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Tau is a microtubule-associated phosphoprotein (MAP), localized in neuronal axons. It promotes tubulin polymerization and stabilizes microtubules. Tau proteins constitute a family of six isoforms, which range from 352 to 441 amino acids. The tau variants differ from each other by the presence of either three or four repeat-regions in the carboxy-terminal part of the molecule and the absence or presence of one or two inserts in the amino-terminal part.Tau is hyperphosphorylated by ERK, GSK-3, TPKII, and CDK5. At least thirty phosphorylation sites have been described, including Thr39, Ser46, Thr50, Thr69, Thr153, Thr175, Thr181, Ser198, Ser199, Ser202, Thr205, Ser208, Ser210, Thr212, Ser214, Thr217, Thr231, Ser235, Ser237, Ser241, Ser262, Ser285, Ser305, Ser324, Ser352, Ser356, Ser396, Ser400, Thr403, Ser404, Ser409, Ser412, Ser413, Ser416, and Ser422. Specifically, TPKII phosphorylates serines 202 and 404. GSK-3β transfection phosphorylates serines 199, 202, 235, 396, 404 and 413, and threonines 205 and 231. These sites are among the major abnormal phosphorylation sites of Tau. Phosphorylation on these sites reduces the ability of a given Tau species to promote microtubule self-assembly. Hyperphosphorylated Tau is the major protein of the paired helical filaments (PHFs), which make up the pathological neurofibrillary tangles of Alzheimer's disease (AD). These PHFs are also found in the lesions of other central nervous system disorders.GenScript Rabbit Anti-Tau (Phospho-Thr217) Polyclonal Antibody is developed in rabbit using a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Thr217 of human Tau.
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, 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. 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.
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Protein Aliases: FLJ31424; FTDP17; G protein beta1/gamma2 subunit-interacting factor 1; map tau; MGC138549; Microtubule-associated protein tau; microtubule-associated protein tau, isoform 4; microtubules; Neurofibrillary tangle protein; neurofibrillary tangles; Neuronal Marker; Paired helical filament-tau; PHF-tau; PHFtau; protein phosphatase 1, regulatory subunit 103; Tau microtubule-associated protein; Tau-4; Tau5
Gene Aliases: AI413597; AW045860; DDPAC; FTDP-17; MAPT; MAPTL; MSTD; Mtapt; MTBT1; MTBT2; PPND; PPP1R103; pTau; RNPTAU; TAU
UniProt ID: (Human) P10636, (Mouse) P10637
Entrez Gene ID: (Human) 4137, (Rat) 29477, (Mouse) 17762
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