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Description

Tau or Microtubule-associated protein tau (MAPT), also known as neurofibrillary tangle protein and paired helical filament-tau (PHF-tau), is a cytosolic protein that promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of axonal polarity in neurons. Tau binds to and is thought to function as a linker protein between axonal microtubules and neural plasma membrane components. There are multiple isoforms, and the short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. PAD is the phosphatase activating domain, and has been demonstrated to be involved in the inhibition of anterograde, kinesin-based fast axonal transport (FAT) by activating axonal protein phosphatase 1 (PP1) and glycogen synthase kinase 3 (GSK3), independent of microtubule binding. Defects in Tau are thought to be the cause of a number of neurodegenerative diseases, including frontotemporal dementia (FTD), pallido-ponto-nigral degeneration (PPND), Pick disease of the brain (PIDB), corticobasal degeneration (CBD), supranuclear palsy type 1 (PSNP1), Alzheimer disease, and Parkinson disease. Clone T49 exhibits immunoreactivity against bovine, rat, and murine, but not human, Tau (UniProt P29172, P19332, P10637, P10636, respectively).