Pan-Cadherin Antibody

4068:

IHC / Paraffin , Immunoprecipitation , Western Blotting

Pan-Cadherin Antibody detects endogenous levels of E-, P-, N-, R-, VE-, and K-Cadherins.

Polyclonal antibodies are produced by immunizing animals with two synthetic peptides corresponding to two conserved regions of human N-Cadherin. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western blot analysis of extracts from A431, MCF-7, C2C12, HUVEC, BAEC, NIH/3T3, C6, H-4-II-E, Cos and PC3 cells, using Pan-Cadherin Antibody.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human breast carcinoma, using Pan-cadherin Antibody.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human bronchioalveolar cell carcinoma using Pan-cadherin Antibody, showing membrane localization.

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human prostate carcinoma, using Pan-cadherin Antibody.

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). 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 overexpression of MMP-9 and cellular invasion (3). In endothelial cells, VE-cadherin signaling, expression, and localization correlate 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).

1. Wheelock, M.J. and Johnson, K.R. (2003) Annu. Rev. Cell. Dev. Biol. 19, 207-235.
2. Christofori, G. (2003) EMBO J. 22, 2318-2323.
3. Hazan, R.B. et al. (2004) Ann. NY Acad. Sci. 1014, 155-163.
4. Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol. 14, 427-434.
5. Rabascio, C. et al. (2004) Cancer Res. 64, 4373-4377.
6. Yamaoka-Tojo, M. et al. (2006) Arterioscler. Thromb. Vasc. Biol. 26, 1991-1997.
7. Patel, I.S. et al. (2003) Int. J. Cancer 106, 172-177.
8. Sanders, D.S. et al. (2000) J. Pathol. 190, 526-530.

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For Research Use Only. Not For Use In Diagnostic Procedures.