E-Cadherin Blocking Peptide #1056
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Description
This peptide is used to block E-Cadherin (24E10) Rabbit mAb #3195 reactivity, as well as E-Cadherin Antibody #4065.
Quality Control
The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks E-Cadherin (24E10) Rabbit mAb #3195 and E-Cadherin Antibody #4065 by immunohistochemistry.
IHC-P (paraffin)
Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using E-Cadherin (24E10) Rabbit mAb #3195 in the presence of control peptide (left) or E-Cadherin Blocking Peptide (right).
Applications
Use as a blocking reagent to evaluate the specificity of antibody reactivity in immunohistochemistry protocols.
Directions for Use
For immunohistochemistry, add twice the volume of peptide as volume of antibody used in 100 µl total volume. Incubate for a minimum of 30 minutes prior to adding the entire volume to the slide. Recommended antibody dilutions can be found on the relevant product data sheet.
BackgroundCadherins 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 which 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). Unlike β- and γ-catenin, p120 regulates cadherin adhesive activity and trafficking rather than having a structural role in the junctional complex (1-4). E-cadherin is considered an active suppressor of invasion and growth of many epithelial cancers (1-3). Recent 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 over-expression of MMP-9 and cellular invasion (3). In endothelial cells, VE-cadherin signaling, expression and localization are correlated with vascular permeability and tumor angiogenesis (5,6). 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, 207-235.
- Christofori, G. (2003) EMBO J. 22, 2318-2323.
- Hazan, R.B. et al. (2004) Ann. NY Acad. Sci. 1014, 155-163.
- Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol. 14, 427-434.
- Rabascio, C. et al. (2004) Cancer Res. 64, 4373-4377.
- Yamaoka-Tojo, M. et al. (2006) Arterioscler. Thromb. Vasc. Biol. 26, 1991-1997.
- Patel, I.S. et al. (2003) Int. J. Cancer 106, 172-177.
- Sanders, D.S. et al. (2000) J. Pathol. 190, 526-530.
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Companion ProductsThis product is intended for research purposes only. The product is not intended to be used for therapeutic or diagnostic purposes in humans or animals.