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Key Documents

AB9658

Sigma-Aldrich

Anti-Tau phospho Serine 396 Antibody

Chemicon®, from rabbit

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About This Item

Kod UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41

pochodzenie biologiczne

rabbit

Poziom jakości

forma przeciwciała

affinity purified immunoglobulin

rodzaj przeciwciała

primary antibodies

klon

polyclonal

oczyszczone przez

affinity chromatography

reaktywność gatunkowa

human

producent / nazwa handlowa

Chemicon®

metody

western blot: suitable

numer dostępu UniProt

Warunki transportu

dry ice

docelowa modyfikacja potranslacyjna

phosphorylation (pSer396)

informacje o genach

human ... MAPT(4137)

Opis ogólny

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.

Specyficzność

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.

Immunogen

Synthetic peptide of amino acids surrounding the phosphoSerine 396 site of human Tau.

Zastosowanie

Anti-Tau phospho Serine 396 Antibody detects level of Tau phospho Serine 396 & has been published & validated for use in WB.

Informacje prawne

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
This page may contain text that has been machine translated.

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Kod klasy składowania

10 - Combustible liquids

Klasa zagrożenia wodnego (WGK)

WGK 2


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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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