Tau is a neuronal microtubule-associated protein found predominantly on axons. Tau's function is to stabilize microtubules and promote tubulin polymerization. Tau functions as a linker protein, binding both axonal and neural microtubules. The C-terminus also binds to axonal microtubules. TAU/MAPT localization in the neuronal cells determines axonal polarity.
It is located in the zone of the cell body that is defined by the centrosome. The shorter isoforms enable plasticity in the cytoskeleton, while the length may play a preferential role in its stabilization. Tau antigen, in its hyper-phosphorylated state, is the main component of paired Helical Filaments (PHF), which are the building blocks of neurofibrillary lesions in the Alzheimer's disease (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.
Hyperphosphorylated Tau can be found in the neurofibrillary lesions in a range as well as other central nervous system disorders like Pick's disease and frontotemporal dementia. Antibodies that detect Tau are useful in a variety of scientific applications including Western Blot and Immunohistochemistry. These antibodies target Tau in human, rat, mouse, bovine, and ovine samples.
To confirm the specificity of these antibodies, they have been tested by cell treatment, relative expression, Knockout, and peptide array. Choose the Tau antibody that best suits your needs. Tauopathies refers to a group that causes neurodegeneration by cytosolic tau protein accumulation in brain cells.