• Product nameAnti-Tau antibody [TAU-5]
    See all Tau primary antibodies
  • Description
    Mouse monoclonal [TAU-5] to Tau
  • SpecificityThis antibody is specific to 45-68 kDa proteins identified as tau proteins and does not cross react with tubulin or other microtubule associated proteins. It reacts with phosphorylated as well as non-phosphorylated forms of tau and stains human neurofibrillary tangles, neutrophil threads and neurotic plaques associated with Alzheimer’s disease.
  • Tested applicationsIHC-P, IHC-Fr, WB, ICC/IFmore details
  • Species reactivity
    Reacts with: Mouse, Human
  • Immunogen

    Other Immunogen Type corresponding to Cow Tau. Purified bovine microtubule-associated proteins.

  • EpitopeEpitope maps in the middle of tau.
  • Positive control
    • Alzheimer brain.



Our Abpromise guarantee covers the use of ab3931 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
IHC-P Use at an assay dependent concentration. Perform enzymatic antigen retrieval before commencing with IHC staining protocol. PubMed: 22699908
IHC-Fr 1/25 - 1/50. We suggest an incubation period of 30 minutes at room temperature.
WB 1/50 - 1/100. Predicted molecular weight: 60 kDa.
ICC/IF Use at an assay dependent concentration.


  • FunctionPromotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.
  • Tissue specificityExpressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.
  • Involvement in diseaseNote=In Alzheimer disease, the neuronal cytoskeleton in the brain is progressively disrupted and replaced by tangles of paired helical filaments (PHF) and straight filaments, mainly composed of hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU).
    Defects in MAPT are a cause of frontotemporal dementia (FTD) [MIM:600274]; also called frontotemporal dementia (FTD), pallido-ponto-nigral degeneration (PPND) or historically termed Pick complex. This form of frontotemporal dementia is characterized by presenile dementia with behavioral changes, deterioration of cognitive capacities and loss of memory. In some cases, parkinsonian symptoms are prominent. Neuropathological changes include frontotemporal atrophy often associated with atrophy of the basal ganglia, substantia nigra, amygdala. In most cases, protein tau deposits are found in glial cells and/or neurons.
    Defects in MAPT are a cause of Pick disease of the brain (PIDB) [MIM:172700]. It is a rare form of dementia pathologically defined by severe atrophy, neuronal loss and gliosis. It is characterized by the occurrence of tau-positive inclusions, swollen neurons (Pick cells) and argentophilic neuronal inclusions known as Pick bodies that disproportionally affect the frontal and temporal cortical regions. Clinical features include aphasia, apraxia, confusion, anomia, memory loss and personality deterioration.
    Note=Defects in MAPT are a cause of corticobasal degeneration (CBD). It is marked by extrapyramidal signs and apraxia and can be associated with memory loss. Neuropathologic features may overlap Alzheimer disease, progressive supranuclear palsy, and Parkinson disease.
    Defects in MAPT are a cause of progressive supranuclear palsy type 1 (PSNP1) [MIM:601104, 260540]; also abbreviated as PSP and also known as Steele-Richardson-Olszewski syndrome. PSNP1 is characterized by akinetic-rigid syndrome, supranuclear gaze palsy, pyramidal tract dysfunction, pseudobulbar signs and cognitive capacities deterioration. Neurofibrillary tangles and gliosis but no amyloid plaques are found in diseased brains. Most cases appear to be sporadic, with a significant association with a common haplotype including the MAPT gene and the flanking regions. Familial cases show an autosomal dominant pattern of transmission with incomplete penetrance; genetic analysis of a few cases showed the occurrence of tau mutations, including a deletion of Asn-613.
  • Sequence similaritiesContains 4 Tau/MAP repeats.
  • Developmental stageFour-repeat (type II) tau is expressed in an adult-specific manner and is not found in fetal brain, whereas three-repeat (type I) tau is found in both adult and fetal brain.
  • DomainThe tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.
  • Post-translational
    Phosphorylation at serine and threonine residues in S-P or T-P motifs by proline-directed protein kinases (PDPK: CDK1, CDK5, GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold increase in mitosis, and in PHF-tau), and at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) in Alzheimer diseased brains. Phosphorylation decreases with age. Phosphorylation within tau's repeat domain or in flanking regions seems to reduce tau's interaction with, respectively, microtubules or plasma membrane components. Phosphorylation on Ser-610, Ser-622, Ser-641 and Ser-673 in several isoforms during mitosis.
    Polyubiquitinated. Requires functional TRAF6 and may provoke SQSTM1-dependent degradation by the proteasome (By similarity). PHF-tau can be modified by three different forms of polyubiquitination. 'Lys-48'-linked polyubiquitination is the major form, 'Lys-6'-linked and 'Lys-11'-linked polyubiquitination also occur.
    Glycation of PHF-tau, but not normal brain tau. Glycation is a non-enzymatic post-translational modification that involves a covalent linkage between a sugar and an amino group of a protein molecule forming ketoamine. Subsequent oxidation, fragmentation and/or cross-linking of ketoamine leads to the production of advanced glycation endproducts (AGES). Glycation may play a role in stabilizing PHF aggregation leading to tangle formation in AD.
  • Cellular localizationCytoplasm > cytosol. Cell membrane. Cytoplasm > cytoskeleton. Cell projection > axon. Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.
  • Information by UniProt
  • Database links
  • FormThere are 9 isoforms produced by alternative splicing.
  • Alternative names
    • AI413597 antibody
    • AW045860 antibody
    • DDPAC antibody
    • Disinhibition Dementia Parkinsonism Amyotrophy Complex antibody
    • FLJ31424 antibody
    • FTDP 17 antibody
    • FTDP17 antibody
    • G Protein Beta 1 Gamma 2 Subunit Interacting Factor 1 antibody
    • G protein beta1/gamma2 subunit interacting factor 1 antibody
    • MAPT antibody
    • MAPTL antibody
    • MGC134287 antibody
    • MGC138549 antibody
    • MGC156663 antibody
    • Microtubule Associated Protein Tau antibody
    • Microtubule associated protein tau isoform 4 antibody
    • Microtubule-associated protein tau antibody
    • MSTD antibody
    • Mtapt antibody
    • MTBT1 antibody
    • MTBT2 antibody
    • Neurofibrillary Tangle Protein antibody
    • Paired Helical Filament Tau antibody
    • Paired helical filament-tau antibody
    • PHF Tau antibody
    • PHF-tau antibody
    • PPND antibody
    • PPP1R103 antibody
    • Protein phosphatase 1, regulatory subunit 103 antibody
    • pTau antibody
    • RNPTAU antibody
    • TAU antibody
    • TAU_HUMAN antibody
    • Tauopathy and respiratory failure, included antibody
    see all

