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AB2286 | Anti-Amyloid Fibrils OC Antibody

AB2286
100 µL  
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      Replacement Information

      Ofertas especiais

      Tabela com principais espec.

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H IP, ICC, IHC, ELISA, WB, DB Rb Serum Polyclonal Antibody
      Description
      Catalogue NumberAB2286
      Trade Name
      • Chemicon
      DescriptionAnti-Amyloid Fibrils OC Antibody
      Alternate Names
      • Amyloid Fibrils, Amyloid Fibrils OC
      Background InformationAmyloid monomeric proteins can sometimes oligomerize into destructive amyloid fibrils. Amyloidogenic conformations of non-disease related proteins can be created by partial protein misfolding or denaturation. In disease state oligomerization, extensive amyloid oligomerization creates plaques in neural tissue that correlates with Alzheimer’s symptomology.
      References
      Product Information
      FormatSerum
      Control
      • Alzheimer's Brain tissue
      PresentationUnpurified rabbit polyclonal antibody serum containing 0.05% sodium azide.
      Applications
      ApplicationAnti-Amyloid Fibrils OC Antibody is an antibody against Amyloid Fibrils OC for use in IP, IC, IH, ELISA, WB, DB.
      Key Applications
      • Immunoprecipitation
      • Immunocytochemistry
      • Immunohistochemistry
      • ELISA
      • Western Blotting
      • Dot Blot
      Application NotesDot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in monomers, oligos, and fibrils.
      Biological Information
      ImmunogenFibrils prepared from human Aß42 peptide.
      EpitopeN/A
      HostRabbit
      SpecificityThis antibody recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not prefibrillar oligomers or natively folded proteins. It may also show weak reactivity against Aβ monomers while AB2287 does not.
      IsotypeIgG
      Species Reactivity
      • Human
      Species Reactivity NoteProven to react with human. Expected to detect amyloid fibrils in mouse and rat based on the species homology.
      Antibody TypePolyclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryThis gene encodes a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Multiple transcript variants encoding several different isoforms have been found for this gene.
      Gene Symbol
      • Amyloid Fibrils OC
      Purification MethodUnpurified
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P05067 # The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
      SIZE: 770 amino acids; 86943 Da
      SUBUNIT: Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, Numb and Dab1 (By similarity). Binding to Dab1 inhibits its serine phosphorylation (By similarity). Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains) (By similarity), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains (By similarity). Associates with microtubules in the presence of ATP and in a kinesin-dependent manner (By similarity). Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 (By similarity).
      SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O- glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C- terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with Fe65. Beta- APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment.
      TISSUE SPECIFICITY: Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex- opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra- striate and motor cortices. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.
      DOMAIN: SwissProt: P05067 The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells. & The NPXY sequence motif found in many tyrosine- phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C- terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The NPXY site is also involved in clathrin-mediated endocytosis.
      PTM: Proteolytically processed under normal cellular conditions. Cleavage by alpha-secretase or alternatively by beta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, respectively, and the retention of corresponding membrane-anchored C-terminal fragments, C83 and C99. Subsequent processing of C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). & Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides. & N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region (By similarity). & Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell- cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin. & Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of beta-amyloid-containing peptides.
      DISEASE: SwissProt: P05067 # Defects in APP are a cause of autosomal dominant Alzheimer disease (AD) [MIM:104300]. AD is the most prevelant form of dementia, characterized by neurofibrillary tangles and amyloid plaques deposition in the brain. Identical lesions occur in the neurons of aged Down syndrome but at an earlier age than in AD. The major constituent of these neuritic plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. Mutations occurring at the beta-amyloid N-terminal, such as the Swedish double mutation, appear to increase levels of beta-amyloid by facilitating beta-secretase cleavage resulting in elevated levels of both beta-APP42 and beta-APP40. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31, are also implicated in AD neuronal death. Alzheimer disease caused by mutations in APP is a rare occurrence and usually causes the familial or early-onset form of the disease (FAD). Flemish-type AD is characterized by, in addition to presenile dementia, cerebral hemorrhaging due to cerebral amyloid angiopathy which is similar to, but distinct from, cerebroarterial amyloidosis Dutch type. Only about 5% of all cases of Alzheimer disease are caused by FAD mutations, the rest are sporadic. & Defects in APP are the cause of hereditary cerebral hemorrhage with amyloidosis Dutch type (HCHWAD) [MIM:609065]. HCHWAD is characterized by amyloid deposits in cerebral vessels. The principal clinical characteristics are recurring cerebral hemorrhages, sometimes preceded by migrainous headaches or mental cleavage. Beta-APP40 is the predominant form of cerebrovascular amyloid. & Defects in APP are the cause of hereditary cerebroarterial amyloidosis Iowa type [MIM:605714]. Hereditary cerebroarterial amyloidosis Iowa type is an autosomal dominant dementia beginning in the sixth or seventh decade of life. The patients have progressive aphasic dementia, leukoencephalopathy, and occipital calcifications. They do not present cerebral hemorrhaging.
      SIMILARITY: Belongs to the APP family. & Contains 1 BPTI/Kunitz inhibitor domain.
      MISCELLANEOUS: Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between beta-amyloid molecules resulting in beta-amyloid-metal aggregates. The affinity for copper is much higher than for other transient metals and is increased under acidic conditions. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding.
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceEvaluated by Dot Blot in monomers, oligos, and fibrils.

      Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in monomers, oligos, and fibrils.
      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 receipt 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.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information
      Specifications

      Documentation

      MSDS

      Título

      Ficha de Segurança de Produtos (MSDS) 

      Certificados de análise

      TítuloNúmero do lote
      Anti-Amyloid Fibrils OC - 2147135 2147135
      Anti-Amyloid Fibrils OC - 2424776 2424776
      Anti-Amyloid Fibrils OC - 1966929 1966929
      Anti-Amyloid Fibrils OC - 1993788 1993788
      Anti-Amyloid Fibrils OC - 2022060 2022060
      Anti-Amyloid Fibrils OC - 2038298 2038298
      Anti-Amyloid Fibrils OC - 2073638 2073638
      Anti-Amyloid Fibrils OC - 2287786 2287786
      Anti-Amyloid Fibrils OC - 2345063 2345063
      Anti-Amyloid Fibrils OC - NG1648320 NG1648320
      Anti-Amyloid Fibrils OC - NG1732175 NG1732175
      Anti-Amyloid Fibrils OC - NG1865063 NG1865063
      Anti-Amyloid Fibrils OC - NG1916160 NG1916160
      Anti-Amyloid Fibrils OC -2489077 2489077
      Anti-Amyloid Fibrils OC -2554096 2554096
      Anti-Amyloid Fibrils OC -2587247 2587247
      Anti-Amyloid Fibrils OC -2620587 2620587
      Anti-Amyloid Fibrils OC -2649156 2649156
      Anti-Amyloid Fibrils OC -2682434 2682434
      Anti-Amyloid Fibrils OC -2726819 2726819
      Anti-Amyloid Fibrils OC -2772691 2772691
      Anti-Amyloid Fibrils OC -2834757 2834757

      Referências | 12 Disponível | Ver todas as referências

      Visão geral das referênciasAplicaçãoPub Med ID
      Characterization of a Novel Mouse Model of Alzheimer's Disease--Amyloid Pathology and Unique β-Amyloid Oligomer Profile.
      Liu, P; Paulson, JB; Forster, CL; Shapiro, SL; Ashe, KH; Zahs, KR
      PloS one 10 e0126317 2015

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      25946042 25946042
      Cytotoxic helix-rich oligomer formation by melittin and pancreatic polypeptide.
      Singh, PK; Ghosh, D; Tewari, D; Mohite, GM; Carvalho, E; Jha, NN; Jacob, RS; Sahay, S; Banerjee, R; Bera, AK; Maji, SK
      PloS one 10 e0120346 2015

      Mostrar Resumo
      25803428 25803428
      Amyloid properties of the mouse egg zona pellucida.
      Egge, N; Muthusubramanian, A; Cornwall, GA
      PloS one 10 e0129907 2015

      Mostrar Resumo
      26043223 26043223
      Microglia constitute a barrier that prevents neurotoxic protofibrillar Aβ42 hotspots around plaques.
      Condello, C; Yuan, P; Schain, A; Grutzendler, J
      Nature communications 6 6176 2015

      Mostrar Resumo
      25630253 25630253
      Forebrain microglia from wild-type but not adult 5xFAD mice prevent amyloid-β plaque formation in organotypic hippocampal slice cultures.
      Hellwig, S; Masuch, A; Nestel, S; Katzmarski, N; Meyer-Luehmann, M; Biber, K
      Scientific reports 5 14624 2015

      Mostrar Resumo
      26416689 26416689
      Functional amyloids in the mouse sperm acrosome.
      Guyonnet, B; Egge, N; Cornwall, GA
      Molecular and cellular biology 34 2624-34 2014

      Mostrar Resumo
      24797071 24797071
      Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?
      Leal, Sónia S, et al.
      J. Biol. Chem., (2013) 2013

      Mostrar Resumo
      23861388 23861388
      Intrinsically disordered and aggregation prone regions underlie β-aggregation in S100 proteins.
      Carvalho, SB; Botelho, HM; Leal, SS; Cardoso, I; Fritz, G; Gomes, CM
      PloS one 8 e76629 2013

      Mostrar Resumo
      24098542 24098542
      S100A6 amyloid fibril formation is calcium-modulated and enhances superoxide dismutase-1 (SOD1) aggregation.
      Botelho, Hugo M, et al.
      J. Biol. Chem., (2012) 2012

      Mostrar Resumo
      23076148 23076148
      Methylene blue modulates huntingtin aggregation intermediates and is protective in Huntington's disease models.
      Sontag, EM; Lotz, GP; Agrawal, N; Tran, A; Aron, R; Yang, G; Necula, M; Lau, A; Finkbeiner, S; Glabe, C; Marsh, JL; Muchowski, PJ; Thompson, LM
      The Journal of neuroscience : the official journal of the Society for Neuroscience 32 11109-19 2012

      Mostrar Resumo
      Western Blotting22875942 22875942