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company name :
Invitrogen
other brands :
NeoMarkers, Lab Vision, Endogen, Pierce, BioSource International, Zymed Laboratories, Caltag, Molecular Probes, Research Genetics, Life Technologies, Applied Biosystems, GIBCO BRL, ABgene, Dynal, Affinity BioReagents, Nunc, Invitrogen, NatuTec, Oxoid, Richard-Allan Scientific, Arcturus, Perseptive Biosystems, Proxeon, eBioscience
product type :
antibody
product name :
Phospho-Tau (Thr217) Polyclonal Antibody
catalog :
44-744
quantity :
100 µL
price :
US 446
clonality :
polyclonal
host :
domestic rabbit
conjugate :
nonconjugated
antigen modification :
phosphorylated
reactivity :
baboons, African green monkey, human, mouse, rat, dogs, bovine, domestic sheep
application :
western blot, ELISA, immunohistochemistry, immunocytochemistry, immunohistochemistry - paraffin section, western blot knockout validation
more info or order :
citations: 23
Published Application/Species/Sample/DilutionReference
  • western blot; mouse
  • western blot knockout validation; human; 1:500; tbl 1
  • immunocytochemistry; human; 1:100; tbl 2
Ercan E, Eid S, Weber C, Kowalski A, Bichmann M, Behrendt A, et al. A validated antibody panel for the characterization of tau post-translational modifications. Mol Neurodegener. 2017;12:87 pubmed publisher
  • ELISA; human; loading ...; fig 1a
Ercan Herbst E, Ehrig J, Schöndorf D, Behrendt A, Klaus B, Gomez Ramos B, et al. A post-translational modification signature defines changes in soluble tau correlating with oligomerization in early stage Alzheimer's disease brain. Acta Neuropathol Commun. 2019;7:192 pubmed publisher
  • western blot; mouse; 1:1000; loading ...; fig 2A
Chen S, Sun J, Zhao G, Guo A, Chen Y, Fu R, et al. Liraglutide Improves Water Maze Learning and Memory Performance While Reduces Hyperphosphorylation of Tau and Neurofilaments in APP/PS1/Tau Triple Transgenic Mice. Neurochem Res. 2017;42:2326-2335 pubmed publisher
  • immunohistochemistry; rat
  • western blot; rat
  • western blot; domestic sheep
  • western blot; bovine
  • western blot; African green monkey
  • western blot; baboons
  • western blot; mouse
  • immunohistochemistry - paraffin section; dogs; 1:1000
Smolek T, Madari A, Farbáková J, Kandrac O, Jadhav S, Cente M, et al. Tau hyperphosphorylation in synaptosomes and neuroinflammation are associated with canine cognitive impairment. J Comp Neurol. 2016;524:874-95 pubmed publisher
Stoner A, Fu L, Nicholson L, Zheng C, Toyonaga T, Spurrier J, et al. Neuronal transcriptome, tau and synapse loss in Alzheimer's knock-in mice require prion protein. Alzheimers Res Ther. 2023;15:201 pubmed publisher
Kemppainen S, Huber N, Willman R, Zamora A, M xe4 kinen P, Martiskainen H, et al. Organotypic Hippocampal Slice Cultures from Adult Tauopathy Mice and Theragnostic Evaluation of Nanomaterial Phospho-TAU Antibody-Conjugates. Cells. 2023;12: pubmed publisher
Sakakibara Y, Yamashiro R, Chikamatsu S, Hirota Y, Tsubokawa Y, Nishijima R, et al. Drosophila Toll-9 is induced by aging and neurodegeneration to modulate stress signaling and its deficiency exacerbates tau-mediated neurodegeneration. iScience. 2023;26:105968 pubmed publisher
Zhang Y, Yang Y, Hu Z, Zhu M, Qin S, Yu P, et al. Long-Term Depression-Inducing Low Frequency Stimulation Enhances p-Tau181 and p-Tau217 in an Age-Dependent Manner in Live Rats. J Alzheimers Dis. 2022;89:335-350 pubmed publisher
Ashton N, Benedet A, Pascoal T, Karikari T, Lantero Rodriguez J, Brum W, et al. Cerebrospinal fluid p-tau231 as an early indicator of emerging pathology in Alzheimer's disease. EBioMedicine. 2022;76:103836 pubmed publisher
Xie C, Zhuang X, Niu Z, Ai R, Lautrup S, Zheng S, et al. Amelioration of Alzheimer's disease pathology by mitophagy inducers identified via machine learning and a cross-species workflow. Nat Biomed Eng. 2022;6:76-93 pubmed publisher
Saroja S, Sharma A, Hof P, Pereira A. Differential expression of tau species and the association with cognitive decline and synaptic loss in Alzheimer's disease. Alzheimers Dement. 2022;18:1602-1615 pubmed publisher
Pushkarsky T, Ward A, Ivanov A, Lin X, Sviridov D, Nekhai S, et al. Abundance of Nef and p-Tau217 in Brains of Individuals Diagnosed with HIV-Associated Neurocognitive Disorders Correlate with Disease Severance. Mol Neurobiol. 2022;59:1088-1097 pubmed publisher
Javonillo D, Tran K, Phan J, Hingco E, Kram xe1 r E, da Cunha C, et al. Systematic Phenotyping and Characterization of the 3xTg-AD Mouse Model of Alzheimer's Disease. Front Neurosci. 2021;15:785276 pubmed publisher
