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AB4749

Anti-Tau (phospho S199) antibody

5

(1 Review)

|

(8 Publications)

Rabbit Polyclonal TAU phospho S199 antibody. Suitable for WB, IHC-P and reacts with African green monkey, Mouse, Human samples. Cited in 8 publications. Immunogen corresponding to Synthetic Peptide within Human MAPT phospho S199.

View Alternative Names

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

3 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Tau (phospho S199) antibody (AB4749)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Tau (phospho S199) antibody (AB4749)

Paraffin embedded human brain tissue (right) stained for Tau using ab4749 at 1/100 dilution in immunohistochemical analysis. Negative control without primary antibody (left).

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Tau (phospho S199) antibody (AB4749)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Tau (phospho S199) antibody (AB4749)

Paraffin embedded mouse brain tissue (right) stained for Tau using ab4749 at 1/100 dilution in immunohistochemical analysis. Negative control without primary antibody (left).

Western blot - Anti-Tau (phospho S199) antibody (AB4749)
  • WB

Unknown

Western blot - Anti-Tau (phospho S199) antibody (AB4749)

Cell extracts from African green monkey kidney (CV-1) cells, stably expressing human four repeat tau and a protein phosphatase inhibitor, were resolved by SDS-PAGE on a 10% Tris-glycine gel. The proteins were transferred to nitrocellulose. Membranes were incubated with 0.50 μg/mL anti-phospho tau [pS199] (ab4749), following prior incubation in the absence (a) or presence of the peptide immunogen (b), or the nonphosphopeptide corresponding to the tau phosphopeptide (c). Cell extracts from African green monkey kidney (CV-1) cells, stably expressing human four repeat tau and a protein phosphatase inhibitor, were resolved by SDS-PAGE on a 10% Tris-glycine gel. The proteins were transferred to nitrocellulose. Membranes were incubated with 0.50 µg/mL anti-phospho tau [pS199] (ab4749), following prior incubation in the absence (a) or presence of the peptide immunogen (b), or the nonphosphopeptide corresponding to the tau phosphopeptide (c).

All lanes:

Western blot - Anti-Tau (phospho S199) antibody (ab4749)

Predicted band size: 78 kDa

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Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human, African green monkey

Applications

WB, IHC-P

applications

Immunogen

Synthetic Peptide within Human MAPT phospho S199. 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 serine 199.
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 S199

Additional targets

MAPT phospho S199
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Publications (8)

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

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

Frontiers in molecular neuroscience 15:852368 PubMed35359570

2022

Hyperphosphorylated Human Tau Accumulates at the Synapse, Localizing on Synaptic Mitochondrial Outer Membranes and Disrupting Respiration in a Mouse Model of Tauopathy.

Applications

Unspecified application

Species

Unspecified reactive species

Andrew J Trease,Joseph W George,Nashanthea J Roland,Eliezer Z Lichter,Katy Emanuel,Steven Totusek,Howard S Fox,Kelly L Stauch

Molecular neurodegeneration 16:78 PubMed34809709

2021

CCR5 antagonist reduces HIV-induced amyloidogenesis, tau pathology, neurodegeneration, and blood-brain barrier alterations in HIV-infected hu-PBL-NSG mice.

Applications

Unspecified application

Species

Unspecified reactive species

Biju Bhargavan,Shawna M Woollard,Jo Ellyn McMillan,Georgette D Kanmogne

Scientific reports 11:20075 PubMed34625606

2021

Hypermethylation of Mest promoter causes aberrant Wnt signaling in patients with Alzheimer's disease.

Applications

Unspecified application

Species

Unspecified reactive species

Renuka Prasad,Hwajin Jung,Anderson Tan,Yonghee Song,Sungho Moon,Mohammed R Shaker,Woong Sun,Junghee Lee,Hoon Ryu,Hyun Kook Lim,Eek-Hoon Jho

Frontiers in neuroscience 14:585476 PubMed33328854

2020

Electroacupuncture Protects Cognition by Regulating Tau Phosphorylation and Glucose Metabolism via the AKT/GSK3β Signaling Pathway in Alzheimer's Disease Model Mice.

Applications

Unspecified application

Species

Unspecified reactive species

Anping Xu,Qingtao Zeng,Yinshan Tang,Xin Wang,Xiaochen Yuan,You Zhou,Zhigang Li

Experimental & molecular medicine 49:e333 PubMed28524178

2017

Transcriptome analyses of chronic traumatic encephalopathy show alterations in protein phosphatase expression associated with tauopathy.

Applications

ICC/IF, WB, IHC-P

Species

Human, Human, Human

Jeong-Sun Seo,Seungbok Lee,Jong-Yeon Shin,Yu Jin Hwang,Hyesun Cho,Seong-Keun Yoo,Yunha Kim,Sungsu Lim,Yun Kyung Kim,Eun Mi Hwang,Su Hyun Kim,Chong-Hyun Kim,Seung Jae Hyeon,Ji-Young Yun,Jihye Kim,Yona Kim,Victor E Alvarez,Thor D Stein,Junghee Lee,Dong Jin Kim,Jong-Il Kim,Neil W Kowall,Hoon Ryu,Ann C McKee

Journal of Alzheimer's disease : JAD 35:525-39 PubMed23478312

2013

Natural cannabinoids improve dopamine neurotransmission and tau and amyloid pathology in a mouse model of tauopathy.

Applications

IHC-P

Species

Mouse

Maria J Casarejos,Juan Perucho,Ana Gomez,Maria P Muñoz,Marian Fernandez-Estevez,Onintza Sagredo,Javier Fernandez Ruiz,Manuel Guzman,Justo Garcia de Yebenes,Maria A Mena

Neurobiology of disease 39:423-38 PubMed20546895

2010

Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation.

Applications

Unspecified application

Species

Unspecified reactive species

Jose A Rodríguez-Navarro,Laura Rodríguez,María J Casarejos,Rosa M Solano,Ana Gómez,Juan Perucho,Ana María Cuervo,Justo García de Yébenes,María A Mena
View all publications
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