Invitrogen™ Phospho-Tau (Ser396) Monoclonal Antibody (PHF13.6) 

Description

This monoclonal antibody recognizes phosphorylation-dependent epitopes of ser-396 on PHF-tau as well as fetal tau, but does not recognize autopsy-derived normal adult tau. Phosphoamino ser-396 is one of the two major immunodominant residues of PHF-tau. PHF 13.6 does not recognize unphosphorylated peptide 390-408 or the same peptide phosphorylated at ser-400, thr-403, or ser-404. PHF 13.6 specifically recognizes the ser-396 phosphorylated peptide and all diphosphorylated peptides containing phosphorylated ser-396. Reactivity was confirmed with human PHF-Tau.

Tau is a neuronal microtubule-associated protein found predominantly on axons. The function of Tau is to promote tubulin polymerization and stabilize microtubules. The C-terminus binds axonal microtubules while the N- terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton while the longer isoforms may preferentially play a role in its stabilization. In its hyper-phosphorylated form, Tau is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer's diseases (AD) brain. Hyper-phosphorylation impairs the microtubule binding function of Tau, resulting in the destabilization of microtubules in AD brains, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases phosphorylate Tau, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II. Hyper-phosphorylated Tau is found in neurofibrillary lesions in a range and other central nervous system disorders such as Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.