Phospho-Tau (Thr212, Ser214) Monoclonal Antibody (AT100), Invitrogen™

Description

MN1060 recognized PHF-Tau. No cross reactivity with normal biopsy-or-autopsy-derived Tau or fetal Tau has been observed. This suggests that this antibody detects an abnormal phosphorylation site unique to PHF-Tau. The epitope of this antibody has been show to contain phosphorylated Ser214 and phosphorylated Thr212 residues (numbering according to human Tau40). MN1060 detects PHF-tau (Thr212/Ser214) which has a predicted molecular weight of approximately 79 kDa. This product is a Low Endotoxin formulation. Purity is >95% as determined by SDS-PAGE.

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, μgtimately 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.