A monoclonal antibody that cross-reacts with phosphorylated epitopes on two microtubule-associated proteins and two neurofilament polypeptides.
A monoclonal antibody that cross-reacts with phosphorylated epitopes on two microtubule-associated proteins and two neurofilament polypeptides.
复制标题
一种单克隆抗体，可与两种微管相关蛋白和两种神经丝多肽上的磷酸化表位发生交叉反应。
DOI：
10.1073/pnas.83.4.1006
复制
发表时间：
1986
影响因子：
11.1
通讯作者：
Vallee,RB
中科院分区：
文献类型：
--
作者：
Luca,FC;Bloom,GS;Vallee,RB
描述了一种针对牛脑微管相关蛋白（MAP） 1B的单克隆抗体。免疫印迹分析显示抗原的去磷酸化使免疫反应性消失。磷酸钠也能直接抑制抗原/抗体反应。在全脑组织中，MAP 1B是主要的免疫反应种。然而，该抗体也被发现与MAP 1A以及高分子量和中等分子量的神经丝多肽发生反应。未观察到与已知广泛磷酸化的MAP 2、其他MAP或低分子量神经丝多肽的交叉反应。这一证据表明，至少在神经元细胞骨架的这些不同多肽组分之间存在一些序列同源性，并指出了它们磷酸化的共同机制。
A monoclonal antibody is described that was raised against bovine brain microtubule-associated protein (MAP) 1B. Immunoblot analysis revealed that immunoreactivity was abolished by dephosphorylation of the antigen. The antigen/antibody reaction was also directly inhibited by sodium phosphate. In whole brain tissue, MAP 1B was the primary immunoreactive species. However, the antibody was also found to react with MAP 1A as well as with the high and middle molecular weight neurofilament polypeptides. No cross-reaction with MAP 2, which is known to be extensively phosphorylated, other MAPs, or the low molecular weight neurofilament polypeptide was observed. This evidence suggests at least some sequence homology between these different polypeptide components of the neuronal cytoskeleton and points to a common mechanism for their phosphorylation.