Overview

  • Product nameAnti-Tau (phospho S262) antibodySee all Tau primary antibodies ...
  • Description
    Rabbit polyclonal to Tau (phospho S262)
  • SpecificityPhosphorylation site-specific antibody selective for the phosphorylated form of human tau containing a phosphate on serine 262.
  • Tested applicationsWB more details
  • Species reactivity
    Reacts with: Human
    Predicted to work with: Rat, Goat, Cow, Monkey, Baboon
  • Immunogen

    Synthetic peptide (Human) derived from the region of human tau that contains serine 262.

  • Positive control
    • Recombinant human Tau or African green monkey kidney (CV-1) cells, stably expressing human four repeat tau and SV40 small T antigen to induce specific inhibition of PP2A.

Properties

Applications

Our Abpromise guarantee covers the use of ab4856 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
  • Application notesWB: 1/1000. Predicted molecular weight: 62 kDa. Can be blocked with Tau peptide - phospho S262 (phospho and non-phospho pair).

    Not tested in other applications.
    Optimal dilutions/concentrations should be determined by the end user.
  • 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 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
      • pTau antibody
      • RNPTAU antibody
      • TAU antibody
      • TAU_HUMAN antibody
      • Tauopathy and respiratory failure, included antibody
      see all

    Anti-Tau (phospho S262) antibody images



    • Predicted band size : 62 kDa


      Cell extracts from African green monkey kidney (CV-1) cells, stably expressing human four repeat tau and a protein phosphatase inhibitor, were resolved by SDS-PAGE on a 10% Tris-glycine gel. The proteins were transferred to nitrocellulose. Membranes were incubated with 0.50 µg/mL ab4856, following prior incubation in the absence (1) or presence of the peptide immunogen (2), or the non-phosphopeptide corresponding to the tau phosphopeptide (3). After washing, membranes were incubated with goat (ab’)2 anti-rabbit IgG alkaline phosphatase and bands were detected using the Tropix WesternStar detection method. The data show that only the phosphopeptide corresponding to this site blocks the antibody signal, illustrating the specificity of ab4856 antibody for this phosphorylation site.


    • Predicted band size : 62 kDa


      WB using ab4856. The peptide corresponding to Tau [pS262] blocks the antibody signal, thereby demonstrating the specificity of the antibody.

    References for Anti-Tau (phospho S262) antibody (ab4856)

    This product has been referenced in:
    • Allyson J  et al. Blockade of NR2A-containing NMDA receptors induces Tau phosphorylation in rat hippocampal slices. Neural Plast 2010:340168 (2010). WB ; Rat . Read more (PubMed: 20508838) »

    See 1 Publication for this product

    Product Wall

    Thank you for your enquiry. I have contacted the originator of the product for the peptide information but unfortunately, the information is proprietary and cannot be released. I am sorry I can't be of more assistance in this occasion but should...

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    Thank you for your enquiry. The Tau antibody concentration is 0.25 mg/mL. Please let me know if I can help further.

    Thank you for your enquiry. The concentration of the lot that you received is 0.25 mg/ml. This antibody has been optimized to work in Western blotting at a dilution of 1:1000. If you have any additional questions, please contact us again.

    Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"