Tau Monoclonal Antibody (T46), Invitrogen™ 

Description

This antibody recognizes an epitope near the C-terminal region (404-441 aa) of human tau. It reacts with all 7 isoforms of human tau (binding-competent and binding-incompetent), A68 (an abnormal phosphorylated derivative of tau), bovine tau, and human NeuroFibrillary Tangles (NFTs). Reactivity is independent of the state of tau phosphorylation. Some cross-reactivity with MAP2 is also observed. This antibody is suitable for immunohistochemical staining of Bouin's-fixed or alcohol-fixed, paraffin-embedded or frozen tissue sections.

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.