Rabbit Polyclonal TAU phospho T181 antibody. Suitable for WB, IHC-P and reacts with Mouse, Rat samples. Cited in 9 publications. Immunogen corresponding to Synthetic Peptide within Human MAPT phospho T181.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
WB | IHC-P | |
---|---|---|
Mouse | Tested | Expected |
Rat | Expected | Tested |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info 1/500 - 1/1000 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info Use at an assay dependent concentration. | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Rat | Dilution info 1/50 - 1/100 | Notes - |
Species | Dilution info | Notes |
---|---|---|
Species Mouse | Dilution info Use at an assay dependent concentration. | Notes - |
Select an associated product type
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.
MAPT phospho T181
MAPTL, MTBT1, TAU, MAPT, Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau
Rabbit Polyclonal TAU phospho T181 antibody. Suitable for WB, IHC-P and reacts with Mouse, Rat samples. Cited in 9 publications. Immunogen corresponding to Synthetic Peptide within Human MAPT phospho T181.
pH: 7.4
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
ab75679 detects endogenous levels of isoform Tau-F, which is a truncated form of the unprocessed precursor isoform PNS-tau (http://www.uniprot.org/uniprot/P10636)), where the phosphorylation site is located at threonine 181.
The specificity of this antibody refers to P10636-8.
ab75679 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against non-phosphopeptide was removed by chromatogramphy using non-phosphopeptide corresponding to the phosphorylation site.
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.
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.
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.
We have tested this species and application combination and it works. It is covered by our product promise.
We have not tested this specific species and application combination in-house, but expect it will work. It is covered by our product promise.
This species and application combination has not been tested, but we predict it will work based on strong homology. However, this combination is not covered by our product promise.
We do not recommend this combination. It is not covered by our product promise.
We are dedicated to supporting your work with high quality reagents and we are here for you every step of the way should you need us.
In the unlikely event of one of our products not working as expected, you are covered by our product promise.
Full details and terms and conditions can be found here:
Terms & Conditions.
ab75679 at 1/50 dilution staining Tau in rat hippocampal region tissue from a model with Alzheimer’s Disease by Immunohistochemistry, Paraffin-embedded tissue.
All lanes: Western blot - Anti-Tau (phospho T181) antibody (ab75679) at 1/500 dilution
Lane 1: mouse brain tissue extracts with immunising peptide
Lane 2: mouse brain tissue extracts
Predicted band size: 78 kDa
Observed band size: 35 kDa, 46 kDa
Image collected and cropped by CiteAb under a CC-BY license from the publication
Tau (phospho T181) western blot using anti-Tau (phospho T181) antibody ab75679. Publication image and figure legend from Qi, B., Yang, Y., et al., 2020, Mol Brain, PubMed 32272942.
ab75679 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab75679 please see the product overview.
CBD3 expression reduces Aβ1–42 and p-tau plaques. Representative western blots of lysates (n = 4) from the indicated conditions probed with antibodies against ADAM10, Aβ1–42, p-tau, t-tau, or GAPDH (housekeeping/loading control). The hippocampal tissues were from wildtype (WT) mice, APP/PS1 mice, APP/PS1 mice administered control AAV, or APP/PS1 mice administered CBD3 harboring AAV. Quantification of levels of Aβ1–42 (b), p-tau/t-tau (c), and ADAM10 (d) normalized to control (n = 4 per condition). *P < 0.05, one-way ANOVA with Dunnett’s post-hoc test. n.s., not significant.
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com