R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
ZO-1 (D6L1E) Rabbit mAb #13663
Filter:
- WB
- IP
- IF
Supporting Data
REACTIVITY | H Mk |
SENSITIVITY | Endogenous |
MW (kDa) | 220 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
- Mk-Monkey
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunoprecipitation | 1:50 |
Immunofluorescence (Immunocytochemistry) | 1:100 - 1:200 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
ZO-1 (D6L1E) Rabbit mAb recognizes endogenous levels of total ZO-1 protein.
Species Reactivity:
Human, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala1558 of human ZO-1 protein.
Background
Tight junctions, or zona occludens (ZO), 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). 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 ZO-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).
- 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.
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For Research Use Only. Not For Use In Diagnostic Procedures.
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