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Key Documents

MAB5450

Sigma-Aldrich

Anti-Tau Antibody, phosphoThreonine 231, clone PHF-6

ascites fluid, clone PHF-6, Chemicon®

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About This Item

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

Source biologique

mouse

Forme d'anticorps

ascites fluid

Clone

PHF-6, monoclonal

Espèces réactives

human

Fabricant/nom de marque

Chemicon®

Technique(s)

ELISA: suitable
western blot: suitable

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Modification post-traductionnelle de la cible

phosphorylation (pThr231)

Spécificité

Reacts with human Tau phosphorylated at threonine 231 and fetal tau. The antibody also reacts with dephosphorylated neurofibrillary tangles. MAB5450 is reactive with the Thr231 phosphorylated and diphosphorylated peptides. No reactivity with normal adult tau or with unphosphorylated or serine 235 phosphorylated protein.

Immunogène

Epitope: phosphoThreonine 231
Paired helical filaments tau preparation from human brain.

Application

Anti-Tau Antibody, phosphoThreonine 231, clone PHF-6 is an antibody against Tau for use in ELISA & WB.
Research Category
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Western blot: 1:1000, non-phosphate buffers recommended. Specific for phospho-tau however highly phosphorylated blocking materials like non-fat milk can sometimes cause difficulties, thus we generally recommend blocking western blots with TBS-1-2% BSA solutions (filtered through a 0.45μm membrane) for better results.

Immunohistochemistry: fresh frozen tissues with Tris-NaCl-Triton treatment

{http://www.jhc.org/cgi/content/full/48/12/1627} & http://ajp.amjpathol.org/cgi/content/full/160/6/2045

Optimal working dilutions must be determined by end user.

Forme physique

Liquid.

Stockage et stabilité

Maintain at -20°C in undiluted aliquots for up to 12 months after date of receipt. Avoid repeated freeze/thaw cycles.

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.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Aggregates of small nuclear ribonucleic acids (snRNAs) in Alzheimer's disease.
Hales, CM; Dammer, EB; Diner, I; Yi, H; Seyfried, NT; Gearing, M; Glass, JD; Montine et al.
Brain Pathology null
Quantitative phosphoproteomics of Alzheimer's disease reveals cross-talk between kinases and small heat shock proteins.
Dammer, EB; Lee, AK; Duong, DM; Gearing, M; Lah, JJ; Levey, AI; Seyfried, NT
Proteomics null
G T Bramblett et al.
Neuron, 10(6), 1089-1099 (1993-06-01)
Abnormally phosphorylated tau proteins (A68) are the building blocks of Alzheimer's disease (AD) paired helical filaments. The biological consequences of the conversion of normal adult tau to A68 remain unknown. Here we demonstrate that native A68 does not bind to
Chien-Ning Huang et al.
BMC complementary medicine and therapies, 20(1), 370-370 (2020-12-04)
Insulin resistance could be associated with the development of Alzheimer disease (AD). The neuropathological hallmarks of AD are beta amyloid (Aβ) produced from sequential cleavage initiated by β-secretase and degraded by insulin degradation enzyme (IDE), as well as hyperphosphorylation of
Pablo Martinez et al.
Nature neuroscience, 25(12), 1597-1607 (2022-11-08)
Tau aggregation is a defining histopathological feature of Alzheimer's disease and other tauopathies. However, the cellular mechanisms involved in tau propagation remain unclear. Here, we performed an unbiased quantitative proteomic study to identify proteins that specifically interact with this tau

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