Cell Signaling Technology

Product Pathways - Adhesion

ZO-2 Antibody #2847

Applications Reactivity Sensitivity MW (kDa) Source
W IF-IC H M R Mk B Dg Endogenous 150 Rabbit

Applications Key:  W=Western Blotting  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey  B=Bovine  Dg=Dog
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

ZO-2 Antibody recognizes endogenous levels of total ZO-2 protein. The antibody does not cross-react with ZO-1 or ZO-3.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy-terminal sequence of mouse ZO-2.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell types using ZO-2 Antibody.

IF-IC

IF-IC

Confocal immunofluorescent analysis of A431 cells using ZO-2 Antibody (green). Actin filaments have been labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).

Background

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).

  1. Shin, K. et al. (2006) Annu Rev Cell Dev Biol 22, 207-35.
  2. Matter, K. and Balda, M.S. (2007) J Cell Sci 120, 1505-11.
  3. Hernandez, S. et al. (2007) Exp Cell Res 313, 1533-47.
  4. Umeda, K. et al. (2006) Cell 126, 741-54.
  5. Betanzos, A. et al. (2004) Exp Cell Res 292, 51-66.
  6. Traweger, A. et al. (2003) J Biol Chem 278, 2692-700.
  7. Huerta, M. et al. (2007) Mol Biol Cell 18, 4826-36.
  8. Chlenski, A. et al. (2000) Biochim Biophys Acta 1493, 319-24.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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