Tau is a neuronal microtubule-associated protein found predominantly on axons and functions to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer′s disease (AD) brain. Hyperphosphorylated Tau is also found in neurofibrillary lesions in a range of other central nervous system disorders. Hyperphosphorylation 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, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II (CK2), phosphorylate Tau. Serine 396 is phosphorylated by GSK-3beta and cdk5 in vitro and in vivo.
Especificidad
Tau phosphoSerine 396. The antibody recognizes Tau pSerine 396 in samples of recombinant human Tau treated with GSK-3beta for 45 minutes. The reactivity of the antibody is blocked with the pSerine 396 peptide but not the non-phosphopeptide or a generic phosphoSerine-containing peptide.
The immunogen is conserved in rat, mouse, rhesus monkey, goat, bovine and baboon.
Inmunógeno
Synthetic peptide of amino acids surrounding the phosphoSerine 396 site of human Tau.
Aplicación
Anti-Tau phospho Serine 396 Antibody detects level of Tau phospho Serine 396 & has been published & validated for use in WB.
Información legal
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 2
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Tauopathies, a group of neurodegenerative disorders, are characterized by disrupted homeostasis of the microtubule binding protein tau. Nogo-A mainly hinders axonal growth and development in neurons, but the underlying mechanism of tau vulnerability has not been determined. Here, to gain
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