Telefon:
+49 (0)241 95 163 153
Fax:
+49 (0)241 95 163 155
E-Mail:
orders@antikoerper-online.de

Abeta 1-42 Protein (GST tag,His tag)

Abeta 1-42 Spezies: Human Wirt: Escherichia coli (E. coli) Recombinant > 80 % as determined by reducing SDS-PAGE.
Produktnummer ABIN7317786
  • Target Alle Abeta 1-42 Produkte
    Abeta 1-42 (Amyloid beta 1-42 (Abeta 1-42))
    Protein-Typ
    Recombinant
    Spezies
    Human
    Quelle
    • 1
    Escherichia coli (E. coli)
    Aufreinigungstag / Konjugat
    Dieses Abeta 1-42 Protein ist gelabelt mit GST tag,His tag.
    Verwendungszweck
    Recombinant Human Beta-amyloid 42/Beta-APP42 Protein (His & GST Tag)
    Sequenz
    Asp672-Ala713
    Produktmerkmale
    A DNA sequence encoding the amino acids (Asp672-Ala713) of human Amyloid beta A4 protein (APP770) (P05067-1), corresponding to the Beta-amyloid protein 42, was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
    Reinheit
    > 80 % as determined by reducing SDS-PAGE.
    Endotoxin-Niveau
    Please contact us for more information.
  • Kommentare

    34 kDa

    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Lyophilized
    Rekonstitution
    Please refer to the printed manual for detailed information.
    Buffer
    Lyophilized from sterile PBS, 10 % glycerol, pH 7.4
    Lagerung
    4 °C,-20 °C,-80 °C
    Informationen zur Lagerung
    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
    Abeta 1-42 (Amyloid beta 1-42 (Abeta 1-42))
    Andere Bezeichnung
    Beta-amyloid 42 (Abeta 1-42 Produkte)
    Synonyme
    amyloid beta precursor protein Protein, App Protein, APP Protein
    Hintergrund

    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

    Molekulargewicht
    32.4 kDa
Sie sind hier: