05-804 | Anti-Tau (4-repeat isoform RD4) Antibody, clone 1E1/A6

05-804
200 µL  
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      Overview

      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, R, B, MIHC, WBMCulture SupernatantMonoclonal Antibody
      Description
      Catalogue Number05-804
      Brand Family Upstate
      Trade Name
      • Upstate
      DescriptionAnti-Tau (4-repeat isoform RD4) Antibody, clone 1E1/A6
      Background InformationMicrotubule Associated Proteins, or MAPS, bind to the tubulin subunits of microtubule structures and regulate their functional stability. In the cell MAPs bind to monomer and multimerized tubulin. MAP binding to multimerized tubulin further stabilizes the formation of higher order microtubulin structures. MAP binding to microtubule structures is mediated through phosporylation through Microtubule Affinity Regulated Kinase (MARK). Phosphorylation releases MAPs bound to microtubules, destabilizing the structure, driving it toward disassembly. There are predominately two MAP types, I, II. Type II MAP includes MAP2, MAP4, and tau and are found in nervous tissue. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains.
      References
      Product Information
      FormatCulture Supernatant
      Control
      • Rat brain cytosolic fraction.
      PresentationMouse monoclonal cultured supernatant containing 0.05% sodium azide.
      Frozen at -20°C.
      Applications
      ApplicationThis Anti-Tau (4-repeat isoform RD4) Antibody, clone 1E1/A6 is validated for use in IH, WB for the detection of Tau (4-repeat isoform RD4).
      Key Applications
      • Immunohistochemistry
      • Western Blotting
      Application NotesImmunohistochemistry:
      This antibody has been reported by an independent laboratory to detect Tau (4-repeat isoform RD4) in autoclaved paraffin brain sections. (De Silva, R., 2003;Togo, T., 2002)

      Differential Detection of Tauopathies: (Togo, T., 2002)
      Biological Information
      ImmunogenBovine thyroglobulin-conjugated synthetic peptide corresponding to amino acids 275-291 (VQIINKKLDLSNVQSKC) of human Tau (4-repeat isoform RD4). Region is flanking junction coded by adjacent exons 9 & 11 with the inclusion of exon 10. The immunizing sequence is identical in human, rat, mouse and bovine.
      Clone1E1/A6
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      HostMouse
      SpecificityRecognizes Tau (4-repeat isoform RD4), Mr 45-65 kDa. Higher MW band (68-72 kDa) represents phosphorylated Tau.
      IsotypeIgG
      Species Reactivity
      • Human
      • Rat
      • Bovine
      • Mouse
      Species Reactivity NoteHuman and rat. Cross-reactivity with mouse and bovine expected due to sequence homology.
      Antibody TypeMonoclonal 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
      • tau
      • FTDP-17
      • MSTD
      • TAU
      • MTBT1
      • PHF-tau
      • MGC138549
      • MAPTL
      • FLJ31424
      • DDPAC
      • PPND
      Purification MethodUnpurified
      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.
      Molecular Weight~68-72 kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceRoutinely evaluated by western blot on rat brain cytosol fraction.

      Western Blot Analysis:
      A 1:1,000-1:10,000 dilution of this lot detected Tau (4-repeat isoform RD4) in a rat brain cytosolic fraction.
      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 ConditionsStable for 1 year at -20°C from date of receipt.

      Handling Recommendations: Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance. Note: Variabillity in freezer temperatures below -20°C may cause glycerol containing solutions to become frozen during storage.
      Packaging Information
      Material Size200 µL
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      SDS

      Title

      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      Anti-Tau (4-repeat isoform RD4), clone -2823224 2823224
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 2476982
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 2876228
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 (culture supernatant) - DAM1416515 DAM1416515
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 - 2140544 2140544
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 - 2444154 2444154
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 - 0612047747 0612047747
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 - 1967298 1967298
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 - 2017306 2017306
      Anti-Tau (4-repeat isoform RD4), clone 1E1/A6 - 2068180 2068180

      References

      Reference overviewPub Med ID
      Neuropathologic analysis of Tyr69His TTR variant meningovascular amyloidosis with dementia.
      Ziskin, JL; Greicius, MD; Zhu, W; Okumu, AN; Adams, CM; Plowey, ED
      Acta neuropathologica communications  3  43  2015

      Show Abstract
      26156087 26156087
      Profiling murine tau with 0N, 1N and 2N isoform-specific antibodies in brain and peripheral organs reveals distinct subcellular localization, with the 1N isoform being enriched in the nucleus.
      Liu, C; Götz, J
      PloS one  8  e84849  2013

      Show Abstract
      24386422 24386422
      Parenchymal and vascular lesions in ageing equine brains: histological and immunohistochemical studies.
      M T Capucchio,M Márquez,P Pregel,L Foradada,M Bravo,G Mattutino,C Torre,D Schiffer,D Catalano,F Valenza,F Guarda,M Pumarola
      Journal of comparative pathology  142  2010

      Show Abstract
      19744668 19744668
      Differential involvement and heterogeneous phosphorylation of tau isoforms in progressive supranuclear palsy.
      Gibb, G M, et al.
      Brain Res. Mol. Brain Res., 121: 95-101 (2004)  2004

      Show Abstract
      14969740 14969740
      The L266V tau mutation is associated with frontotemporal dementia and Pick-like 3R and 4R tauopathy.
      Hogg, Marion, et al.
      Acta Neuropathol., 106: 323-36 (2003)  2003

      Show Abstract
      12883828 12883828
      Dementia with Lewy bodies from the perspective of tauopathy.
      Iseki, Eizo, et al.
      Acta Neuropathol., 105: 265-70 (2003)  2003

      Show Abstract
      12557014 12557014
      Pathological inclusion bodies in tauopathies contain distinct complements of tau with three or four microtubule-binding repeat domains as demonstrated by new specific monoclonal antibodies.
      de Silva, R, et al.
      Neuropathol. Appl. Neurobiol., 29: 288-302 (2003)  2003

      Show Abstract
      12787326 12787326
      The complex relationship between soluble and insoluble tau in tauopathies revealed by efficient dephosphorylation and specific antibodies
      Hanger, D P, et al
      FEBS Lett, 531:538-42 (2002)  2002

      12435607 12435607
      The slow axonal transport of the microtubule-associated protein tau and the transport rates of different isoforms and mutants in cultured neurons.
      Utton, Michelle A, et al.
      J. Neurosci., 22: 6394-400 (2002)  2002

      Show Abstract
      12151518 12151518
      Argyrophilic grain disease is a sporadic 4-repeat tauopathy
      Togo, Takashi, et al
      J Neuropathol Exp Neurol, 61:547-56 (2002)  2002

      12071638 12071638

      Newsletters / Publications

      Title
      Research Focus - Volume 2, 2013

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      Life Science Research > Antibodies and Assays > Primary Antibodies