Human Recombinant EZR protein, His Tag (V2LY-0526-LY3978)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant EZR protein, His Tag consist of Amino Acid: 2-586 and predicts a molecular mass of 71.2 kDa.
Molecule Mass
71.2 kDa
Sequence
Amino Acid: 2-586
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>60% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.
More Infomation

Target

Full Name
ezrin
Research Area
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.
Biological Process
Actin cytoskeleton reorganization Source: UniProtKB
Actin filament bundle assembly Source: UniProtKB
Astral microtubule organization Source: UniProtKB
Cellular protein-containing complex localization Source: UniProtKB
Cellular response to cAMP Source: UniProtKB
Cortical microtubule organization Source: UniProtKB
Establishment of centrosome localization Source: UniProtKB
Establishment of endothelial barrier Source: UniProtKB
Establishment or maintenance of apical/basal cell polarity Source: Ensembl
Filopodium assembly Source: UniProtKB
Intestinal D-glucose absorption Source: Ensembl
Leukocyte cell-cell adhesion Source: BHF-UCL
Membrane to membrane docking Source: BHF-UCL
Microvillus assembly Source: UniProtKB
Negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
Negative regulation of interleukin-2 production Source: UniProtKB
Negative regulation of p38MAPK cascade Source: UniProtKB
Negative regulation of T cell receptor signaling pathway Source: UniProtKB
Negative regulation of transcription by RNA polymerase II Source: UniProtKB
Phosphatidylinositol-mediated signaling Source: UniProtKB
Positive regulation of cellular protein catabolic process Source: UniProtKB
Positive regulation of early endosome to late endosome transport Source: UniProtKB
Positive regulation of gene expression Source: UniProtKB
Positive regulation of multicellular organism growth Source: Ensembl
Positive regulation of protein localization to early endosome Source: UniProtKB
Positive regulation of protein localization to plasma membrane Source: Ensembl
Positive regulation of protein secretion Source: UniProtKB
Protein kinase A signaling Source: UniProtKB
Protein localization to cell cortex Source: UniProtKB
Protein localization to plasma membrane Source: UniProtKB
Receptor internalization Source: Ensembl
Regulation of cell shape Source: UniProtKB
Regulation of microvillus length Source: Ensembl
Regulation of organelle assembly Source: UniProtKB
Sphingosine-1-phosphate receptor signaling pathway Source: UniProtKB
Terminal web assembly Source: Ensembl
Cellular Location
Cytoskeleton; Apical cell membrane; Microvillus membrane; Ruffle membrane; Cell projection; Cell cortex; Microvillus. Localization to the apical membrane of parietal cells depends on the interaction with PALS1. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side).
PTM
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.

Lipreri da Silva, J. C., Carvalho, M. F. L., de Miranda, L. B. L., de Almeida, B. O., Lima, K., & Machado-Neto, J. A. (2022). NSC305787, a pharmacological ezrin inhibitor, exhibits antineoplastic activity in pancreatic cancer cells. Investigational New Drugs, 1-10.

da Silva, J. C. L., Carvalho, M. F. L., de Miranda, L. B. L., de Almeida, B. O., Lima, K., & Machado-Neto, J. A. (2022). NSC305787, a pharmacological ezrin inhibitor, exhibits antineoplastic activity in pancreatic cancer cells. Investigational new drugs, 40(4), 728-737.

Lipreri da Silva, J. C., Coelho-Silva, J. L., Lima, K., Vicari, H. P., Lazarini, M., Costa-Lotufo, L. V., ... & Machado-Neto, J. A. (2021). Comprehensive analysis of cytoskeleton regulatory genes identifies ezrin as a prognostic marker and molecular target in acute myeloid leukemia. Cellular Oncology, 44(5), 1105-1117.

Fan, C., Qu, H., Xiong, F., Tang, Y., Tang, T., Zhang, L., ... & Zeng, Z. (2021). CircARHGAP12 promotes nasopharyngeal carcinoma migration and invasion via ezrin-mediated cytoskeletal remodeling. Cancer Letters, 496, 41-56.

Qureshi-Baig, K., Kuhn, D., Viry, E., Pozdeev, V. I., Schmitz, M., Rodriguez, F., ... & Letellier, E. (2020). Hypoxia-induced autophagy drives colorectal cancer initiation and progression by activating the PRKC/PKC-EZR (ezrin) pathway. Autophagy, 16(8), 1436-1452.

Chang, Y. T., Peng, H. Y., Hu, C. M., Huang, S. C., Tien, S. C., & Jeng, Y. M. (2020). Pancreatic cancer-derived small extracellular vesical Ezrin regulates macrophage polarization and promotes metastasis. American Journal of Cancer Research, 10(1), 12.

Yano, K., Okabe, C., Fujii, K., Kato, Y., & Ogihara, T. (2020). Regulation of breast cancer resistance protein and P-glycoprotein by ezrin, radixin and moesin in lung, intestinal and renal cancer cell lines. Journal of Pharmacy and Pharmacology, 72(4), 575-582.

Zhang, R., Zhang, S., Xing, R., & Zhang, Q. (2019). High expression of EZR (ezrin) gene is correlated with the poor overall survival of breast cancer patients. Thoracic cancer, 10(10), 1953-1961.

Ye, D. J., Kwon, Y. J., Baek, H. S., Shin, S., Lee, C., Yun, J. W., ... & Chun, Y. J. (2018). Discovery of ezrin expression as a potential biomarker for chemically induced ocular irritation using human corneal epithelium cell line and a reconstructed human cornea-like epithelium model. Toxicological Sciences, 165(2), 335-346.

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For research use only. Not intended for any clinical use.

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