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Merck

MAB5450

Sigma-Aldrich

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

ascites fluid, clone PHF-6, Chemicon®

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About This Item

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

Biologische Quelle

mouse

Antikörperform

ascites fluid

Klon

PHF-6, monoclonal

Speziesreaktivität

human

Hersteller/Markenname

Chemicon®

Methode(n)

ELISA: suitable
western blot: suitable

Isotyp

IgG1

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Posttranslationale Modifikation Target

phosphorylation (pThr231)

Spezifität

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.

Immunogen

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

Anwendung

Research Category
Neurowissenschaft
Research Sub Category
Neurodegenerative Krankheiten
Anti-Tau Antibody, phosphoThreonine 231, clone PHF-6 is an antibody against Tau for use in ELISA & WB.
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.

Physikalische Form

Liquid.

Lagerung und Haltbarkeit

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

Rechtliche Hinweise

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

Haftungsausschluss

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.

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

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
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
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
Chadwick M Hales et al.
Brain pathology (Zurich, Switzerland), 24(4), 344-351 (2014-02-28)
We recently discovered that protein components of the ribonucleic acid (RNA) spliceosome form cytoplasmic aggregates in Alzheimer's disease (AD) brain, resulting in widespread changes in RNA splicing. However, the involvement of small nuclear RNAs (snRNAs), also key components of the
Qi Guo et al.
Frontiers in molecular neuroscience, 14, 623659-623659 (2021-04-06)
Core spliceosome and related RNA-binding proteins aggregate in Alzheimer's disease (AD) brain even in early asymptomatic stages (AsymAD) of disease. To assess the specificity of RNA-binding protein aggregation in AD, we developed a targeted mass spectrometry approach to quantify broad

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