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AB9674 | Anti-Tau phospho Serine 199/202 Antibody

100 µL  
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      Replacement Information

      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H WB Rb Affinity Purified Polyclonal Antibody
      Catalogue NumberAB9674
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Tau phospho Serine 199/202 Antibody
      Background InformationTau is a neuronal microtubule-associated protein found predominantly on axons and functions to promote tubulin polymerization and stabilize microtubules. Tau, in its hyperphosphorylated form, is the major component of paired helical filaments (PHF), the building block of neurofibrillary lesions in Alzheimer's disease (AD) brain. Hyperphosphorylated Tau is also found in neurofibrillary lesions in a range of other central nervous system disorders. Hyperphosphorylation impairs the microtubule binding function of Tau, resulting in the destabilization of microtubules in AD brains, ultimately leading to the degeneration of the affected neurons. Numerous serine/threonine kinases, including GSK-3beta, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II (CK2), phosphorylate Tau. Serines 199 and 202 are phosphorylated by GSK-3beta and have been linked to hereditary frontotemporal dementia. Serine 202 phosphorylation by cdk5, stimulated by the presence of microtubules, has been linked to hereditary neurodegenerative disease.
      Product Information
      FormatAffinity Purified
      PresentationAffinity purified immunoglobulin. Liquid in Dulbecco's PBS (without Mg2+ and Ca2+), pH 7.3, 50% glycerol with 1.0 mg/mL BSA and 0.05% sodium azide.
      ApplicationDetect Tau phospho Serine 199/202 using this Anti-Tau phospho Serine 199/202 Antibody validated for use in WB.
      Key Applications
      • Western Blotting
      Application NotesWestern blot: 1:1,000. Suggested blocking buffer is 5% BSA-TBST overnight at 2-8°C. Suggested antibody dilution buffer is 3% BSA-TBST. Suggested antibody incubation time is 2 hours at room temperature.

      Optimal working dilutions must be determined by the end user.
      Biological Information
      ImmunogenSynthetic peptide of amino acids surrounding the phosphoSerine 199 and 202 sites of human Tau.
      SpecificityTau phosphoSerine 199/202. The antibody recognizes Tau pSerine 199/202 in samples of recombinant human Tau treated with GSK-3beta for 45 minutes. The reactivity of the antibody is blocked with the pSerine 199/202 peptide but not the non-phosphopeptide, tau phosphopeptide corresponding to pSerine 199, tau phosphopeptide corresponding to pSerine 202 or a generic phosphoSerine-containing peptide.
      Species Reactivity
      • Human
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryThis gene encodes the microtubule-associated protein tau (MAPT) whose transcript undergoes complex, regulated alternative splicing, giving rise to several mRNA species. MAPT transcripts are differentially expressed in the nervous system, depending on stage of neuronal maturation and neuron type. MAPT gene mutations have been associated with several neurodegenerative disorders such as Alzheimer's disease, Pick's disease, frontotemporal dementia, cortico-basal degeneration and progressive supranuclear palsy.
      Gene Symbol
      • MAPT
      • MTBT2
      • MAPTL
      • PHF-tau
      • tau
      • DDPAC
      • FTDP-17
      • MGC138549
      • MSTD
      • TAU
      • FLJ31424
      • MTBT1
      • PPND
      • Phosphorylation
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P10636 # Promotes 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.
      SIZE: 758 amino acids; 78878 Da
      SUBUNIT: Interacts with PSMC2 through SQSTM1 (By similarity). Interacts with SQSTM1 when polyubiquitinated.
      SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane. Note=Mostly found in the axons of neurons, in the cytosol and in association with plasma membrane components.
      TISSUE SPECIFICITY: Expressed in neurons. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.DEVELOPMENTAL STAGE: Four-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.
      DOMAIN: SwissProt: P10636 The tau/MAP repeat binds to tubulin. Type I isoforms contain 3 repeats while type II isoforms contain 4 repeats.
      PTM: Phosphorylation at serine and threonine residues in S-P or T- P motifs by proline-directed protein kinases (PDPK: CDC2, 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.
      DISEASE: SwissProt: P10636 # 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 and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274, 172700]; also called frontotemporal dementia (FTD) 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 pallido-ponto-nigral degeneration (PPND) [MIM:168610]. The clinical features include ocular motility abnormalities, dystonia and urinary incontinence, besides progressive parkinsonism and dementia. & 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 (PSP) [MIM:601104, 260540]; also known as Steele-Richardson- Olszewski syndrome. PSP 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. & Defects in MAPT may be a cause of hereditary dysphasic disinhibition dementia (HDDD) [MIM:607485]. HDDD is a frontotemporal dementia characterized by progressive cognitive deficits with memory loss and personality changes, severe dysphasic disturbances leading to mutism, and hyperphagia.
      SIMILARITY: Contains 4 Tau/MAP repeats.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain at -20°C in undiluted for up to 6 months after date of receipt. Avoid repeated freeze/thaw cycles. Do not store in a self defrosting freezer.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      RABBIT ANTI-Tau phosphoSerine 199/202 - 2492184 2492184
      RABBIT ANTI-Tau phosphoSerine 199/202 -2567087 2567087
      RABBIT ANTI-Tau phosphoSerine 199/202 -2615046 2615046
      RABBIT ANTI-Tau phosphoSerine 199/202 -2659205 2659205
      RABBIT ANTI-Tau phosphoSerine 199/202 -2659760 2659760
      RABBIT ANTI-Tau phosphoSerine 199/202 -2670379 2670379
      RABBIT ANTI-Tau phosphoSerine 199/202 -2689091 2689091
      RABBIT ANTI-Tau phosphoSerine 199/202 -2795057 2795057
      RABBIT ANTI-Tau phosphoSerine 199/202 POLYCLONAL ANTIBODY - 2074741 2074741


