Figure 1. E-cadherin is detected by PathScan® Total E-Cadherin Sandwich ELISA Kit #7886. Lysates were prepared from various cell lines and analyzed for E-cadherin using PathScan® Total E-Cadherin Sandwich ELISA Kit #7886 or by western blotting. Absorbance readings at 450 nm are shown in the top figure while the corresponding western blot using an E-cadherin antibody is shown in the bottom figure.
Figure 2. The relationship between the protein concentration of the lysate from A431 and Jurkat cells and the absorbance at 450 nm is shown.
The PathScan® Total E-Cadherin Sandwich ELISA Kit #7886 is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of E-cadherin. An E-cadherin mouse antibody has been coated onto the microwells. After incubation with cell lysates, E-cadherin is captured by the coated antibody. Following extensive washing, an E-Cadherin rabbit detection antibody is added to detect the captured E-cadherin. Anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of the absorbance for this developed color is proportional to the quantity of E-cadherin.
Antibodies in kit are custom formulations specific to kit.
CST's PathScan® Total E-Cadherin Sandwich ELISA Kit #7886 detects endogenous levels of E-cadherin. As shown in Figure 1, using the Total E-Cadherin Sandwich ELISA Kit #7886, a high level of E-cadherin is detected in A431 and MCF-7 cells, but not in E-cadherin null Jurkat cells. The PathScan® Total E-Cadherin Sandwich ELISA Kit #7886 does not cross-react with human N-, P- or VE-cadherin. This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
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 upregulated 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).
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