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Western blot analysis of β-Catenin on HeLa cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of the Mouse Anti- β-Catenin antibody.
Immunofluorescent staining of A431 cell line with the Anti- β-Catenin antibody.
BD Transduction Laboratories™ Purified Mouse Anti-β-Catenin
BD Transduction Laboratories™ Purified Mouse Anti-β-Catenin
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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.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- 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.
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関連製品
The 14/Beta-Catenin monoclonal antibody specifically binds to Beta-Catenin (β-Catenin). β-Catenin is a 92 kDa protein that binds to the cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions (zonula adherens). Deletions in the cytoplasmic domain of E-Cadherin which eliminate catenin binding also result in a loss of cell adhesion, indicating that this binding is essential for E-Cadherin function. Although the α- and β-Catenins have been cloned, very little is known about their biochemical roles. However a link between β-Catenin and colon cancer has been described. β-Catenin was found to co-immunoprecipitate with the APC tumor suppressor protein in human colorectal tumor cell lines, as well as in human kidney 293 cells. E-Cadherin, however, was not detectable in these complexes. Thus the APC-Catenin complex may be affecting the transmission of contact inhibition signals and/or the regulation of cell adhesion.
Development References (6)
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Eger A, Stockinger A, Schaffhauser B, Beug H, Foisner R. Epithelial mesenchymal transition by c-Fos estrogen receptor activation involves nuclear translocation of beta-catenin and upregulation of beta-catenin/lymphoid enhancer binding factor-1 transcriptional activity. J Cell Biol. 2000; 148(1):173-187. (Clone-specific: Electron microscopy, Immunofluorescence, Immunoprecipitation, Western blot). View Reference
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Fallone F, Britton S, Nieto L, Salles B, Muller C. ATR controls cellular adaptation to hypoxia through positive regulation of hypoxia-inducible factor 1 (HIF-1) expression. Oncogene. 2013; 32(37):4387-4396. (Clone-specific: Western blot). View Reference
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Lee MS, D'Amour KA, Papkoff J. A yeast model system for functional analysis of beta-catenin signaling. J Cell Biol. 2002; 158(6):1067-1078. (Clone-specific: Immunofluorescence, Immunoprecipitation, Western blot). View Reference
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Ozawa M, Ringwald M, Kemler R. Uvomorulin-catenin complex formation is regulated by a specific domain in the cytoplasmic region of the cell adhesion molecule. Proc Natl Acad Sci U S A. 1990; 87(11):4246-4250. (Biology). View Reference
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Persad S, Troussard AA, McPhee TR, Mulholland DJ, Dedhar S. Tumor suppressor PTEN inhibits nuclear accumulation of beta-catenin and T cell/lymphoid enhancer factor 1-mediated transcriptional activation. J Cell Biol. 2001; 153(6):1161-1173. (Clone-specific: Gel shift, Immunofluorescence, Immunoprecipitation, Western blot). View Reference
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Tateishi K, Omata M, Tanaka K, Chiba T. The NEDD8 system is essential for cell cycle progression and morphogenetic pathway in mice. J Cell Biol. 2001; 155(4):571-579. (Clone-specific: Immunofluorescence, Immunohistochemistry). View Reference
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