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Render Timestamp: 2024-12-23T10:49:08.918Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-11-19 23:03:09.972
Product last modified at: 2024-11-23T09:00:10.684Z
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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.

APP (Aducanumab Biosimilar) Human mAb #59870

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Human IgG kappa
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    APP (Aducanumab Biosimilar) Human mAb is a biosimilar antibody for Aducanumab. Aducanumab is a human monoclonal antibody that targets aggregated forms of amyloid beta (Aβ) derived from amyloid precursor protein (APP).
    Endotoxin <0.1 EU/μg of antibody

    Product Usage Information

    This product is intended for research use only (RUO). Optimal dilutions/concentrations should be determined by the end user.

    Formulation

    Supplied in 1X PBS, BSA and Azide Free.

    Storage

    Store at -20°C. This product will freeze at -20°C so it is recommended to aliquot into single-use vials to avoid multiple freeze/thaw cycles. A slight precipitate may be present and can be dissolved by gently vortexing. This will not interfere with antibody performance.

    Specificity / Sensitivity

    APP (Aducanumab Biosimilar) Human mAb was confirmed to bind to its intended target aggregated Aβ using bio-layer interferometry.

    Species Reactivity:

    Human

    Source / Purification

    APP (Aducanumab Biosimilar) Human mAb is produced at Cell Signaling Technology. Aducanumab is an antibody directed against aggregated Aβ.

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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