Tau Monoclonal Antibody (HT7), Invitrogen™

Description

MN1000 recognizes normal Tau from human and bovine brain and PHF-Tau. No cross reactivity with Tau from rat brain has been observed. The epitope of this antibody has been mapped on human Tau between residue 159 and 163 (numbering according to human Tau40), corresponding to the amino acid sequence PPGQK. MN1000 detects Tau which has a predicted molecular weight of approximately 79 kDa. 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.