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BRAND / VENDOR: Abcam

Abcam, ab226492, Tau Research (Tau, S198, S199, S202 + T205, S214, S396, S404, S422, T231) Antibody Sampler Panel

CATALOG NUMBER: ab226492
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Product Description

Size: 1Pack
Tau Research (Tau, S198, S199, S202 + T205, S214, S396, S404, S422, T231) Antibody Sampler Panel (ab226492) is part of the multiplex kits range. Abcam offers high-quality biological reagents and tools including antibodies, proteins, assays, cell lines and lysates.
Key facts
Target:MAPTSee target data

Product details:
ab226492 is a tau research panel containing 1 recombinant mouse monoclonal antibody, 1 anti-mouse secondary antibody, 8 recombinant rabbit monoclonal antibodies and 1 anti-rabbit secondary antibody: Anti-Tau antibody, Goat Anti-Mouse IgG (H&L) (HRP), Anti-Tau (phospho S396) antibody, Anti-Tau (phospho T231) antibody, Anti-Tau (phospho S422) antibody, Anti-Tau (phospho S199) antibody, Anti-Tau (phospho S404) antibody, Anti-Tau (phospho S198) antibody, Anti-Tau (phospho S214) antibody, Anti-Tau (phospho S202 + T205) antibody, and Goat Anti-Rabbit IgG (H&L) (HRP).
Under normal circumstances, tau is a microtubule-associated protein involved in microtubule stabilization, but under pathological conditions, tau becomes hyperphosphorylated and detaches from microtubules. Phosphorylated tau then aggregates to form paired helical filaments (PHFs) and neurofibrillary tangles (NFTs).
The antibodies in this panel were selected for their exceptional performance. Please see the individual datasheets for additional information.
Explore our range of antibody sample panels designed to provide you with a variety of trial-size antibodies in a convenient and cost-effective format.
Carrier-free formulations of our recombinant antibodies are also available for easy conjugation to labels of your choice and for multiplex applications. Use our intuitive search and select carrier-free or your label of choice. For bespoke conjugations or large volumes email bespoke@abcam.com.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°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

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