15-202 | Alzheimer's Disease I - Tauopathy Investigator Antibody Mini-Pack

Immunoblot Analysis:
Cat. # AB9560SP can detect WWOX at 1:5000 dilution on e13 mouse brain Lysate.
Immunoblot Analysis:
Cat. # AB9560SP can detect WWOX at 1:5000 dilution on e13 mouse brain Lysa
3 vials/Pk  
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      Catalogue Number 15-202
      Brand Family Upstate
      Synonyms Neurofibrillary Tangle Protein WW domain-containing oxioreductase
      Trade Name
      • Upstate
      Description Alzheimer's Disease I - Tauopathy Investigator Antibody Mini-Pack
      Background Information Pathway Investigator Antibody MiniPack:
      Each Pathway Explorer Antibody Minipack contains three related antibodies as part of a signaling cascade or a combination of total and phosphorylated forms of key signaling targets. Each of the three antibodies are 30% the original pack size. Full size versions of each of the Pathway Explorer antibodies are available for sale individually under the same catalog number with the removal of “SP” off of each one (e.g. 05-591SP can be ordered as 05-591).

      Anti-Tau-1, clone PC1C6
      Cellular and subcellular localization: In situ, anti-tau-1 has a stringent specificity for the axons of neurons. The antibody does not stain the cell bodies or dendrites of neurons, nor does it stain any other cell type (4). However, this in vivo intracellular specificity is not maintained in culture: anti-tau-1 stains the axon, cell bodies, and dendrites of rat hippocampal neurons grown in culture (5). The specificity of anti-tau-1 was originally thought to represent the restricted expression of tau to axons. Later studies revealed that this specificity is dependant on the state of phosphorylation. In dephosphorylated samples (samples treated with alkaline phosphatase) anti-tau-1 stains astrocytes, perineuronal glial cells, and the axons, cell bodies and dendrites of neurons, while in untreated samples, anti-tau-1 stains only axons (6). (The epitope recognized by anti-tau-1 is probably at or near a phosphorylated site).

      Anti-Tau phospho Threonine 231
      Tau 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-3β, protein kinase A (PKA), cyclin-dependent kinase 5 (cdk5) and casein kinase II (CK2), phosphorylate Tau. Threonine 231 is phosphorylated by GSK-3β, cdk5 and cdk1 and has been shown to be involved in the pre-tangle process of AD.

      WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 2 WW domains and a short-chain dehydrogenase/reductase domain (SRD). WW domain-containing oxidoreductase WWOX, also known as WOX1 or FOR, is a proapoptotic protein and a tumor suppressor gene. Because mutation or deletion in the coding region of WWOX is rarely found, it is speculated that the appearance of aberrant transcripts affects progression of many cancers. In addition, protein levels of WWOX, its Tyr33-phosphorylated form, and WOX2 are significantly down-regulated in the neurons of Alzheimer's hippocampi.

      *See full size versions for corresponding references.
      Product Information
      • AB9560SP Anti-WWOX; 30 µg
      • MAB3420SP Anti-Tau-1, clone PC1C6; 30 µg
      • AB9668SP Anti-Tau phospho Threonine 231; 30 µL
      Presentation 3 individual tubes containing either Anti-WWOX; Anti-Tau phospho Threonine 231; or Anti-Tau-1, clone PC1C6
      Properties Each vial is 30% the size of the parent catalog number
      Application This Antibody pack contains Anti-WWOX Antibody, Anti-Tau phospho Threonine 231 Antibody, Anti-Tau-1 Antibody.
      Biological Information
      Cross Reactivity Varies. See individual Data Sheets
      Entrez Gene Number
      Entrez Gene Summary Tau: This 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.

      WWOX: WW domain-containing proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as protein degradation, transcription, and RNA splicing. This gene encodes a protein which contains 2 WW domains and a short-chain dehydrogenase/reductase domain (SRD). The highest normal expression of this gene is detected in hormonally regulated tissues such as testis, ovary, and prostate. This expression pattern and the presence of an SRD domain suggest a role for this gene in steroid metabolism. The encoded protein is more than 90% identical to the mouse protein, which is an essential mediator of tumor necrosis factor-alpha-induced apoptosis, suggesting a similar, important role in apoptosis for the human protein. In addition, there is evidence that this gene behaves as a suppressor of tumor growth. Alternative splicing of this gene generates transcript variants that encode different isoforms.
      Gene Symbol
      • MAPT
      • PRO0128
      • FRA16D
      • HHCMA56
      • D16S432E
      • WOX1
      • FOR
      • WWOX
      • PPND
      • MGC138549
      • DDPAC
      • PHF-tau
      • MTBT1
      • FLJ31424
      • MSTD
      • FTDP-17
      • tau
      • MAPTL
      • MTBT2
      UniProt Number
      UniProt Summary FUNCTION: 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.
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      Material Size 3 vials/Pk
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