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Your Position: Start > Protein > APP > APP-H51H7

Human APP / Abeta40 Protein, His Tag

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  • Synonym
    ABPP,APPI,Amyloid-beta A4 protein
  • Source
    Human Abeta40, His Tag(APP-H51H7) is expressed from E. coli cells. It contains AA Asp 672 - Val 711 (Accession # P05067-1).
    Predicted N-terminus: Met
  • Molecular Characterization
    APP Structure

    This protein carries a polyhistidine tag at the C-terminus

    The protein has a calculated MW of 6.3 kDa. The protein migrates as 11 kDa under reducing (R) condition (SDS-PAGE).

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in PBS, 0.2 M Arginine, pH7.4 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
APP SDS-PAGE

Human Abeta40, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

Bioactivity-ELISA
 APP ELISA

Immobilized Human Abeta40, His Tag (Cat. No. APP-H51H7) at 5 μg/mL (100 μL/well) can bind Aducanumab with a linear range of 0.2-2 ng/mL (QC tested).

  • Background
    Amyloid precursor protein (APP) is a type I integral membrane protein ubiquitously expressed in many tissues and concentrated in the synapses of neurons. It has three predominant splice variants: APP695, APP751, and APP770. The majority of APP is cleaved at the plasma membrane by the α-secretase in the non-amyloidogenic pathway. The amyloidogenic pathway starts with β-secretase cleavage by BACE1 on the N-terminal part of the Aβ domain, releasing sAPPβ from a membrane-anchored fragment named βCTF or C99, which is subsequently cleaved by γ-secretase to release Aβ.
  • Clinical and Translational Updates

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