MAB5450
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
Empfohlene Produkte
Biologische Quelle
mouse
Antikörperform
ascites fluid
Klon
PHF-6, monoclonal
Speziesreaktivität
human
Hersteller/Markenname
Chemicon®
Methode(n)
ELISA: suitable
western blot: suitable
Isotyp
IgG1
NCBI-Hinterlegungsnummer
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
Neurowissenschaft
Research Sub Category
Neurodegenerative Krankheiten
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.
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)
Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.
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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
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
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
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
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