Abcam, ab80579, Anti-Tau antibody [TAU-5] - BSA and Azide free

Size: 100µg
Anti-Tau antibody [TAU-5] - BSA and Azide free (ab80579) is a mouse recombinant monoclonal antibody provided in a PBS only buffer for easy conjugation detecting Tau in Western Blot, ICC/IF . Suitable for Human, Mouse, Rat . - BSA, sodium azide, and glycerol-free for easy conjugation - Biophysical QC for unrivalled batch-batch consistency - Over 150 publications - Trusted since 2009
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:TAU-5,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:Yes,
Reacts with:Mouse, Rat, Human,
Applications:WB, ICC/IFSee 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.,
Epitope:The epitope has been mapped to the Human tau sequence 218-225 (doi:10.1016/j.bbrc.2007.04.187),
Specificity:The specificity of this antibody refers to P29172.

Product details:
Product Specifications
Anti-Tau antibody [TAU-5] - BSA and Azide free (ab80579) is a mouse recombinant monoclonal antibody and is provided in a carrier-free, conjugation ready format. ab80579 is validated in ICC/IF, WBin human, mouse, rat samples. Carrier-free antibodies are compatible with our best-in-class range of Lightning-Link® conjugation kits.
Anti-Tau antibody [TAU-5] - BSA and Azide free (ab80579) specifically detects Tau (UniProt ID: P29172; Molecular weight: 46kDa) and is sold in 100 µg selling sizes.
Quality and Validation
Antibody clone TAU-5 has been cited over 150 times in peer reviewed journals and is trusted by the scientific community.
Anti-Tau antibody [TAU-5] - BSA and Azide free (ab80579) has 5 independent reviews from customers.
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of extensively validated recombinant antibodies and assays sensitive to Tau, Beta-amyloid, and other Alzheimer’s targets of interest, with everything you need in one place.
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, Storage buffer-Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, 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

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.