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AB2287 Anti-Amyloid Fibrils LOC Antibody

This Anti-Amyloid Fibrils LOC Antibody is validated for use in IP, IC, IH, ELISA, WB, DB for the detection of Amyloid Fibrils LOC.

Anti-Amyloid Fibrils LOC Antibody : FDS (Fiches de données de sécurité), certificats d’analyse (CoA) et de qualité (CoQ), dossiers, brochures et autres documents disponibles.
Research Category: Neuroscience Research Sub-Category: Neurodegenerative Diseases Gene Symbol: Amyloid fibrils LOC UniProt Number: P05067
AB2287
100 µL  
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Tableau de caractéristiques principal

Species ReactivityKey ApplicationsHostFormatAntibody Type
HIP, ICC, IHC, ELISA, WB, DBRbSerumPolyclonal Antibody
Description
Catalogue NumberAB2287
Brand Family Chemicon®
Trade Name
  • Chemicon
DescriptionAnti-Amyloid Fibrils LOC Antibody
Alternate Names
  • Amyloid Fibrils, Amyloid Fibrils LOC
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
HS Code3002 15 90
Control
  • Alzheimer's Brain tissue
PresentationUnpurified rabbit polyclonal antibody serum containing 0.05% sodium azide.
Quality LevelMQ100
Applications
ApplicationThis Anti-Amyloid Fibrils LOC Antibody is validated for use in IP, IC, IH, ELISA, WB, DB for the detection of Amyloid Fibrils LOC.
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 fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.
Biological Information
ImmunogenFibrils prepared from human islet amyloid polypeptide.
EpitopeN/A
HostRabbit
SpecificityThis antibody recognizes generic epitopes common to many amyloid fibrils and fibrillar oligomers, but not monomers, prefibrillar oligomers or natively folded proteins.
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 LOC
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, prefibril oligos, and fibrils.

Dot Blot Analysis: 1:1,000 dilution of this antibody detected Amyloid fibrils in fibrils and monomers but not in prefibril oligos. A 1:5,000 dilution, as cited in Glabe C., et al. (2007) Mol Neurodegener 2, 18 shows that the binding with monomers is likely non-specific, and is a possible result of high primary antibody concentration.
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. After thawing, store at 4°C in 0.02% sodium azide.
Packaging Information
Material Size100 µL
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Référence GTIN
AB2287 04053252324420

Documentation

Anti-Amyloid Fibrils LOC Antibody FDS

Titre

Fiche de données de sécurité des matériaux (FDS) 

Anti-Amyloid Fibrils LOC Antibody Certificats d'analyse

TitreNuméro de lot
Anti-Amyloid Fibrils LOC 3082480
Anti-Amyloid Fibrils LOC - 2366003 2366003
Anti-Amyloid Fibrils LOC - 2391207 2391207
Anti-Amyloid Fibrils LOC - 2462843 2462843
Anti-Amyloid Fibrils LOC - 2008677 2008677
Anti-Amyloid Fibrils LOC - 2053401 2053401
Anti-Amyloid Fibrils LOC - 2197264 2197264
Anti-Amyloid Fibrils LOC - 2271211 2271211
Anti-Amyloid Fibrils LOC - 2510280 2510280
Anti-Amyloid Fibrils LOC - 3527764 3527764
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Références bibliographiques

Aperçu de la référence bibliographiqueApplicationNº PubMed
Neuroinflammation and related neuropathologies in APPSL mice: further value of this in vivo model of Alzheimer's disease.
Löffler, T; Flunkert, S; Havas, D; Schweinzer, C; Uger, M; Windisch, M; Steyrer, E; Hutter-Paier, B
Journal of neuroinflammation  11  84  2014

Afficher le résumé 		Immunohistochemistry24886182 24886182
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers.
Kayed, Rakez, et al.
Mol Neurodegener, 2: 18 (2007)  2007

Afficher le résumé 		17897471 17897471