The At100 antibody, also known as MN1060, plays a crucial role in identifying a specific form of Tau protein known as PHF-Tau (Paired Helical Filament Tau). This protein is a hallmark of neurodegenerative diseases like Alzheimer’s disease. This article explores the function of AT100, its target PHF-Tau, and the significance of this interaction in research.
The Specificity of AT100 (MN1060) for PHF-Tau
AT100 specifically recognizes PHF-Tau, a hyperphosphorylated form of Tau protein. It exhibits no cross-reactivity with normal Tau proteins, indicating its unique ability to target the abnormal phosphorylation site characteristic of PHF-Tau. This specificity is attributed to the antibody’s recognition of phosphorylated Ser214 and Thr212 residues within the Tau protein structure. This precise targeting allows researchers to differentiate between healthy and diseased Tau proteins. Furthermore, AT100 detects PHF-tau (Thr212/Ser214) with a predicted molecular weight of around 79 kDa, ensuring accurate identification. The antibody is purified to >95% purity as determined by SDS-PAGE and formulated with low endotoxin levels for optimal research use.
Tau Protein and Its Role in Neurodegenerative Diseases
Tau is a microtubule-associated protein primarily located in axons of neurons. Its primary function is to promote tubulin polymerization and stabilize microtubules, essential for maintaining neuronal structure and function. Tau’s C-terminus binds to axonal microtubules, while the N-terminus interacts with neural plasma membrane components, effectively linking these crucial cellular structures. Tau isoforms, varying in length, contribute to cytoskeleton plasticity and stabilization. However, in certain pathological conditions, Tau undergoes hyperphosphorylation, leading to the formation of PHF. These PHFs are the primary component of neurofibrillary tangles, a defining characteristic of Alzheimer’s disease.
Hyperphosphorylation and the Formation of PHF-Tau
Hyperphosphorylation of Tau disrupts its microtubule binding function, destabilizing microtubules and ultimately leading to neuronal degeneration. Various kinases, including GSK-3β, PKA, CDK5, and casein kinase II, contribute to Tau hyperphosphorylation. The accumulation of hyperphosphorylated Tau in the form of PHF is observed not only in Alzheimer’s disease but also in other neurodegenerative disorders such as Pick’s disease, frontotemporal dementia, cortico-basal degeneration, and progressive supranuclear palsy.
The Importance of AT100 in Research
AT100, with its high specificity for PHF-Tau, serves as a valuable tool for researchers investigating the pathogenesis of neurodegenerative diseases. It enables the detection and quantification of PHF-Tau in biological samples, aiding in the diagnosis, monitoring disease progression, and evaluating the efficacy of potential therapeutic interventions.
Conclusion
The AT100 antibody is a powerful research tool for studying PHF-Tau and its role in neurodegenerative diseases. Its specificity for the abnormally phosphorylated Tau protein allows researchers to distinguish between healthy and diseased states, providing valuable insights into disease mechanisms and potential therapeutic targets. While not intended for diagnostic use, AT100 continues to be instrumental in advancing our understanding of complex neurological disorders.
