Anti-Tau antibody [SP70] (ab93726)

Overview

• Product nameAnti-Tau antibody [SP70]See all Tau primary antibodies ...
• Description
  Rabbit monoclonal [SP70] to Tau
• Tested applicationsIHC-P more details
• Species reactivity
  Reacts with: Human
  
• Immunogen

  Synthetic peptide from the N terminal region of Human Tau.

• Positive controlBreast carcinoma tissue.

Properties

• FormLiquid
• Storage instructionsStore at +4°C.
• Storage bufferPreservative: 0.1% Sodium Azide
  Constituents: BSA, 10mM PBS, pH 7.4
• Concentration information loading...
• PurityIgG fraction
• Clonality Monoclonal
• Clone numberSP70
• IsotypeIgG
• Research Areas
  • Signal Transduction
  • Cytoskeleton / ECM
  • Cytoskeleton
  • Microtubules
  • MT Associated Proteins
  • Tau

  • Neuroscience
  • Cell Type Marker
  • Neuron marker
  • Axon marker

  • Neuroscience
  • Neurology process
  • Neurodegenerative disease
  • Other

  • Neuroscience
  • Neurology process
  • Neurodegenerative disease
  • Alzheimer's disease
  • Tangles & Tau

Applications

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.

Target information above from: UniProt accession P10636 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 4137 Human
  • Omim: 157140 Human
  • SwissProt: P10636 Human
  • Unigene: 101174 Human

• Alternative names
  AI413597 antibodyAW045860 antibodyDDPAC antibody

  FLJ31424 antibodyFTDP 17 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

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Anti-Tau antibody [SP70] images

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  Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Tau antibody [SP70] (ab93726)
  ab93726 at 1/100 dilution staining Tau in formalin-fixed, paraffin-embedded Human breast carcinoma tissue.