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Western blot analysis of α-Catenin on a human endothelial cell lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of the anti- α-Catenin antibody.
Immunofluorescence staining of HeLa cells.
BD Transduction Laboratories™ Purified Mouse Anti- α-Catenin
BD Transduction Laboratories™ Purified Mouse Anti- α-Catenin
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
The catenins (α-, β-, and γ-) are cytoplasmic proteins that bind to the highly conserved cytoplasmic tail of E-Cadherin. The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions (zonula adherens). These junctions are critical for cell-cell adhesion, signal transmission between neighboring cells, and for the anchoring of the actin cytoskeleton. α-Catenin (CAP102) shows homology to vinculin, while β-Catenin is similar to plakoglobin or the Drosophila armadillo gene product. α-Catenin was identified as an E-Cadherin-associated protein, however, it also appears to interact with other cadherin family members. There are at least two subtypes of α-Catenin: αE-Catenin and αN-Catenin. The predominant form is known as αE-Catenin. It is ubiquitously expressed, but at low levels in the nervous system. The expression of αN-Catenin is more restricted and this form predominates in the brain. Increased tyrosine phosphorylation of adherens junction proteins can disrupt catenin-cadherin complexes, leading to changes in cell adhesion properties. It has been noted that down-regulation of this group of proteins often precedes metastasis. In fact, data suggests a correlation between deletions within the α-Catenin gene and the development of prostate cancer.
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 (5)
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Baki L, Marambaud P, Efthimiopoulos S, et al. Presenilin-1 binds cytoplasmic epithelial cadherin, inhibits cadherin/p120 association, and regulates stability and function of the cadherin/catenin adhesion complex. Proc Natl Acad Sci U S A. 2001; 98(5):2381-2386. (Biology: Immunoprecipitation, Western blot). View Reference
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Giannini AL, Vivanco M, Kypta RM. alpha-catenin inhibits beta-catenin signaling by preventing formation of a beta-catenin*T-cell factor*DNA complex. J Biol Chem. 2000; 275(29):21883-21888. (Biology: Immunofluorescence). View Reference
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Herrenknecht K, Ozawa M, Eckerskorn C, Lottspeich F, Lenter M, Kemler R. The uvomorulin-anchorage protein alpha catenin is a vinculin homologue. Proc Natl Acad Sci U S A. 1991; 88(20):9156-9160. (Biology). View Reference
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Hirano S, Kimoto N, Shimoyama Y, Hirohashi S, Takeichi M. Identification of a neural alpha-catenin as a key regulator of cadherin function and multicellular organization. Cell. 1992; 70(2):293-301. (Biology). View Reference
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Huan Y, van Adelsberg J. Polycystin-1, the PKD1 gene product, is in a complex containing E-cadherin and the catenins. J Clin Invest. 1999; 104(10):1459-1468. (Biology: Immunohistochemistry, Western blot). View Reference
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For Research Use Only. Not for use in diagnostic or therapeutic procedures.