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Key Documents

AB9674

Sigma-Aldrich

Anti-Tau phospho Serine 199/202 Antibody

Chemicon®, from rabbit

Synonyme(s) :

Anti-Anti-DDPAC, Anti-Anti-FTDP-17, Anti-Anti-MAPTL, Anti-Anti-MSTD, Anti-Anti-MTBT1, Anti-Anti-MTBT2, Anti-Anti-PPND, Anti-Anti-PPP1R103, Anti-Anti-TAU, Anti-Anti-tau-40

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About This Item

Code UNSPSC :
12352203
eCl@ss :
32160702
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Forme d'anticorps

affinity purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

polyclonal

Produit purifié par

affinity chromatography

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

western blot: suitable

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

phosphorylation (pSer199/pSer202)

Informations sur le gène

human ... MAPT(4137)

Description générale

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. Serines 199 and 202 are phosphorylated by GSK-3beta and have been linked to hereditary frontotemporal dementia. Serine 202 phosphorylation by cdk5, stimulated by the presence of microtubules, has been linked to hereditary neurodegenerative disease.

Spécificité

Tau phosphoSerine 199/202. The antibody recognizes Tau pSerine 199/202 in samples of recombinant human Tau treated with GSK-3beta for 45 minutes. The reactivity of the antibody is blocked with the pSerine 199/202 peptide but not the non-phosphopeptide, tau phosphopeptide corresponding to pSerine 199, tau phosphopeptide corresponding to pSerine 202 or a generic phosphoSerine-containing peptide.

Immunogène

Synthetic peptide of amino acids surrounding the phosphoSerine 199 and 202 sites of human Tau.

Application

Detect Tau phospho Serine 199/202 using this Anti-Tau phospho Serine 199/202 Antibody validated for use in WB.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Western blot: 1:1,000. Suggested blocking buffer is 5% BSA-TBST overnight at 2-8°C. Suggested antibody dilution buffer is 3% BSA-TBST. Suggested antibody incubation time is 2 hours at room temperature.

Optimal working dilutions must be determined by the end user.

Stockage et stabilité

Maintain at -20°C in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.

Informations légales

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

Clause de non-responsabilité

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

A Alvarez et al.
FEBS letters, 459(3), 421-426 (1999-10-20)
The key target of this study was the tau protein kinase II system (TPK II) involving the catalytic subunit cdk5 and the regulatory component p35. TPK II is one of the tau phosphorylating systems in neuronal cells, thus regulating its
Alzheimer's disease. The tangled tale of tau.
E Mandelkow
Nature, 402(6762), 588-589 (1999-12-22)
P K Davis et al.
The Journal of biological chemistry, 274(50), 35686-35692 (1999-12-10)
Although the importance of the microtubule network throughout cell life is well established, the dynamics of microtubules during apoptosis, a regulated cell death process, is unclear. In a previous study (Davis, P. K., and Johnson, G. V. (1999) Biochem. J.
N Haque et al.
Brain research, 838(1-2), 69-77 (1999-08-14)
Tau, one of the best characterized microtubule-associated proteins (MAPs), is a phosphoprotein, the biological activity of which is regulated by its degree of phosphorylation. The objective of the present study was to evaluate the regulation, phosphorylation and the biological activity
E Sontag et al.
The Journal of biological chemistry, 274(36), 25490-25498 (1999-08-28)
Hyperphosphorylated forms of the neuronal microtubule (MT)-associated protein tau are major components of Alzheimer's disease paired helical filaments. Previously, we reported that ABalphaC, the dominant brain isoform of protein phosphatase 2A (PP2A), is localized on MTs, binds directly to tau

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