RabMAb

Anti-Tau (phospho S422) antibody [EPR2866] (ab79415)

Overview

  • Product nameAnti-Tau (phospho S422) antibody [EPR2866]See all Tau primary antibodies ...
  • Description
    Rabbit monoclonal [EPR2866] to Tau (phospho S422)
  • Specificityab79415 only detects Tau phosphorylated on serine 422.
  • Tested applicationsWB more details
  • Species reactivity
    Reacts with: Human

    Does not react with

    Mouse, Rat
  • Immunogen

    A phospho-specific peptide corresponding to residues surrounding serine 422 of Human Tau.

  • Positive control
    • SH-SY5Y cell lysate treated with Okadiac acid and calyculin A.
  • General notes

    Produced under U.S. Patent No. 5,675,063. A 40 μl trial size is available to purchase for this antibody.

Properties

Applications

Our Abpromise guarantee covers the use of ab79415 in the following tested applications.

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

Application Notes
WB 1/10000 - 1/20000. Detects a band of approximately 50-70 kDa (predicted molecular weight: 79 kDa).
  • Application notesIs unsuitable for Flow Cyt,IHC-P or IP.
  • 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
      modifications
      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.
    • 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
    • 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, isoform 4 antibody
      • Microtubule-associated protein tau antibody
      • MSTD antibody
      • MTAPT antibody
      • MTBT 1 antibody
      • MTBT 2 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
      • pTau antibody
      • RNPTAU antibody
      • TAU antibody
      • TAU_HUMAN antibody
      • Tauopathy and respiratory failure, included antibody
      see all

    Anti-Tau (phospho S422) antibody [EPR2866] images

    • All lanes : Anti-Tau (phospho S422) antibody [EPR2866] (ab79415) at 1/20000 dilution

      Lane 1 : SH-SY5Y cell lysates
      Lane 2 : SH-SY5Y cell lysates treated with Okadiac acid and calyculin A

      Lysates/proteins at 10 µg per lane.

      Secondary
      HRP labelled goat anti-rabbit at 1/2000 dilution

      Predicted band size : 79 kDa
      Observed band size : 55 kDa (why is the actual band size different from the predicted?)

    References for Anti-Tau (phospho S422) antibody [EPR2866] (ab79415)

    ab79415 has not yet been referenced specifically in any publications.

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