Vaughan Meredith H, Xia Xiaobo, Wang Xiao, Chronopoulou Efthalia, Gao Guo-Jian, Campos-Gonzalez Roberto, Reynolds Albert B
Department of Cancer Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-6840, USA.
Hybridoma (Larchmt). 2007 Dec;26(6):407-15. doi: 10.1089/hyb.2007.0527.
To better understand the mechanisms that regulate p120-catenin (p120) and E-cadherin function, we are systematically generating phospho-specific monoclonal antibodies (MAb) to the major p120 phosphorylation sites. p120 has emerged recently as a master regulator of E-cadherin stability and an important modulator of RhoGTPase activities. A number of phosphorylation sites have been identified, but none have as yet been linked to specific regulatory roles. Here, we describe a novel phospho-specific monoclonal antibody to the major PKC-induced p120 phosphorylation site, phospho-serine 879 (pS879). With a few exceptions, p120 MAb pS879 is remarkably specific for the phosphorylated S879 epitope and works effectively in common applications such as Western blot analysis, immunoprecipitation, and immunofluorescence. p120 MAb pS879 should facilitate efforts to identify the role of S879 phosphorylation and to map signaling pathways that modify p120 function through activation of PKC.
为了更好地理解调节p120连环蛋白（p120）和E-钙黏蛋白功能的机制，我们正在系统地制备针对主要p120磷酸化位点的磷酸化特异性单克隆抗体（MAb）。p120最近已成为E-钙黏蛋白稳定性的主要调节因子以及RhoGTPase活性的重要调节剂。已经鉴定出许多磷酸化位点，但尚未发现它们与特定的调节作用相关。在此，我们描述了一种针对主要PKC诱导的p120磷酸化位点——磷酸化丝氨酸879（pS879）的新型磷酸化特异性单克隆抗体。除了少数例外，p120 MAb pS879对磷酸化的S879表位具有显著特异性，并且在诸如蛋白质免疫印迹分析、免疫沉淀和免疫荧光等常见应用中有效发挥作用。p120 MAb pS879应有助于确定S879磷酸化的作用，并绘制通过激活PKC来改变p120功能的信号通路。
