AB9658
Anti-Tau phospho Serine 396 Antibody
Chemicon®, from rabbit
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About This Item
Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Productos recomendados
origen biológico
rabbit
Nivel de calidad
forma del anticuerpo
affinity purified immunoglobulin
tipo de anticuerpo
primary antibodies
clon
polyclonal
purificado por
affinity chromatography
reactividad de especies
human
fabricante / nombre comercial
Chemicon®
técnicas
western blot: suitable
Nº de acceso NCBI
Nº de acceso UniProt
Condiciones de envío
dry ice
modificación del objetivo postraduccional
phosphorylation (pSer396)
Información sobre el gen
human ... MAPT(4137)
Categorías relacionadas
Descripción general
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
Certificados de análisis (COA)
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Protein kinase C and calcium / calmodulin-dependent protein kinase II phosphorylate three-repeat and four-repeat tau isoforms at different rates.
Singh, T.J., et al.
Molecular and Cellular Biochemistry, 168(1-2), 141-148 (1997)
E Sontag et al.
Neuron, 17(6), 1201-1207 (1996-12-01)
Recently, we reported that a pool of protein phosphatase 2A (PP2A) is associated with microtubules. Here, we demonstrate that specific isoforms of PP2A bind and dephosphorylate the neuronal microtubule-associated protein tau. Coexpression of tau and SV40 small t, a specific
G A Jicha et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 19(17), 7486-7494 (1999-08-25)
To elucidate the role cAMP-dependent protein kinase (PKA) phosphorylations on tau play in Alzheimer's disease, we have generated highly specific monoclonal antibodies, CP-3 and PG-5, which recognize the PKA-dependent phosphorylations of ser214 and ser409 in tau respectively. The present study
Jean C Augustinack et al.
Acta neuropathologica, 103(1), 26-35 (2002-02-12)
Microtubule associated protein tau is abnormally phosphorylated in Alzheimer's disease (AD) and aggregates as paired helical filaments (PHFs) in neurofibrillary tangles (NFTs). We show here that the pattern of tau phosphorylation correlates with the loss of neuronal integrity. Studies using
A D Alonso et al.
The Journal of biological chemistry, 276(41), 37967-37973 (2001-08-10)
The microtubule-associated protein tau is a family of six isoforms that becomes abnormally hyperphosphorylated and accumulates in neurons undergoing neurodegeneration in the brains of patients with Alzheimer disease (AD). We investigated the isoform-specific interaction of normal tau with AD hyperphosphorylated
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