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beta Amyloid Protéine

Abeta Origine: Humain Hôte: Synthetic Synthetic >95% pure using mass spec and HPLC. WB, in vitro, in vivo
N° du produit ABIN7272125
  • Antigène Voir toutes beta Amyloid (Abeta) Protéines
    beta Amyloid (Abeta) (Amyloid beta (Abeta))
    Type de proteíne
    Synthetic
    Origine
    Humain
    Source
    • 1
    Synthetic
    Application
    Western Blotting (WB), In vitro Assay (in vitro), In vivo Studies (in vivo)
    Fonction
    Human Synthetic Amyloid Beta Peptide 1-42 (HFIP treated) Monomers
    Séquence
    DAEFRHDSGY EVHHQKLVFF AEDVGSNKGA IIGLMVGGVV IA
    Pureté
    >95% pure using mass spec and HPLC.
  • Indications d'application
    Optimal working dilution should be determined by the investigator.
    Restrictions
    For Research Use only
  • Stock
    -80 °C
    Stockage commentaire
    -80°C
  • Antigène
    beta Amyloid (Abeta) (Amyloid beta (Abeta))
    Autre désignation
    Amyloid Beta (Abeta Produits)
    Synonymes
    AAA Protein, ABETA Protein, ABPP Protein, AD1 Protein, APPI Protein, CTFgamma Protein, CVAP Protein, PN-II Protein, PN2 Protein, aaa Protein, abeta Protein, abpp Protein, ad1 Protein, appi Protein, ctfgamma Protein, cvap Protein, pn2 Protein, Abeta Protein, Abpp Protein, Adap Protein, Ag Protein, Cvap Protein, E030013M08Rik Protein, betaApp Protein, amyloid beta precursor protein Protein, amyloid beta (A4) precursor protein Protein, APP Protein, app Protein, App Protein
    Sujet
    Our amyloid beta peptide 1-42 (Aβ42) is produced synthetically and treated with 1,1,1,3,3,3-Hexafluoro-2-propanol (HFIP) prior to drying which breaks down pre-formed fibrils and monomerizes the peptide, as previously published (1,2). Upon resuspension in DMSO/dH2O, our Aβ42 presents as a monomeric peptide without fibrils when observed under TEM, AFM and on a Western Blot with an anti-amyloid beta antibody. In contrast to AB42 oligomer and fibril constructs, our Aβ42 monomers were not toxic to primary rat cortical neurons. In the brain, amyloid beta peptide (Aβ) is generated by protease cleavage of amyloid precursor protein (APP), which aggregates into oligomers, protofibrils, fibrils and ultimately plaques in neurodegenerative diseases. The accumulation of Aβ plaques in the brain is considered a hallmark of Alzheimer's disease (AD), and most of the drugs tested for AD in the past 20 years have targeted amyloid beta accumulation (3). Soluble Aβ oligomers isolated from the brains of AD patients or those generated in vitro potently impaired synapse structure and function (4). Aβ oligomers generated in vitro were toxic to PC12 cells (2) and SH-SY5Y cells (5). Aβ was demonstrated to interact with tauopathies to affect neurodegeneration in AD patients (6) and accumulations of Aβ were shown to be associated with lower survival rates in Parkinson's disease patients with dementia (7)., cellular localisation: Cell Membrane , Intracellular Vesicles
    Poids moléculaire
    4.5 kDa
    ID gène
    351
    UniProt
    P05067
    Pathways
    Inflammasome
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