      Reference overviewPub Med ID
      Modulation of tau phosphorylation and intracellular localization by cellular stress.
      Jenkins, S.M., et al.
      Biochem. J., 345:263-270 (2000) 2000

      10620503 10620503
      Phosphorylation of microtubule-associated protein tau is regulated by protein phosphatase 2A in mammalian brain. Implications for neurofibrillary degeneration in Alzheimer's disease.
      Gong, C.X., et al.
      J. Biol. Chem., 275(8):5535-5544 (2000) 2000

      10681533 10681533
      Distribution of tau protein kinase I/glycogen synthase kinase-3beta, phosphatases 2A and 2B, and phosphorylated tau in the developing rat brain.
      Takahashi, M., et al.
      Brain Res., 857(1-2):193-206 (2000) 2000

      10700568 10700568
      Expression of human apolipoprotein E4 in neurons causes hyperphosphorylation of protein tau in the brains of transgenic mice.
      Tesseur,I., et al.
      Am. J. Pathol., 156(3):951-964 (2000) 2000

      10702411 10702411
      Regulation of expression, phosphorylation and biological activity of tau during differentiation in SY5Y cells.
      Haque, N., et al.
      Brain Res., 838(1-2):69-77 (1999) 1999

      10446318 10446318
      Molecular interactions among protein phosphatase 2A, tau, and microtubules. Implications for the regulation of tau phosphorylation and the development of tauopathies.
      Sontag, E., et al.
      J. Biol. Chem., 274:25490-25498 (1999) 1999

      10464280 10464280
      Inhibition of tau phosphorylating protein kinase cdk5 prevents beta-amyloid-induced neuronal death.
      Alvarez, A., et al.
      FEBS Lett., 459:421-426 (1999) 1999

      10526177 10526177
      The microtubule binding of tau and high molecular weight tau in apoptotic PC12 cells is impaired because of altered phosphorylation.
      Davis, P.K. and G.V. Johnson
      J. Biol. Chem., 274(50):35686-35692 (1999) 1999

      10585448 10585448
      Alzheimer's disease. The tangled tale of tau.
      Mandelkow, E.
      Nature , 402(6762):588-589 (1999) 1999

      10604460 10604460

      Data Sheet

      Anti-Tau phospho Serine 199/202 - Data Sheet

      Newsletters / Publications

      Research Focus - Volume 2, 2013

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      Life Science Research > Antibodies and Assays > Primary Antibodies