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Western blot analysis of ZO-1 on a HeLa cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti- ZO-1 antibody.
Immunofluorescent staining of EAHY human endothelial cells.
BD Transduction Laboratories™ Purified Mouse Anti-Human ZO-1
BD Transduction Laboratories™ Purified Mouse Anti-Human ZO-1
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Companion Products
Tight junctions (zonulae occludens) are critical to the maintenance of cell polarity and intracellular barriers between epithelial and endothelial cells. Protein components of the tight junctions include actin filaments, symplekin, occludin, Rab3B, AF-6, 7H6, ZO-1, and ZO-2. Analysis of ZO-1 and -2 resulted in their inclusion in the MAGUK protein family. This family also includes the discs large tumor suppressor protein (Dlg-A) of Drosophila; p55, an erythrocyte membrane protein; and PSD-95/SAP90, a synaptic membrane protein. All family members contain a region homologous to guanylate kinase (GuK), a src homology (SH3) domain, and multiple PDZ domains. Through these elements, MAGUK proteins function in signal transduction and, possibly, tumor suppression. ZO-1 is a peripheral membrane phosphoprotein that binds to other tight junction proteins such as occludin and AF-6. Via its SH3 domain, ZO-1 interacts with a serine protein kinase that phosphorylates a region immediately C-terminal of the SH3 domain. Taken together, these data indicate that ZO-1 is a critical element in the formation of tight junctions and may also serve an important role in signaling and tumor suppression.
This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
Development References (4)
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Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D. Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J Biol Chem. 2000; 275(36):27979-27988. (Clone-specific: Western blot). View Reference
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Hirase T, Kawashima S, Wong EY, et al. Regulation of tight junction permeability and occludin phosphorylation by Rhoa-p160ROCK-dependent and -independent mechanisms. J Biol Chem. 2001; 276(13):10423-10431. (Clone-specific: Western blot). View Reference
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Nix SL, Chishti AH, Anderson JM, Walther Z. hCASK and hDlg associate in epithelia, and their src homology 3 and guanylate kinase domains participate in both intramolecular and intermolecular interactions. J Biol Chem. 2000; 275(52):41192-41200. (Clone-specific: Immunoprecipitation). View Reference
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Willott E, Balda MS, Fanning AS, Jameson B, Van Itallie C, Anderson JM. The tight junction protein ZO-1 is homologous to the Drosophila discs-large tumor suppressor protein of septate junctions. Proc Natl Acad Sci U S A. 1993; 90(16):7834-7838. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
Refer to manufacturer's instructions for use and related User Manuals and Technical Data Sheets before using this product as described.
Comparisons, where applicable, are made against older BD technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.