Render Target: STATIC
Render Timestamp: 2024-11-21T13:47:37.701Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-08-01 15:32:11.452
Product last modified at: 2024-10-15T17:45:13.508Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

β-Amyloid (pE3 Peptide) (D5N5H) Rabbit mAb #14975

Filter:
  • WB
  • IHC
  • IF

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 4
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IHC-Immunohistochemistry 
    • IF-Immunofluorescence 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunohistochemistry (Paraffin) 1:100
    Immunofluorescence (Frozen) 1:200

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    For a carrier free (BSA and azide free) version of this product see product #76486.

    Protocol

    Specificity / Sensitivity

    β-Amyloid (pE3 Peptide) (D5N5H) Rabbit mAb recognizes recombinant pE3 form of β-amyloid peptides. This antibody does not cross-react with the non-pyroglutamate (E3) form of β-amyloid peptides.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of β-amyloid (pE3) peptide.

    Background

    Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).
    Aβ peptides can be further modified by amino-terminal truncation that exposes a free glutamate residue to the enzyme glutaminyl cyclase, which catalyzes the formation of an amino-terminal pyroglutamate (pE) (7,8). Aβ (pE3) peptides exhibit increased stability relative to non-modified peptides due to an enhanced resistance to peptidase-mediated degradation (9) and a higher propensity to form β-sheets and aggregate (10). Antibodies targeting Aβ (pE3) peptides may be plaque-specific as there is no evidence for circulating Aβ (pE3) peptides (11).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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