Phospho-tau (pSer413)

Class

Anti-phospho-tau (pSer413) monoclonal antibody

Tau is a protein that normally stabilizes microtubules, the internal scaffolding of neurons that supports transport of materials along nerve cell projections. Its activity is regulated by phosphorylation, the addition of phosphate groups at specific sites. In Alzheimer's disease and related tauopathies, tau becomes abnormally and excessively phosphorylated at multiple sites, one of which is serine 413. This hyperphosphorylation causes tau to detach from microtubules, misfold, and aggregate into insoluble tangles inside and between neurons, disrupting cell function and contributing to neuronal death. Because phosphorylation at particular residues is enriched in diseased tissue relative to healthy tau, antibodies designed against a specific phosphoepitope such as pSer413 aim to recognize pathological tau conformations preferentially over the normal, functional protein. This selectivity is intended to neutralize toxic tau species and interfere with their transfer between neurons, a process thought to underlie the spread of pathology through the brain, without disrupting tau's normal role in intact neurons. This mechanism is being explored broadly across neurodegenerative conditions characterized by tau pathology, including Alzheimer's disease and certain frontotemporal dementias, as part of efforts to slow disease progression rather than merely address symptoms.