Product Pathways - Cytoskeletal Signaling
ZO-3 (D57G7) XP® Rabbit mAb #3704
|3704S||100 µl (10 western blots)||---||In Stock||---|
|3704P||40 µl (4 western blots)||---||In Stock||---|
|3704||carrier free and custom formulation / quantity||email request|
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Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry)
Specificity / Sensitivity
ZO-3 (D57G7) XP® Rabbit mAb detects endogenous levels of total ZO-3 protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to carboxy-terminal residues of human ZO-3.
Western blot analysis of extracts from MCF-7, HT-29 and HCT-15 cells using ZO-3 (D57G7) XP® Rabbit mAb.
Tight junctions, or zona occludens, form a continuous barrier to fluids across the epithelium and endothelium. They function in regulation of paracellular permeability and in the maintenance of cell polarity, blocking the movement of transmembrane proteins between the apical and the basolateral cell surfaces (reviewed in 1). Zona occludens proteins ZO-1, -2, and -3 (also known as TJP1, 2, and 3) are peripheral membrane adaptor proteins that link junctional transmembrane proteins such as occludin and claudin to the actin cytoskeleton (reviewed in 2). ZO-1 and -2 are required for tight junction formation and function (3,4). In subconfluent proliferating cells, ZO-1 and ZO-2 have been shown to colocalize to the nucleus and play a role in transcriptional regulation, possibly through facilitating nuclear import/export of transcriptional regulators (5-7). The ZO-2 gene is transcribed from two promoters, generating the ZO-2A and ZO-2C isoforms. ZO-2C lacks a 23 amino acid amino-terminal sequence found in other ZO-2 isoforms. While both isoforms appear to be widely expressed, abnormal regulation of the ZO-2 gene may be correlated with development of ductal cancer (8).
Exogenous expression of the amino terminal portion of ZO-3 exerts a dominant negative effect that interferes with assembly of tight junctions and adherens junctions (9). However, additional evidence indicates that tight junctions do form in the absence of ZO-3 protein (10), and that mice lacking ZO-3 appear to develop normally (11).
- Shin, K. et al. (2006) Annu Rev Cell Dev Biol 22, 207-35.
- Matter, K. and Balda, M.S. (2007) J Cell Sci 120, 1505-11.
- Hernandez, S. et al. (2007) Exp Cell Res 313, 1533-47.
- Umeda, K. et al. (2006) Cell 126, 741-54.
- Betanzos, A. et al. (2004) Exp Cell Res 292, 51-66.
- Traweger, A. et al. (2003) J Biol Chem 278, 2692-700.
- Huerta, M. et al. (2007) Mol Biol Cell 18, 4826-36.
- Chlenski, A. et al. (2000) Biochim Biophys Acta 1493, 319-24.
- Wittchen, E.S. et al. (2000) J Cell Biol 151, 825-36.
- Adachi, M. et al. (2006) Mol Cell Biol 26, 9003-15.
- Xu, J. et al. (2008) Mol Cell Biol 28, 1669-78.
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For Research Use Only. Not For Use In Diagnostic Procedures.
XP® is a trademark of Cell Signaling Technology, Inc.
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Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.