Phospho-Tau (Thr50) antibodies are specialized tools used to study post-translational modifications of the microtubule-associated protein Tau, which plays a critical role in stabilizing neuronal microtubules. In pathological conditions like Alzheimer’s disease (AD) and other tauopathies, Tau becomes hyperphosphorylated, leading to its detachment from microtubules, aggregation into neurofibrillary tangles (NFTs), and neuronal dysfunction. The Thr50 phosphorylation site, located within Tau's proline-rich domain, is implicated in modulating Tau’s conformation, microtubule-binding affinity, and interaction with other proteins. Antibodies targeting phospho-Tau (Thr50) enable researchers to detect and quantify this specific phosphorylation event, providing insights into disease mechanisms and Tau’s pathological transformation.
These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to assess Tau phosphorylation in cellular models, animal studies, and human postmortem brain tissues. Their specificity helps distinguish pathological Tau from normal isoforms, aiding in the diagnosis and staging of tauopathies. Additionally, they serve as valuable tools for evaluating therapeutic strategies aimed at reducing Tau hyperphosphorylation, such as kinase inhibitors or phosphatase activators. Understanding Thr50 phosphorylation’s role in Tau aggregation and toxicity may contribute to developing biomarkers or targeted treatments for neurodegenerative diseases.