E-Cadherin (24E10) Rabbit mAb (Biotinylated)Product information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Adhesion
E-Cadherin (24E10) Rabbit mAb (Biotinylated) #8834
|8834S||100 µl (10 western blots)||---||In Stock||---|
|8834||carrier free and custom formulation / quantity||email request|
|W||1:1000||Human, Mouse||Endogenous||135||Rabbit IgG|
Species cross-reactivity is determined by western blot using the unconjugated antibody.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Bovine, Dog, Pig.
Specificity / Sensitivity
E-Cadherin (24E10) Rabbit mAb (Biotinylated) detects endogenous levels of total E-cadherin protein. The antibody does not cross-react with related family members, such as N-cadherin.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the sequence surrounding Pro780 of human E-cadherin protein.
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated E-Cadherin (24E10) Rabbit mAb #3195.
Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have up-regulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch". N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).
- Wheelock, M.J. and Johnson, K.R. (2003) Annu Rev Cell Dev Biol 19, 207-35.
- Christofori, G. (2003) EMBO J 22, 2318-23.
- Hazan, R.B. et al. (2004) Ann N Y Acad Sci 1014, 155-63.
- Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol 14, 427-34.
- Rabascio, C. et al. (2004) Cancer Res 64, 4373-7.
- Yamaoka-Tojo, M. et al. (2006) Arterioscler Thromb Vasc Biol 26, 1991-7.
- Patel, I.S. et al. (2003) Int J Cancer 106, 172-7.
- Sanders, D.S. et al. (2000) J Pathol 190, 526-30.
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This product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.
Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.