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BRAND / VENDOR: Abcam

Abcam, ab92627, Anti-Tau (phospho S262 + T263) antibody [EPR2454]

CATALOG NUMBER: ab92627
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Product Description

Size: 20µL / 100µL / 1mL
Rabbit Recombinant Monoclonal TAU phospho S262 + T263 antibody. Suitable for ELISA, Dot, WB and reacts with Synthetic peptide, Human samples. Cited in 13 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR2454,
Isotype:IgG,
Carrier free:No,
Reacts with:Human,
Applications:WB, Dot, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:WB band is consistent with what is found in PMID 16682510 (Peng et. al.)The specificity of this antibody refers to P10636-8.

Product details:
Species reactivity
Mouse, Rat: We have preliminary internal testing data to indicate this antibody may not react with these species.
Please
contact us
for more information.
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Storage information-Stable for 12 months at -20°C

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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Collaboration

Tony Tang

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