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  • Anti-APP antibody

Anti-APP antibody

Cat.#: 142077

Special Price 145.0 USD

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Product Information

  • Product Name
    Anti-APP antibody
  • Documents
  • Description
    Rabbit Polyclonal to Human APP
  • Tested applications
    ELISA
  • Species reactivity
    Human Amyloid beta A4 protein
  • Alternative names
    AD1 antibody; PN2 antibody; ABPP antibody; APPI antibody; CVAP antibody; ABETA antibody; PN-II antibody; CTFgamma antibody; Ag antibody; Abpp antibody; Adap antibody; Cvap antibody; Abeta antibody; betaApp antibody; E030013M08Rik antibody; AAA antibody; AAA antibody; ABETA antibody; Abeta antibody; ABPP antibody; AD1 antibody; Adap antibody; AL024401 antibody; APPI antibody; appican antibody; betaAPP antibody; CTFgamma antibody; Cvap antibody; CVAP antibody; E030013M08Rik antibody; PN2 antibody; protease nexin II antibody; protease nexin II antibody
  • Immunogen
  • Isotype
    Rabbit IgG
  • Preparation
    Produced in rabbits immunized with purified, recombinant Human Amyloid beta A4 protein . Amyloid beta A4 protein specific IgG was purified by Human Amyloid beta A4 protein affinity chromatography.
  • Clonality
    Polyclonal
  • Formulation
    0.2 μm filtered solution in PBS
  • Storage instructions
    This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free.
    Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.
  • Applications

    ELISA: 0.1-0.2 μg/ml

    This antibody can be used at 0.1-0.2 μg/ml with the appropriate secondary reagents to detect Human Amyloid beta A4 protein.

  • Validations
  • 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.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"