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Merck
CN

MAB5450

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

ascites fluid, clone PHF-6, Chemicon®

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Clone:
PHF-6, monoclonal
Species reactivity:
human
Application:
ELISA, WB
Citations:
8
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biological source

mouse

antibody form

ascites fluid

clone

PHF-6, monoclonal

species reactivity

human

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable, western blot: suitable

isotype

IgG1

UniProt accession no.

shipped in

dry ice

target post-translational modification

phosphorylation (pThr231)

Immunogen

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.

Biochem/physiol Actions

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.

Physical form

Liquid.

Preparation Note

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

Legal Information

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

Disclaimer

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.

存储类别

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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
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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