Zo 1 and zo 2

Manufactured by Cell Signaling Technology

ZO-1 and ZO-2 are proteins that are important for the formation and maintenance of tight junctions, which are specialized cell-cell adhesion complexes found in epithelial and endothelial cells. These proteins play a crucial role in regulating the permeability of cellular barriers and maintaining cellular polarity. ZO-1 and ZO-2 act as scaffolding proteins, linking transmembrane tight junction proteins to the actin cytoskeleton. They are commonly used as marker proteins for the identification and study of tight junctions in various experimental systems.

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Lab products found in correlation

Complete lysis buffer, by Merck Group (1 mentions) Claudin 5, by Cell Signaling Technology (1 mentions) Pan akt, by Cell Signaling Technology (1 mentions) Ser33 37 thr41β catenin, by Cell Signaling Technology (1 mentions) Anti β actin, by Merck Group (1 mentions) Dc protein assay, by Bio-Rad (1 mentions) Protease and phosphatase inhibitor cocktail, by Roche (1 mentions) Polyvinyldifluoridene membranes, by Merck Group (1 mentions) Caspase 3, by Cell Signaling Technology (1 mentions) Horseradish peroxidase linked anti rabbit or anti mouse secondary antibody, by Cell Signaling Technology (1 mentions) β actin, by Merck Group (1 mentions) Protease inhibitors cocktail, by Roche (1 mentions)

2 protocols using zo 1 and zo 2

Western Blot Analysis of Cell Signaling

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Cell lysates were prepared using complete lysis buffer (EMD Millipore, San Diego, CA) with protease and phosphatase inhibitor cocktails (Roche Diagnostics, Indianapolis, IN). Protein quantification was performed using Dc protein assay (Bio-Rad, Hercules, CA). Western blot analysis was performed as described previously.^{16 (link), 17 (link)} Antibodies used include Akt1, Akt2, Akt3, pan-Akt, ^Tyr216GSK-3β, ^{Ser33/37/Thr41}β-catenin, claudin-5, ZO-1 and ZO-2 (Cell Signaling) and anti-β-actin (Sigma). Densitometry was done using NIH Image J software.

Gao F., Alwhaibi A., Artham S., Verma A, & Somanath P.R. (2018). Endothelial Akt1 loss promotes prostate cancer metastasis via β-catenin-regulated tight-junction protein turnover. British Journal of Cancer, 118(11), 1464-1475.

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Protein Isolation and Western Blot Analysis

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Proteins were isolated with mammalian Protein Extraction Buffer (Pierce) containing a protease inhibitors cocktail (Roche Diagnostics). The lysates were centrifuged at 12,000 g for 10 min at 4°C, and then protein concentration was determined with BCA Protein Assay Kit (Pierce). Equivalent samples (20 μg protein) were subjected to sodium dodecyl sulfate–poly-acrylamide gel electrophoresis on 10% or 15% gel. After electrophoretic transfer to polyvinyldifluoridene membranes (Millipore and Bio-Rad), proteins were probed with caspase 3 (Cell Signaling Technology), ZO-1 and ZO-2 (Cell Signaling Technology), KGA and GAC (Dr. N. Curthoys, Colorado State University, Fort Collins, CO), or β-actin (Sigma-Aldrich) antibodies overnight at 4°C followed by a horseradish peroxidase-linked secondary anti-rabbit or anti-mouse antibody (Cell Signaling Technology). Antigen–antibody complexes were visualized by Pierce ECL Western Blotting Substrate (Pierce).

Liu F., Huang Y., Zhang F., Chen Q., Wu B., Rui W., Zheng J.C, & Ding W. (2015). Macrophages treated with particulate matter PM2.5 induce selective neurotoxicity through glutaminase-mediated glutamate generation. Journal of neurochemistry, 134(2), 315-326.

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