangiocarcinogenesis, and its loss results in a more aggressive phenotype. PMID: 26791814
  19. A signature of ezrin-interacting proteins accurately predicts esophageal squamous cell carcinoma patient survival or tumor recurrence. PMID: 28603065
  20. The results of this meta-analysis suggest that ezrin positive immunoexpression confers a higher risk of recurrence and a worse survival in osteosarcoma patients. PMID: 23805177
  21. PM blebbing triggered SRF-mediated up-regulation of the metastasis-associated ERM protein Ezrin. Notably, Ezrin is sufficient and important to sustain bleb dynamics for cell-in-cell invasion when SRF is suppressed. PMID: 28774893
  22. EZR is a novel biomarker in terms of invasion among the 3 subtypes of NFPAs, and it is a promising guide for therapeutic decision making as well. PMID: 28093347
  23. Increased ezrin and HER2 expression in patients with salivary gland carcinomas represents a high-grade histopathological subtype. PMID: 28300573
  24. SMYD3 enhances tumorigenicity in esophageal squamous cell carcinoma by enhancing transcription of ezrin and LOXL2, which are involved in proliferation, migration, and invasion. PMID: 26980013
  25. 3-dimensional cell cultures were found to mimic different tumor sites and be applicable as a model. The in vitro results concur with the clinical specimen analysis, suggesting that in ovarian carcinoma, the role of ezrin in disease progression is more pronounced than that of p130Cas. PMID: 27622508
  26. The expression of ezrin was up-regulated and significantly associated with the stage, lymph node involvement and distant metastasis PMID: 28261953
  27. there were significant decreases in intercellular adhesion molecules 1 (ICAM1), ezrin (EZR), mitogen-activated protein kinase kinase 2 (MAP2K2), and nitric oxide synthase 3 (NOS3) gene expressions in metabolic syndrome patients. PMID: 26956845
  28. Immunohistochemistry staining for ezrin, was similar in AFX and UPS tumors. PMID: 28079637
  29. Ezrin and HER2/neu are overexpressed and coexpressed in osteosarcoma with adverse prognostic features such as high grade. Therefore, ezrin and HER2/neu could be potential prognostic markers and treatment targets for osteosarcoma PMID: 26067138
  30. Study indicates the usual relationship between estrogen and ezrin induction is abridged. Study suggests that changes in ezrin may be associated with the development of the invasive phenotype and penetration of the basement membrane. PMID: 27688241
  31. The present study showed over-expression of ezrin and moesin in colorectal carcinoma PMID: 27042764
  32. study indicates that the presence of autoantibodies against Ezrin is significantly associated with ESCC PMID: 28298808
  33. Ezrin protein is highly expressed in human PHC tissue which can be used for the prediction of metastasis disease. PMID: 28230040
  34. results show that the activation of the ezrin-pAkt signaling axis is associated with the more aggressive clinicopathological features of PPA compared with LPA PMID: 27059464
  35. Ezrin and p65 interactions in MDA-MB-231 cells were confirmed using co-immunoprecipitation. PMID: 27420986
  36. the distribution of NHERF1 in ovarian cancer and reveals a different regulation of NHERF1 and EZRIN expression in ovarian tumors which represents the complexity of the molecular changes of this disease PMID: 27823775
  37. Phosphorylation of ezrin together with its binding to phosphatidylinositol-4,5-bisphosphate tethers the F508del CFTR to the actin cytoskeleton, stabilizing it on the apical membrane and rescuing the sub-membrane compartmentalization of cAMP and activated PKA. PMID: 26823603
  38. Data show that gene silence of ezrin inhibits the proliferation and invasion of prostate cancer PC-3 cells, meanwhile the level of E-cadherin is upregulated and N-cadherin is downregulated. PMID: 27371852
  39. Knockdown of ezrin in HUVECs significantly induced the morphogenetic changes and cytoskeletal reorganization of the transfected cells, and also reduced cell migration and angiogenesis capacity in vitro. PMID: 27072970
  40. High EZRIN expression is associated with prostate cancer. PMID: 26799186
  41. Elevated Ezrin expression is associated with a poor prognosis in a variety of solid tumors. PMID: 26632332
  42. These findings suggest that ezrin-EGFR interaction augments oncogenic functions of EGFR and that targeting ezrin may provide a potential novel approach to overcome erlotinib resistance in non-small cell lung cancer cells PMID: 26936397
  43. The value of ezrin expression as a prognostic biomarker is further consolidated in urothelial cancer. PMID: 25278252
  44. Suggest a role for ezrin in advanced glycation end product-induced podocyte damage. PMID: 26032400
  45. Phospho-Ezrin/Radixin/Moesin (ERM) inhibit cell adhesion, and therefore, dephosphorylation of ERM proteins is essential for cell adhesion.Phospho-ERM induce formation and/or maintenance of spherical cell shape. PMID: 26555866
  46. Activation of liver PKCs during cholestasis leads to Ezrin Thr567 phosphorylation resulting in MRP2 internalization and degradation where ubiquitin ligase E3 GP78 is involved. PMID: 26212029
  47. Data indicate that a quinoline-based small molecule, NSC305787, directly binds to ezrin and inhibits its functions. PMID: 26358752
  48. We identified and confirmed that Fra-1 affected the expression level of CTTN and EZR in vitro through LC-MS/MS analyses and western blot technology. PMID: 26330014
  49. Data show that both Ezrin and SIX1 proteins are highly expressed in alpha fetoprotein-negative hepatocellular carcinoma (HCC) and significantly related with the TNM stage. PMID: 26927385
  50. it was found that expression of miR-96 was negatively correlated with the metastatic ability of renal cell carcinoma, and that downregulation of miR-96 could suppress the invasion of renal cancer cell via downregulation of Ezrin expression. PMID: 26419932


Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed