Product Pathways - Adhesion
P-Cadherin Antibody #2130
|W IP IF-IC F||H||Endogenous||120||Rabbit|
Reactivity Key: H=Human
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
P-Cadherin Antibody recognizes endogenous levels of total P-cadherin protein. The antibody does not cross-react with other cadherin family members.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to human P-cadherin. Antibodies are purified using protein A and peptide affinity chromatography.
Western blot anlaysis of extracts from A431, Panc1 and HUVE cells, using P-Cadherin Antibody.
Immunofluorescent analysis of A431 cells, using P-Cadherin Antibody (left). Nuclei in the same cells were stained with DAPI (right).
Confocal immunofluorescent images of A431 cells labeled with P-Cadherin Antibody (green, left) compared to an isotype control (right). Actin filaments have been labeled with Alexa Fluor® 555 phalloidin (red). Blue pseudocolor = DRAQ® #4084 (fluorescent DNA dye).
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). 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). 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, 207-235.
- 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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For Research Use Only. Not For Use In Diagnostic Procedures.