Wu R, Li L, Shi R, Zhou Y, Jin N, Gu J, et al. Dephosphorylation Passivates the Seeding Activity of Oligomeric Tau Derived From Alzheimer's Brain. Front Mol Neurosci. 2021;14:631833 pubmed publisher
Karikari T, Emer x161 i x10d A, Vrillon A, Lantero Rodriguez J, Ashton N, Kramberger M, et al. Head-to-head comparison of clinical performance of CSF phospho-tau T181 and T217 biomarkers for Alzheimer's disease diagnosis. Alzheimers Dement. 2021;17:755-767 pubmed publisher
Su xe1 rez Calvet M, Karikari T, Ashton N, Lantero Rodr xed guez J, Mil xe0 Alom xe0 M, Gispert J, et al. Novel tau biomarkers phosphorylated at T181, T217 or T231 rise in the initial stages of the preclinical Alzheimer's continuum when only subtle changes in Aβ pathology are detected. EMBO Mol Med. 2020;12:e12921 pubmed publisher
Gu J, Xu W, Jin N, Li L, Zhou Y, Chu D, et al. Truncation of Tau selectively facilitates its pathological activities. J Biol Chem. 2020;295:13812-13828 pubmed publisher
Zhang Y, Huang N, Lu H, Huang J, Jin H, Shi J, et al. Icariin protects against sodium azide-induced neurotoxicity by activating the PI3K/Akt/GSK-3β signaling pathway. Peerj. 2020;8:e8955 pubmed publisher
Miao J, Shi R, Li L, Chen F, Zhou Y, Tung Y, et al. Pathological Tau From Alzheimer's Brain Induces Site-Specific Hyperphosphorylation and SDS- and Reducing Agent-Resistant Aggregation of Tau in vivo. Front Aging Neurosci. 2019;11:34 pubmed publisher
Zhou Y, Shi J, Chu D, Hu W, Guan Z, Gong C, et al. Relevance of Phosphorylation and Truncation of Tau to the Etiopathogenesis of Alzheimer's Disease. Front Aging Neurosci. 2018;10:27 pubmed publisher
Hu W, Wu F, Zhang Y, Gong C, Iqbal K, Liu F. Expression of Tau Pathology-Related Proteins in Different Brain Regions: A Molecular Basis of Tau Pathogenesis. Front Aging Neurosci. 2017;9:311 pubmed publisher
Hodgson L, Spiering D, Sabouri Ghomi M, Dagliyan O, DerMardirossian C, Danuser G, et al. FRET binding antenna reports spatiotemporal dynamics of GDI-Cdc42 GTPase interactions. Nat Chem Biol. 2016;12:802-809 pubmed publisher
Blas Rus N, Bustos Morán E, Perez de Castro I, de Carcer G, Borroto A, Camafeita E, et al. Aurora A drives early signalling and vesicle dynamics during T-cell activation. Nat Commun. 2016;7:11389 pubmed publisher
product information
Product Type :
Antibody
Product Name :
Phospho-Tau (Thr217) Polyclonal Antibody
Catalog # :
44-744
Quantity :
100 µL
Price :
US 446
Clonality :
Polyclonal
Purity :
Antigen affinity chromatography
Host :
Rabbit
Reactivity :
Human, Mouse, Rat
Applications :
Immunohistochemistry (Paraffin): 1:20-1:200, Western Blot: 1:1,000
Species :
Human, Mouse, Rat
Isotype :
IgG
Storage :
-20°C
Description :
Tau is a neuronal microtubule-associated protein found predominantly on axons. The function of Tau is to promote tubulin polymerization and stabilize microtubules. The C-terminus binds axonal microtubules while the N- terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton while the longer isoforms may preferentially play a role in its stabilization. In its hyper-phosphorylated form, Tau is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer's diseases (AD) brain. Hyper-phosphorylation 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 phosphorylate Tau, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II. Hyper-phosphorylated Tau is found in neurofibrillary lesions in a range and other central nervous system disorders such as Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
Immunogen :
The antiserum was produced against a chemically synthesized phosphopeptide derived from the region of human tau that contains threonine 217.
Format :
Liquid
Applications w/Dilutions :
Immunohistochemistry (Paraffin): 1:20-1:200, Western Blot: 1:1,000
Aliases :
AI413597; AW045860; DDPAC; FLJ31424; FTDP17; FTDP-17; G protein beta1/gamma2 subunit-interacting factor 1; map tau; Mapt; MAPTL; MGC138549; microtubule associated protein tau; microtubule-associated protein tau; microtubule-associated protein tau, isoform 4; microtubules; MSTD; Mtapt; MTBT1; MTBT2; Neurofibrillary tangle protein; neurofibrillary tangles; Neuronal Marker; paired helical filament-tau; PHFtau; PHF-tau; PPND; PPP1R103; protein phosphatase 1, regulatory subunit 103; pTau; RNPTAU; Tau; Tau microtubule-associated protein; tau protein; Tau-4; Tau5; Unknown (protein for MGC:134287)
more info or order :
company information
Invitrogen
Thermo Fisher Scientific
81 Wyman Street
Waltham, MA USA 02451
https://www.thermofisher.com
800-678-5599
headquarters: USA