Overview
- Product nameAnti-Tau antibody [E178]See all Tau primary antibodies ...
- DescriptionRabbit monoclonal [E178] to Tau
- Tested applicationsIHC-P, WB, ICC, IP more details
- Species reactivityReacts with: Mouse, Rat, Human
Predicted to work with: Cow - Immunogen
A synthetic peptide corresponding to 20 amino acids within Human Tau.
- Positive controlWB: SH-SY5Y cell lysate. IHC-P: Human brain.
- General notesProduced under U.S. Patent No. 5,675,063.
Properties
- FormLiquid
- Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
- Storage bufferPBS 49%,Sodium azide 0.01%,Glycerol 50%,BSA 0.05%
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Concentration information loading... - Clonality Monoclonal
- Clone numberE178
- IsotypeIgG
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Research Areas
Applications
Our Abpromise guarantee covers the use of ab32057 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
| Application | Notes |
|---|---|
| IHC-P | IHC-P: 1/500 - 1/1000. Perform heat mediated antigen retrieval before commencing with IHC staining protocol. |
| WB | WB: 1/5000. Predicted molecular weight: 79 kDa. |
| ICC | ICC: 1/250. |
| IP | IP: 1/100. |
Target
- 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
modificationsPhosphorylation 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.
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Database links
- Entrez Gene: 281296 Cow
- Entrez Gene: 4137 Human
- Entrez Gene: 17762 Mouse
- Entrez Gene: 29477 Rat
- Omim: 157140 Human
- SwissProt: P29172 Cow
- SwissProt: P10636 Human
- SwissProt: P10637 Mouse
- SwissProt: P19332 Rat
- Unigene: 101174 Human
- Unigene: 1287 Mouse
- Unigene: 2455 Rat
see all
Target information above from: UniProt accession
P10636
The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010)
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Alternative names
- AI413597 antibodyAW045860 antibodyDDPAC antibody
- Disinhibition Dementia Parkinsonism Amyotrophy Complex antibodyFLJ31424 antibodyFTDP 17 antibodyFTDP17 antibodyG Protein Beta 1 Gamma 2 Subunit Interacting Factor 1 antibodyG protein beta1/gamma2 subunit interacting factor 1 antibodyMAPT antibodyMAPTL antibodyMGC134287 antibodyMGC138549 antibodyMGC156663 antibodyMicrotubule Associated Protein Tau antibodyMicrotubule associated protein tau isoform 4 antibodyMicrotubule-associated protein tau antibodyMSTD antibodyMtapt antibodyMTBT1 antibodyMTBT2 antibodyNeurofibrillary Tangle Protein antibodyPaired Helical Filament Tau antibodyPaired helical filament-tau antibodyPHF Tau antibodyPHF-tau antibodyPPND antibodypTau antibodyRNPTAU antibodyTAU antibodyTAU_HUMAN antibodyTauopathy and respiratory failure, included antibody
see all
Anti-Tau antibody [E178] images
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Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Tau antibody [E178] (ab32057)Carl Hobbs, King`s College London, United KingdomImmunohistochemistical detection of Tau antibody [E178] (ab32057) on formaldehyde fixed paraffin-embedded rat tongue sectionsAntigen retrieval step: Heat mediated. Buffer Used: Citric acid pH6. Permeabilization: None. Primary antibody incubated at 1/1000 for 2 hours @ 21°C in TBS/BSA/azide. Secondary antibody: anti Rabbit IgG Conjugated to Biotin (1/200). A strong pattern of immunostaining which appears to be mostly localised to nerve fibres and their cell bodies (Islet of Langerhans cells are also positive). In submitted image of central area of tongue coloured arrowheads indicate features: red for nerves cut in cross-section (T/S), each brown dot representing a single axon green for what appears to me to be small nerve fibres wrapping around a partial muscle fibre black for a Ganglion containing seven positive nerve cell bodies. Surrounding these are collagen fibres (C), adipocytes (A) and skeletal/striated muscle fibres in L/S ( M- showing blue myocyte nuclei arranged around the periphery of each fibre).
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Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Tau antibody [E178] (ab32057)Carl Hobbs, King`s College London, United KingdomImmunohistochemistical detection of Tau antibody [E178] (ab32057) on formaldehyde-fixed paraffin-embedded human salivary gland sections. Antigen retrieval step: Heat mediated. Buffer Used: Citric acid pH6. Permeabilization: No. Blocking step: 1% BSA for 10 mins @ 21°C. ab32057 incubated at 1/1000 for 2 hours @ 21°C in TBS/BSA/azide. Secondary antibody: anti rabbit IgG conjugated to Biotin (1/200). NB: An interesting pattern of positivity that seems to be supported by the Human Protein Atlas. Coloured arrowheads in the submitted image indicate features: red for positive serous glands, blue for positive intra-lobular collecting ducts, black for negative mucous glands (there is a serous demilune around this acinus), yellow for intralobular collecting ducts, green for nerve tracks in the interlobular areas, blue for positive interlobular collecting ducts. There appears to be a population of positive nuclei but this may be due to the fact that ab32057 @ 1/1000 gives a positivity that is too strong (should be further diluted).
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Ab32057, at a dilution of 1/500, staining Tau in paraffin embedded human brain sections by Immunohistochemistry.
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All lanes : Anti-Tau antibody [E178] (ab32057) at 1/1000 dilution
Lane 1 : Untreated SH-SY5Y cell lysate
Lane 2 : SH-SY5Y cell lysate SH SY5Y cell lysate treated with Oka/CalA. Cells are serum-starved overnight, and then treated with 1nM calyculin A and 500nM Okadaic acid for 2 hours at 37°C.
Predicted band size : 79 kDa
References for Anti-Tau antibody [E178] (ab32057)
This product has been referenced in:
- Manczak M & Reddy PH Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage. Hum Mol Genet 21:2538-47 (2012). WB ; Human . Read more (PubMed: 22367970) »
- Manczak M & Reddy PH Abnormal interaction of VDAC1 with amyloid beta and phosphorylated tau causes mitochondrial dysfunction in Alzheimer's disease. Hum Mol Genet 21:5131-46 (2012). IP ; Human, Mouse . Read more (PubMed: 22926141) »

![Immunohistochemistry (Paraffin-embedded sections) - Anti-Tau antibody [E178] (ab32057) Immunohistochemistry (Paraffin-embedded sections) - Anti-Tau antibody [E178] (ab32057)](http://a.abcam.com/ps/datasheet/Images/32/ab32057/ab32057_1.jpg)
![Western blot - Anti-Tau antibody [E178] (ab32057) Western blot - Anti-Tau antibody [E178] (ab32057)](http://a.abcam.com/ps/datasheet/images/32/ab32057/Tau-Primary-antibodies-ab32057-10.jpg)