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AB4842

Anti-Tau (phospho T212) antibody

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(6 Publications)

Rabbit Polyclonal TAU phospho T212 antibody. Suitable for ICC/IF and reacts with Human samples. Cited in 6 publications. Immunogen corresponding to Synthetic Peptide within Human MAPT phospho T212.

View Alternative Names

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

1 Images
Immunocytochemistry/ Immunofluorescence - Anti-Tau (phospho T212) antibody (AB4842)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-Tau (phospho T212) antibody (AB4842)

SHSY5Y cells stained for Tau (green) using ab4842 at 1μg/mL in ICC/IF. Followed by Alexa Fluor 488 Goat Anti-Rabbit IgG Secondary Antibody at 1/400 dilution for 45 minutes at room temperature (Panel a). Nuclei (Panel b : blue) were stained with SlowFade® Gold Antifade Mountant with DAPI. F-actin (Panel c : red) was stained with Alexa Fluor 594 Phalloidin. Panel d is a merged image showing nuclear and cytoplasmic localization. Panel e is a no primary antibody control.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

ICC/IF

applications

Immunogen

Synthetic Peptide within Human MAPT phospho T212. The exact immunogen used to generate this antibody is proprietary information.

P10636

Specificity

Phosphorylation site-specific antibody selective for the phosphorylated form of human tau containing a phosphate on threonine 212.

The specificity of this antibody refers to P10636-8.

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "ICCIF" : {"fullname" : "Immunocytochemistry/ Immunofluorescence", "shortname":"ICC/IF"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "ICCIF-species-checked": "testedAndGuaranteed", "ICCIF-species-dilution-info": "1 µg/mL", "ICCIF-species-notes": "<p></p>" } } }
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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 212.
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 T212
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Publications (6)

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 physiology 10:110 PubMed30837891

2019

Increased Ratio of Global -GlcNAcylation to Tau Phosphorylation at Thr212 Site Is Associated With Better Memory Function in Patients With Type 2 Diabetes.

Applications

Unspecified application

Species

Unspecified reactive species

Rong Huang,Sai Tian,Jing Han,Rongrong Cai,Hongyan Lin,Dan Guo,Jiaqi Wang,Shaohua Wang

Scientific reports 8:17702 PubMed30531974

2018

Phosphorylation of nuclear Tau is modulated by distinct cellular pathways.

Applications

Unspecified application

Species

Unspecified reactive species

Giorgio Ulrich,Agnese Salvadè,Paul Boersema,Tito Calì,Chiara Foglieni,Martina Sola,Paola Picotti,Stéphanie Papin,Paolo Paganetti

The Journal of cell biology 216:3161-3178 PubMed28877993

2017

Stabilization of dynamic microtubules by mDia1 drives Tau-dependent Aβ synaptotoxicity.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaoyi Qu,Feng Ning Yuan,Carlo Corona,Silvia Pasini,Maria Elena Pero,Gregg G Gundersen,Michael L Shelanski,Francesca Bartolini

Journal of cell science 122:2424-35 PubMed19549690

2009

Nonprimed and DYRK1A-primed GSK3 beta-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons.

Applications

WB

Species

Unspecified reactive species

Timothy M E Scales,Shen Lin,Michaela Kraus,Robert G Goold,Phillip R Gordon-Weeks

Journal of Alzheimer's disease : JAD 16:341-50 PubMed19221424

2009

Alzheimer's disease-specific tau phosphorylation is induced by herpes simplex virus type 1.

Applications

ICC/IF

Species

Human

Matthew A Wozniak,Alison L Frost,Ruth F Itzhaki
View all publications
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Product promise

We are committed to supporting your work with high-quality reagents, and we're here for you every step of the way. In the unlikely event that one of our products does not perform as expected, you're protected by our Product Promise.
For full details, please see our Terms & Conditions
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