MONOCLONAL-ANTIBODY AT8 RECOGNIZES TAU-PROTEIN PHOSPHORYLATED AT BOTH SERINE-202 AND THREONINE-205
MONOCLONAL-ANTIBODY AT8 RECOGNIZES TAU-PROTEIN PHOSPHORYLATED AT BOTH SERINE-202 AND THREONINE-205
复制标题
DOI：
10.1016/0304-3940(95)11484-e
复制
发表时间：
1995-04-21
影响因子：
2.5
通讯作者：
VANMECHELEN, E
中科院分区：
文献类型：
--
作者：
GOEDERT, M;JAKES, R;VANMECHELEN, E
过度磷酸化的微管相关蛋白tau是阿尔茨海默病的成对螺旋丝的主要成分，磷酸化依赖性抗tau抗体被用于鉴定来自正常脑和阿尔茨海默病脑的tau中磷酸化的特定氨基酸。因此，单克隆抗体AT8被广泛使用。通过重组TAN的定点诱变和体外磷酸化的组合，我们表明AT8需要tau蛋白在丝氨酸202和苏氨酸205处磷酸化（使用最长的人脑TAN同种型的编号）。
Hyperphosphorylated microtubule-associated protein tau is the major component of the paired helical filament of Alzheimer's disease, Phosphorylation-dependent anti-tau antibodies are being used to identify specific amino acids that are phosphorylated in tau from normal brain and Alzheimer's disease brain. As such, monoclonal antibody AT8 is widely used. By a combination of site-directed mutagenesis of recombinant tan and in vitro phosphorylation, we show that AT8 requires tau protein to be phosphorylated at both serine 202 and threonine 205 (using the numbering of the longest human brain tan isoform).