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APP Protein (Fc Tag)

APP Origin: Human Host: HEK-293 Cells Recombinant > 95 % as determined by reducing SDS-PAGE. Active
Catalog No. ABIN7194239
  • Target See all APP Proteins
    APP (Amyloid beta (A4) Precursor Protein (APP))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Origin
    • 10
    • 4
    • 3
    Human
    Source
    • 7
    • 5
    • 2
    • 2
    • 1
    HEK-293 Cells
    Purification tag / Conjugate
    This APP protein is labelled with Fc Tag.
    Purpose
    Recombinant Human APP/Protease nexin-II Protein (Fc Tag)(Active)
    Sequence
    Met 1-Leu 669
    Characteristics
    A DNA sequence encoding the human APP-751 isoform (NP_958816.1) (Met 1-Leu 669) was expressed with the C-terminal fused Fc region of human IgG1.
    Purity
    > 95 % as determined by reducing SDS-PAGE.
    Endotoxin Level
    < 1.0 EU per μg as determined by the LAL method.
    Biological Activity Comment
    Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2, (R&D Systems, Catalog # ES002). The IC50 value is < 1.2 nM.
    Top Product
    Discover our top product APP Protein
  • Restrictions
    For Research Use only
  • Format
    Lyophilized
    Reconstitution
    Please refer to the printed manual for detailed information.
    Buffer
    Lyophilized from sterile PBS, pH 7.4
    Storage
    4 °C,-20 °C,-80 °C
    Storage Comment
    Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
  • Target
    APP (Amyloid beta (A4) Precursor Protein (APP))
    Alternative Name
    APP/Protease nexin-II (APP Products)
    Synonyms
    AAA Protein, ABETA Protein, ABPP Protein, AD1 Protein, APPI Protein, CTFgamma Protein, CVAP Protein, PN-II Protein, PN2 Protein, aaa Protein, abeta Protein, abpp Protein, ad1 Protein, appi Protein, ctfgamma Protein, cvap Protein, pn2 Protein, APP Protein, APP-like Protein, APPL Protein, Abeta Protein, BcDNA:GH04413 Protein, CG7727 Protein, Dmel\\CG7727 Protein, EG:65F1.5 Protein, appl Protein, Abpp Protein, Adap Protein, Ag Protein, Cvap Protein, E030013M08Rik Protein, betaApp Protein, app Protein, wu:fj34d10 Protein, wu:fk65e12 Protein, zgc:85740 Protein, amyloid beta precursor protein Protein, amyloid beta (A4) precursor protein Protein, beta amyloid protein precursor-like Protein, amyloid beta (A4) precursor protein a Protein, amyloid beta precursor protein L homeolog Protein, APP Protein, app Protein, Appl Protein, App Protein, appa Protein, app.L Protein
    Background

    Background: Amyloid precursor protein (APP) is a type I transmembrane protein expressed in many tissues and concentrated in the synapses of neurons, and is suggested as a regulator of synapse formation and neural plasticity. APP can be processed by two different proteolytic pathways. In one pathway, APP is cleaved by β- and γ-secretase to produce the amyloid-β-protein (Aβ, Abeta, beta-amyloid) which is the principal component of the amyloid plaques, the major pathological hallmark of Alzheimer’s disease (AD), while in the other pathway, α-secretase is involved in the cleavage of APP whose product exerts antiamyloidogenic effect and prevention of the Aβ peptide formation. The aberrant accumulation of aggregated beta-amyloid peptides (Abeta) as plaques is a hallmark of AD neuropathology and reduction of Abeta has become a leading direction of emerging experimental therapies for the disease. Besides this pathological function of Abeta, recently published data reveal that Abeta also has an essential physiological role in lipid homeostasis. Cholesterol increases Abeta production, and conversely A beta production causes a decrease in cholesterol synthesis. Abeta may be part of a mechanism controlling synaptic activity, acting as a positive regulator presynaptically and a negative regulator postsynaptically. The pathological accumulation of oligomeric Abeta assemblies depresses excitatory transmission at the synaptic level, but also triggers aberrant patterns of neuronal circuit activity and epileptiform discharges at the network level. Abeta-induced dysfunction of inhibitory interneurons likely increases synchrony among excitatory principal cells and contributes to the destabilization of neuronal networks. There is evidence that beta-amyloid can impair blood vessel function. Vascular beta-amyloid deposition, also known as cerebral amyloid angiopathy, is associated with vascular dysfunction in animal and human studies. Alzheimer disease is associated with morphological changes in capillary networks, and soluble beta-amyloid produces abnormal vascular responses to physiological and pharmacological stimuli.

    Synonym: AAA;ABETA;ABPP;AD1;APPI;CTFgamma;CVAP;PN-II;PN2

    Molecular Weight
    101 kDa
    NCBI Accession
    NP_958816
    Pathways
    Caspase Cascade in Apoptosis, EGFR Signaling Pathway, Transition Metal Ion Homeostasis, Skeletal Muscle Fiber Development, Toll-Like Receptors Cascades, Feeding Behaviour
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