Anti-Tau antibody [TAU-5] images

  • Immunofluorescence analysis of Human primary culture neurons, either untreated (left) or treated with 500 nM quinolinic acid (right).

    Tau (red) was stained using ab3931. An AlexaFluor®594-conjugated goat anti-mouse IgG  (ab150116) was used as the secondary antibody. Nuclei were stained with DAPI (blue).

References for Anti-Tau antibody [TAU-5] (ab3931)

This product has been referenced in:
  • Vanderweyde T  et al. Contrasting pathology of the stress granule proteins TIA-1 and G3BP in tauopathies. J Neurosci 32:8270-83 (2012). IHC-P . Read more (PubMed: 22699908) »
  • Cronin T  et al. The disruption of the rod-derived cone viability gene leads to photoreceptor dysfunction and susceptibility to oxidative stress. Cell Death Differ 17:1199-210 (2010). Mouse . Read more (PubMed: 20139892) »

See all 4 Publications for this product

Product Wall

I have just issued a credit for the Abcam Tau antibody, ab3931.

Regarding the differences among the quality of antibodies prepared from the same clone, this is either a consequence of differences in the production method (for example, tissue...

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Thank you for providing the details of your protocol. I am sorry to read that the antibody is still failing with your samples and your protocol. I am sending a vial from a different batch, as requested, in the hope that this one will give the result yo...

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I'm afraid we do not have further information regarding what types of Tau are recognised by ab3931. I'm sorry we couldn't help you more on this occasion,

This antibody maps to the sequence 210-241 of tau. This is information is provided in the following publication: Lopresti P, et. al. 91995) Proc Natl Acad Sci USA, 92:10369-10373.

This antibody maps to the sequence 210-241 of tau. This is information is provided in the following publication: Lopresti P, et. al. 91995) Proc Natl Acad Sci USA, 92:10369-10373.

Yes, ab3931 recognizes all 6 isoforms of tau. If you have any more questions, please contact us again.

All the information we have on species cross reactivity is specified on the datasheet. To our knowledge, cross reactivity with Rat or Mouse has not yet been tested. Should you decide to go ahead and purchase this product, please let us know how you get...

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500ul of this antibody contains 50ug of antibody. Currently, we do not plan to produce any more anti-tau antibodies than are on the website already.