E-Cadherin (32A8) Mouse mAb

• 产品编号：CST-5296S      品牌：CST       原厂货号：5296S
• 产品分类：抗体 > 一抗 > 蛋白特异性一抗
• 应用分类：

描述：

E-Cadherin (32A8)鼠单抗可以识别内源性总的E-cadherin蛋白。用人癌症细胞系免疫动物获得单克隆抗体。E-Cadherin (32A8)鼠单抗可以识别E-cadherin细胞外区域的一个抗原表位。钙黏着糖蛋白属于跨膜糖蛋白超家族在细胞外区域包含由大约100个氨基酸残基组成的cadherin重复。钙黏着蛋白介导了钙离子依赖的细胞与细胞间粘着，并在正常组织发育过程中发挥重要作用（1）。经典的钙黏着蛋白超家族包括N-,P-,R-,B-和E-钙黏着蛋白和粘着连接中其他10个成员，粘着连接是一种极化上皮细胞顶端表面的细胞结构。经典粘着连接的细胞区域和β-catenin, γ-catenin（也叫桥粒斑珠蛋白）和p120catenin结合。β-catenin和 γ-catenin与α-catenin相互作用，α-catenin将钙黏着蛋白-catenin复合物与细胞骨架肌动蛋白丝结合（1,2）。当β-catenin和 γ-catenin在连接符合无踪发挥了结构性作用，p120发挥了钙黏着蛋白粘着和运输的功能（1-4）。E-钙黏着蛋白被认为是多种上皮细胞癌迁移和生长的激活型抑制因子（1-3）。最近的研究指出癌细胞会上调 N-钙黏着蛋白的表达并且下调E-钙黏着蛋白。钙黏着蛋白的表达变化被称为“钙粘着转化”。N-钙黏着蛋白与FGF受体，引起MMP-9的过表达和细胞侵润（3）。在内皮细胞中，VE-钙黏着蛋白信号传导，表达和定位与血管通透性和肿瘤学管发生相关（5,6）。在上皮细胞中正常出现的P-cadherin，在人卵巢癌和其他癌症中表达量也会发生变化（7,8）。

1. Wheelock, M.J. and Johnson, K.R. (2003) Annu Rev Cell Dev Biol 19, 207-35.
2. Christofori, G. (2003) EMBO J 22, 2318-23.
3. Hazan, R.B. et al. (2004) Ann N Y Acad Sci 1014, 155-63.
4. Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol 14, 427-34.
5. Rabascio, C. et al. (2004) Cancer Res 64, 4373-7.
6. Yamaoka-Tojo, M. et al. (2006) Arterioscler Thromb Vasc Biol 26, 1991-7.
7. Patel, I.S. et al. (2003) Int J Cancer 106, 172-7.
8. Sanders, D.S. et al. (2000) J Pathol 190, 526-30.

原厂资料：

Specificity / Sensitivity

E-Cadherin (32A8) Mouse mAb detects endogenous levels of total E-cadherin protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with human cancer cell lines. E-Cadherin (32A8) Mouse mAb recognizes an epitope in the extracellular region of E-cadherin.

Background

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 over-expression 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, 207-35.
2. Christofori, G. (2003) EMBO J 22, 2318-23.
3. Hazan, R.B. et al. (2004) Ann N Y Acad Sci 1014, 155-63.
4. Bryant, D.M. and Stow, J.L. (2004) Trends Cell Biol 14, 427-34.
5. Rabascio, C. et al. (2004) Cancer Res 64, 4373-7.
6. Yamaoka-Tojo, M. et al. (2006) Arterioscler Thromb Vasc Biol 26, 1991-7.
7. Patel, I.S. et al. (2003) Int J Cancer 106, 172-7.
8. Sanders, D.S. et al. (2000) J Pathol 190, 526-30.

注意事项：

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150
mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02%
sodium azide. Store at –20°C. Do not aliquot the antibody.