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AB4841

Anti-Tau (phospho T205) antibody

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(15 Publications)

Rabbit Polyclonal TAU phospho T205 antibody. Suitable for Flow Cyt, WB, IHC-Fr and reacts with Human, Recombinant full length protein, Mouse samples. Cited in 15 publications. Immunogen corresponding to Synthetic Peptide within Human MAPT phospho T205.

View Alternative Names

MAPTL, MTBT1, TAU, MAPT, Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau

2 Images
Flow Cytometry - Anti-Tau (phospho T205) antibody (AB4841)
  • Flow Cyt

Supplier Data

Flow Cytometry - Anti-Tau (phospho T205) antibody (AB4841)

Flow cytometric analysis of 70% ethanol-fixed SH-SY5Y (human neuroblastoma cell line from bone marrow) cell line labeling Tau (phospho T205) with ab4841 at 5 μg/million cells (red) compared with a rabbit Isotype control details (pink),an unlabelled control (purple) and a secondary only control (green). Alexa Fluor® 488 Goat Anti-Rabbit, at 1/400 dilution was used as the secondary antibody.

Western blot - Anti-Tau (phospho T205) antibody (AB4841)
  • WB

Unknown

Western blot - Anti-Tau (phospho T205) antibody (AB4841)

WB using ab4841. The peptide corresponding to tau [pT205] blocks the antibody signal, thereby demonstrating the specificity of the antibody.

All lanes:

Western blot - Anti-Tau (phospho T205) antibody (ab4841)

Predicted band size: 78 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Mouse

Applications

IHC-Fr, Flow Cyt, WB

applications

Immunogen

Synthetic Peptide within Human MAPT phospho T205. The exact immunogen used to generate this antibody is proprietary information.

P10636

Specificity

The specificity of this antibody refers to P10636-8.

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Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Purification notes
Purified from rabbit serum by sequential epitope-specific chromatography. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated tau. The final product is generated by affinity chromatography using a tau-derived peptide that is phosphorylated at threonine 205.
Storage buffer
pH: 7.3 Preservative: 0.05% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Tau also known as microtubule-associated protein Tau (MAPT) plays an important role in stabilizing microtubules in neuronal cells. Tau is primarily found in the central nervous system but also exists in peripheral neurons. Human Tau protein comes in six isoforms due to alternative splicing with molecular weights ranging from 48 kDa to 67 kDa. This protein predominantly locates in the axons of neurons where it maintains the stability of microtubule tracks necessary for axonal transport.
Biological function summary

Tau is involved in the assembly and stabilization of microtubules essential for maintaining neuronal structure. It interacts with microtubule-binding domains (MBD) to bind and bundle microtubules facilitating intracellular transport. Tau forms a part of the neuronal cytoskeleton complex working closely with other cytoskeletal proteins to preserve the proper axonal transport and function. Abnormally phosphorylated Tau often termed phospho-Tau disrupts this complex affecting microtubule stability.

Pathways

Tau has critical involvement in several signaling cascades such as the microtubule-binding and transport pathways. Glycogen synthase kinase 3 beta (GSK3β) and cyclin-dependent kinase 5 (CDK5) frequently phosphorylate Tau controlling its interaction with microtubules. Phosphorylated Tau accumulates leading to the formation of neurofibrillary tangles often observed in neurodegenerative conditions. Additionally Tau interacts with GAPDH impacting cellular energy regulation through potential pathway cross-talk involving oxidative stress responses.

Tau is closely associated with Alzheimer's disease and frontotemporal dementia. In Alzheimer's disease hyperphosphorylated Tau aggregates into paired helical filaments forming neurofibrillary tangles while similar aggregates are observed in frontotemporal dementia. In these conditions Tau links to amyloid precursor protein (APP) where misregulated phosphorylation-driven interactions contribute to neurodegeneration. Identifying phospho-Tau and its altered interactions with related proteins aids in understanding and potentially treating these disorders.
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Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:
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Target data

The protein expressed by the MAPT gene promotes microtubule assembly and stability and might be involved in establishing and maintaining neuronal polarity. Its C-terminus binds axonal microtubules, and the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between the two. Axonal polarity is predetermined by MAPT localization within the neuronal cell's domain defined by the centrosome. The short isoforms allow cytoskeleton plasticity, whereas the longer isoforms may preferentially play a role in its stabilization. This supplementary information is collated from multiple sources and compiled automatically.
See full target information MAPT phospho T205
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Publications (15)

Recent publications for all applications. Explore the full list and refine your search

mBio 15:e0152224 PubMed39189744

2024

HSV-1 infection induces phosphorylated tau propagation among neurons via extracellular vesicles.

