Anti-Tau Antibody, Cleaved (D421), clone Tau-C3, Ascites Free clone Tau-C3, from mouse

Microtubule-associated protein tau (UniProt P10636; also known as Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau) is encoded by the MAPT (also known as TAU, MAPT1, MTBTL) gene (Gene ID 4137) in human. Extracellular plaque deposits composed of amyloid-beta and intracellular neurofibrillary tangles (NFTs) composed of truncated and hyperphosphorylated tau are two neuropathological hallmarks of Alzheimer's disease (AD). Tau pathology (tauopathy) can cause toxicity when the brain is devoid of amyloid plaques, and tangle pathology correlates better with clinical dementia than amyloid pathology. Abnormal processing of tau by hyperphosphorylation and proteolytic truncation contribute to the toxicity of tau. Tau is known to be cleaved by various proteases, including caspases, calpains, cathepsins, thrombin, and puromycin-sensitive aminopeptidase, as well as the lysosomal cysteine proteinase asparagine endopeptidase (AEP). MAPK, GSK-3, and Cdk-5 are three known kinases that target various tau phosphorylation sites. Tau also undergoes other types of posttranslational modifications, including glycosylation, ubiquitination, glycation, polyamination, nitration, and lysine methylation, which are believed to be important for its non-pathological functions, including polymerization and stabilization of microtubules.