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  1. Link

    beta-secretase-bace1-activity-assay-kit-fluorometric-ab282921.pdf

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Neuroscience Neurology process Neurodegenerative disease Alzheimer's disease Proteases
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Beta-Secretase (BACE1) Activity Assay Kit (Fluorometric) (ab282921)

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  • SDS
  • Protocol Booklet
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BACE1 Activity
  • Kinetic Measurement of BACE1 Activity
  • Standard Curve

Key features and details

  • Assay type: Enzyme activity (quantitative)
  • Detection method: Fluorescent
  • Sample type: Adherent cells, Suspension cells, Tissue
  • Sensitivity: 0.2 µU

Overview

  • Product name

    Beta-Secretase (BACE1) Activity Assay Kit (Fluorometric)
    See all BACE1 kits
  • Detection method

    Fluorescent
  • Sample type

    Tissue, Adherent cells, Suspension cells
  • Assay type

    Enzyme activity (quantitative)
  • Sensitivity

    0.2 µU
  • Product overview

    This Beta-Secretase (BACE1) Activity Assay Kit (Fluorometric), (ab282921) provides a fast and easy method for measuring BACE1 activity in a variety of samples. In this kit, a secretase-specific peptide is conjugated with two reporter molecules, EDANS and DABCYL. In the uncleaved form, the fluorescent emissions from EDANS are quenched by the physical proximity of the DABCYL moiety. Cleavage of the peptide by BACE1 separates EDANS and DABCYL groups allowing for the release of a strong fluorescent signal (Ex/Em= 345/500 nm). The level of secretase activity in samples is proportional to the level of fluorescence intensity. The assay is simple, sensitive, high–throughput adaptable and can detect BACE1 activity as low as 0.2 µU per sample. 


    Species activity: Eukaryotes

  • Notes

    This product is manufactured by BioVision, an Abcam company and was previously called K388 β-Secretase (BACE1) Activity Assay Kit (Fluorometric). K388-100 is the same size as the 100 test size of ab282921.

    β-Secretase (EC 3.4.23.46), also called BACE1 (β-site of APP cleaving enzyme) or memapsin-2 (membrane-associated aspartic protease), is an aspartic-acid protease. Along with γ-secretase, BACE1 cleaves the APP (Membrane-anchored amyloid precursor protein) and generates soluble amyloid-β (Aβ). Accumulation of Aβ is the key event for pathogenesis of Alzheimer's disease, thus monitoring and targeting BACE1 activity are important for the study and development of therapeutic strategies that could alleviate/cure Alzheimer’s disease. Recent studies have shown that inhibiting BACE1 activity with synthetic compounds helped to slow or arrest Alzheimer’s disease symptoms.

Properties

  • Storage instructions

    Store at -20°C. Please refer to protocols.
  • Components Identifier 100 tests
    BACE1 Assay Buffer WM 1 x 10ml
    BACE1 Extraction Buffer NM 1 x 25ml
    BACE1 Inhibitor Control (in DMSO) Blue 1 x 100µl
    BACE1 Positive Control Red 1 x 20µl
    BACE1 Substrate (in DMSO) Amber 1 x 200µl
    EDANS Standard (100 µM) Yellow 1 x 100µl
  • Research areas

    • Neuroscience
    • Neurology process
    • Neurodegenerative disease
    • Alzheimer's disease
    • Proteases
    • Cell Biology
    • Proteolysis / Ubiquitin
    • Proteolytic enzymes
    • Aspartic protease
    • BACEs
    • Neuroscience
    • Diseases
  • Function

    Responsible for the proteolytic processing of the amyloid precursor protein (APP). Cleaves at the N-terminus of the A-beta peptide sequence, between residues 671 and 672 of APP, leads to the generation and extracellular release of beta-cleaved soluble APP, and a corresponding cell-associated C-terminal fragment which is later released by gamma-secretase.
  • Tissue specificity

    Expressed at high levels in the brain and pancreas. In the brain, expression is highest in the substantia nigra, locus coruleus and medulla oblongata.
  • Sequence similarities

    Belongs to the peptidase A1 family.
  • Domain

    The transmembrane domain is necessary for its activity. It determines its late Golgi localization and access to its substrate, APP.
  • Post-translational
    modifications

    Glycosylated.
  • Cellular localization

    Membrane. Golgi apparatus > trans-Golgi network. Endoplasmic reticulum. Endosome. Cell surface. Predominantly localized to the later Golgi/trans-Golgi network (TGN) and minimally detectable in the early Golgi compartments. A small portion is also found in the endoplasmic reticulum, endosomes and on the cell surface.
  • Target information above from: UniProt accession P56817 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt
  • Alternative names

    • APP beta secretase
    • Asp 2
    • ASP2
    • Aspartyl protease 2
    • BACE
    • BACE 1
    • BACE1
    • BACE1_HUMAN
    • Beta secretase
    • Beta secretase 1
    • Beta site amyloid beta A4 precursor protein cleaving enzyme
    • Beta site amyloid precursor protein cleaving enzyme
    • Beta site amyloid precursor protein cleaving enzyme 1
    • Beta site APP cleaving enzyme
    • Beta site APP cleaving enzyme 1
    • Beta-secretase 1
    • Beta-site amyloid precursor protein cleaving enzyme 1
    • Beta-site APP cleaving enzyme 1
    • FLJ90568
    • HSPC104
    • Memapsin 2
    • Memapsin-2
    • Memapsin2
    • Membrane associated aspartic protease 2
    • Membrane-associated aspartic protease 2
    • Transmembrane aspartic proteinase Asp2
    see all

Images

  • BACE1 Activity
    BACE1 Activity

    Relative BACE1 Activity was calculated in lysates (4 µg) prepared from mouse whole brain (Sample 1) and mouse whole brain (Sample 2). Assays were performed following the kit protocol.

  • Kinetic Measurement of BACE1 Activity
    Kinetic Measurement of BACE1 Activity

    Kinetic measurement of BACE1 activity in mouse whole brain lysate (4 µg).

  • Standard Curve
    Standard Curve

    EDANS Standard Curve.

Protocols

  • Protocol Booklet

Click here to view the general protocols

Datasheets and documents

  • SDS download

  • Datasheet download

    Download

References (0)

Publishing research using ab282921? Please let us know so that we can cite the reference in this datasheet.

ab282921 has not yet been referenced specifically in any publications.

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