Phospho-α-E-Catenin (Ser652) Antibody

• 产品编号：CST-13061S      品牌：CST       原厂货号：13061S
• 产品分类：抗体 > 一抗 > 磷酸化抗体
• 应用分类：

描述：

Phospho-α-E-Catenin (Ser652) Antibody可以识别Ser652被磷酸化的内源性α-E-catenin蛋白。多克隆抗体由合成肽段免疫动物产生，该肽段与人α-E-catenin的Ser652残基及邻近氨基酸序列一致。抗体经过蛋白A和肽亲和层析纯化。粘着连接是一种形成细胞间接触的动力结构， 在发育、分化、组织完整性、形态学和细胞极性中很重要。它们由跨膜蛋白cadherins组成，cadherin以钙依赖的方式在临近细胞上结合cadherin。在粘着连接细胞质的一边，经典模型说明cadherins通过β- 和 α-catenin与细胞骨架联系。α-E-catenin广泛表达，α-N-catenin在神经组织中表达，α-T-catenin主要在心脏组织中表达。E-cadherin 和α-E-catenin的减少发生在一些人类癌症进程中，说明粘着连接的降解对于癌症进程的重要性（综述1）。近来证据显示，在cadherins 和 actin之间不是静态连接，α-catenin直接调控肌动蛋白动力学机制，很可能通过和肌动蛋白竞争成核arp2/3复合物（2,3）. α-catenin也起作用调控β-catenin依赖的转录活性，影响分化和对Wnt信号通路的反应。α-catenin在核内结合β-catenin，阻止它调控转录，两种蛋白的水平被蛋白酶体依赖的降解所调控（4）。α-E-catenin的磷酸化被认为是一个有重要功能的翻译后修饰。例如，casein kinase 2磷酸化Ser641调节了α-E-catenin 和 β-catenin的相互作用(5)。质谱结果在多种细胞类型中确认了α-E-catenin的Ser652磷酸化，尽管这个修饰的功能尚未完全清楚。

1. Kobielak, A. and Fuchs, E. (2004) Nat Rev Mol Cell Biol 5, 614-25.
2. Yamada, S. et al. (2005) Cell 123, 889-901.
3. Drees, F. et al. (2005) Cell 123, 903-15.
4. Hwang, S.G. et al. (2005) J Biol Chem 280, 12758-65.
5. Ji, H. et al. (2009) Mol Cell 36, 547-59.
6. Rigbolt, K.T. et al. (2011) Sci Signal 4, rs3.
7. Chen, L. et al. (2010) J Proteome Res 9, 174-8.
8. Brill, L.M. et al. (2009) Cell Stem Cell 5, 204-13.

原厂资料：

Specificity / Sensitivity

Phospho-α-E-Catenin (Ser652) Antibody recognizes endogenous levels of α-E-catenin protein only when phosphorylated at Ser652.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser652 of human α-E-catenin protein. Antibodies are purified by protein A and peptide affinity chromatography.

Background

Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).

Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).

1. Kobielak, A. and Fuchs, E. (2004) Nat Rev Mol Cell Biol 5, 614-25.
2. Yamada, S. et al. (2005) Cell 123, 889-901.
3. Drees, F. et al. (2005) Cell 123, 903-15.
4. Hwang, S.G. et al. (2005) J Biol Chem 280, 12758-65.
5. Ji, H. et al. (2009) Mol Cell 36, 547-59.
6. Rigbolt, K.T. et al. (2011) Sci Signal 4, rs3.
7. Chen, L. et al. (2010) J Proteome Res 9, 174-8.
8. Brill, L.M. et al. (2009) Cell Stem Cell 5, 204-13.

注意事项：

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