Description
Recombinant Human Beta-amyloid 38/Beta-APP38 Protein (aa 672-709, His & GST Tag) | PKSH031463 | Gentaur US, UK & Europe Disrtribition
Synonyms: AAA;ABETA;ABPP;AD1;APPI;CTFgamma;CVAP;PN-II;PN2
Active Protein: N/A
Activity: A DNA sequence encoding the amino acids (Asp672-Gly709) of human Amyloid beta A4 protein (APP770) (P05067-1); corresponding to the Beta-amyloid protein 38; was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Protein Construction: A DNA sequence encoding the amino acids (Asp672-Gly709) of human Amyloid beta A4 protein (APP770) (P05067-1); corresponding to the Beta-amyloid protein 38; was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
Fusion Tag: N-His & GST
Species: Human
Expressed Host: E.coli
Shipping: This product is provided as lyophilized powder which is shipped with ice packs.
Purity: > 85 % as determined by reducing SDS-PAGE.
Endotoxin: Please contact us for more information.
Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Molecular Mass: 32.1 kDa
Formulation: Lyophilized from sterile 50 mM Tris, 100 mM NaCl, 20% glycerol, 0.05% Tween 20, pH 9.5.
Reconstitution: Please refer to the printed manual for detailed information.
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.
Research Area: N/A
