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MAB5354 Anti-Amyloid β Precursor Protein Antibody, KPI domain, clone 4.1

Anti-Amyloid β Precursor Protein Antibody, KPI domain, clone 4.1 detects level of Amyloid β Precursor Protein & has been published & validated for use in ELISA, WB, IH.

MSDS (material safety data sheet) o SDS, certificato d’analisi (CoA) e certificato di qualità (CoQ), dossier, brochure e altri documenti disponibili.
Research Category: Neuroscience Research Sub-Category: Neurodegenerative Diseases Gene Symbol: APP, ABPP, PN-II, AD1, A4, CVAP, PN2, ABETA, CTFgamma, APPI, PreA4, AAA UniProt Number: P05067
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MAB5354
100 µg  
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      Tabella delle specifiche principali

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      HELISA, WB, IHCMPurifiedMonoclonal Antibody
      Description
      Catalogue NumberMAB5354
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Amyloid β Precursor Protein Antibody, KPI domain, clone 4.1
      References
      Product Information
      FormatPurified
      PresentationPurified immunoglobulin. Liquid in 20 mM Sodium phosphate buffer with 150 mM NaCl.
      Quality LevelMQ100
      Applications
      ApplicationAnti-Amyloid β Precursor Protein Antibody, KPI domain, clone 4.1 detects level of Amyloid β Precursor Protein & has been published & validated for use in ELISA, WB, IH.
      Key Applications
      • ELISA
      • Western Blotting
      • Immunohistochemistry
      Application NotesWestern blot: 2-5 μg/mL using ECL on human brain or platelets. Recognizes a protein of 100-120 kDa.

      Immunohistochemistry: 2-5 μg/mL on frozen tissue sections.

      ELISA: 1 μg/mL in a direct assay and 10 μg/mL in an indirect assay.

      Optimal working dilutions must be determined by the end user.
      Biological Information
      ImmunogenPurified recombinant KPI domain of Amyloid-beta precursor protein.
      EpitopeKPI domain
      Clone4.1
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      HostMouse
      SpecificityAmyloid-beta Precursor Protein, KPI (Kunitz protease inhibitor) domain. The antibody reacts with both native and recombinant protein. The antibody has been shown to partially inhibit protease inhibitory properties.
      IsotypeIgG1
      Species Reactivity
      • Human
      Antibody TypeMonoclonal 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
      • APP
      • ABPP
      • PN-II
      • AD1
      • A4
      • CVAP
      • PN2
      • ABETA
      • CTFgamma
      • APPI
      • PreA4
      • AAA
      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
      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 2-8°C in undiluted aliquots for up to 6 months of date of receipt.
      Packaging Information
      Material Size100 µg
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Numero di catalogo GTIN
      MAB5354 04053252463693

      Documentation

      Anti-Amyloid β Precursor Protein Antibody, KPI domain, clone 4.1 MSDS

      Titolo

      Scheda di sicurezza (MSDS) 

      Anti-Amyloid β Precursor Protein Antibody, KPI domain, clone 4.1 Certificati d'Analisi

      TitoloNumero di lotto
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN MONOCLONAL ANTIBODY - 2138025 2138025
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN - 3307747 3307747
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN - 3993566 3993566
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN -2621736 2621736
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN -2750278 2750278
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN MONOCLONAL ANTIBODY 2882685
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN MONOCLONAL ANTIBODY 3049386
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN MONOCLONAL ANTIBODY - 4093945 4093945
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN MONOCLONAL ANTIBODY - 1997404 1997404
      MOUSE ANTI-AMYLOID-BETA PRECURSOR PROTEIN, KPI DOMAIN MONOCLONAL ANTIBODY - 2188502 2188502
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      Riferimenti bibliografici

      Panoramica dei riferimenti bibliograficiCodice d'identificazione nel Pub Med
      Activation of extrasynaptic, but not synaptic, NMDA receptors modifies amyloid precursor protein expression pattern and increases amyloid-ß production.
      Bordji, K; Becerril-Ortega, J; Nicole, O; Buisson, A
      The Journal of neuroscience : the official journal of the Society for Neuroscience  30  15927-42  2009

      Mostra il sommario       		21106831 21106831

      Newsletters / Publications

      Title
      Research Focus - Volume 2, 2013