Applications

Unspecified application

Species

Unspecified reactive species

V Protto,M T Miteva,F Iannuzzi,M E Marcocci,D D Li Puma,R Piacentini,M Belli,L Sansone,A Pietrantoni,C Grassi,A T Palamara,G De Chiara

Science advances 8:eabl8809 PubMed35857446

2022

Alzheimer's disease: Ablating single master site abolishes tau hyperphosphorylation.

Applications

Unspecified application

Species

Unspecified reactive species

Kristie Stefanoska,Mehul Gajwani,Amanda R P Tan,Holly I Ahel,Prita R Asih,Alexander Volkerling,Anne Poljak,Arne Ittner

International journal of molecular sciences 23: PubMed35216271

2022

Detection of Pathological Markers of Neurodegenerative Diseases following Microfluidic Direct Conversion of Patient Fibroblasts into Neurons.

Applications

Unspecified application

Species

Unspecified reactive species

Cristiana Mollinari,Chiara De Dominicis,Leonardo Lupacchini,Luigi Sansone,Davide Caprini,Carlo Massimo Casciola,Ying Wang,Jian Zhao,Massimo Fini,Matteo Russo,Enrico Garaci,Daniela Merlo

iScience 24:102993 PubMed34505007

2021

Vascular smooth muscle cell dysfunction contribute to neuroinflammation and Tau hyperphosphorylation in Alzheimer disease.

Applications

Unspecified application

Species

Unspecified reactive species

Jorge A Aguilar-Pineda,Karin J Vera-Lopez,Pallavi Shrivastava,Miguel A Chávez-Fumagalli,Rita Nieto-Montesinos,Karla L Alvarez-Fernandez,Luis D Goyzueta Mamani,Gonzalo Davila Del-Carpio,Badhin Gomez-Valdez,Clint L Miller,Rajeev Malhotra,Mark E Lindsay,Christian L Lino Cardenas

Progress in neurobiology 197:101900 PubMed32841723

2020

Amelioration of Tau pathology and memory deficits by targeting 5-HT7 receptor.

Applications

Unspecified application

Species

Unspecified reactive species

Josephine Labus,Kian-Fritz Röhrs,Jana Ackmann,Hristo Varbanov,Franziska E Müller,Shaobo Jia,Kathrin Jahreis,Anna-Lena Vollbrecht,Malte Butzlaff,Yvonne Schill,Daria Guseva,Katrin Böhm,Rahul Kaushik,Monika Bijata,Philippe Marin,Séverine Chaumont-Dubel,Andre Zeug,Alexander Dityatev,Evgeni Ponimaskin

Theranostics 10:8430-8445 PubMed32724479

2020

Modulation of the Astrocyte-Neuron Lactate Shuttle System contributes to Neuroprotective action of Fibroblast Growth Factor 21.

Applications

Unspecified application

Species

Unspecified reactive species

Yan Sun,Yue Wang,Su-Ting Chen,Ying-Jie Chen,Jie Shen,Wen-Bing Yao,Xiang-Dong Gao,Song Chen

Frontiers in cellular neuroscience 13:239 PubMed31263400

2019

Activated PPARγ Abrogates Misprocessing of Amyloid Precursor Protein, Tau Missorting and Synaptotoxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Susanne Moosecker,Patrícia Gomes,Chrysoula Dioli,Shuang Yu,Ioannis Sotiropoulos,Osborne F X Almeida

Neurobiology of aging 76:80-95 PubMed30708185

2019

Progressive signaling changes in the olfactory nerve of patients with Alzheimer's disease.

Applications

Unspecified application

Species

Unspecified reactive species

Praveen Bathini,Antoine Mottas,Muriel Jaquet,Emanuele Brai,Lavinia Alberi

International journal of molecular medicine 43:435-442 PubMed30365112

2018

Amyloid β and tau are involved in sleep disorder in Alzheimer's disease by orexin A and adenosine A(1) receptor.

Applications

Unspecified application

Species

Unspecified reactive species

Zhenhua Liu,Fumin Wang,Minglu Tang,Yongjun Zhao,Xiaoting Wang

Acta neuropathologica communications 4:64 PubMed27364742

2016

Notch1 hallmarks fibrillary depositions in sporadic Alzheimer's disease.

Applications

Unspecified application

Species

Unspecified reactive species

Emanuele Brai,Noemi Alina Raio,Lavinia Alberi
View all publications
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