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    Anti-beta Amyloid 1-42 Rabbit mAb

    Catalog number :AT0690
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    Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms. The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage. The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease. APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein. Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase. APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation.
    Overview
    Reactivity
    Human, Mouse, Rat
    Tested applications
    Western Blotting 1:1000
    Immunoprecipitation 1:200
    Immunohistochemistry (Paraffin) 1:500
    Optimal dilutions/concentrations should be determined by the end user. 
     
    Specificity
    This antibody recognizes endogenous levels of total Aβ-42 peptide. Reacts with amyloid plaques in AD brain tissue with minimal cross reactivity with beta-amyloid 1-40 or beta-amyloid 1-43
    Properties
    Immunogen
    a synthetic peptide corresponding to residues near the carboxy terminus of human β-amyloid (1-42) peptide.
    Clonality
    Monoclonal, clone number: 6FG1
    Isotype
    Rabbit IgG
    Form
    Liquid, 100 μl,1mg/ml, PBS (pH 7.2) and 40% Glycerol,0.02% Sodium Azide
    Storage instruction
    Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C, Avoid freeze / thaw cycle.
    Host
    Rabbit
    Applications
    IHC Image

    at 1/150 staining human brain tissue sections by IHC-P. The tissue was formaldehyde fixed and blocked with BSA prior to incubation with the antibody for 16 hours. A biotinylated goat anti-rabbit IgG was used as the secondary antibody. All block sections showed exclusive positivity in Amyloid plaques of Alzheimer's disease: no intracellular positivity was detected.

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