Abeta 1-40 Protein (GST tag,His tag)
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- Target Alle Abeta 1-40 Produkte
- Abeta 1-40 (Amyloid beta 1-40 (Abeta 1-40))
- Protein-Typ
- Recombinant
- Biologische Aktivität
- Active
- Spezies
- Human
- Quelle
- Escherichia coli (E. coli)
- Aufreinigungstag / Konjugat
- Dieses Abeta 1-40 Protein ist gelabelt mit GST tag,His tag.
- Verwendungszweck
- Recombinant Human Beta-amyloid 40/Beta-APP40 Protein (His&GST Tag)(Active)
- Sequenz
- Asp 672-Val 711
- Produktmerkmale
- A DNA sequence encoding the amino acids (Asp 672-Val 711) of human Amyloid beta A4 protein (APP770) (P05067-1), corresponding to the Beta-amyloid protein 40, was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
- Reinheit
- > 92 % as determined by reducing SDS-PAGE.
- Endotoxin-Niveau
- Please contact us for more information.
- Biological Activity Comment
- Measured by its ability to bind biotinylated recombinant human AGER in a functional ELISA.
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- Kommentare
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33 kDa
- Beschränkungen
- Nur für Forschungszwecke einsetzbar
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- Format
- Lyophilized
- Rekonstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from sterile 50 mM Tris, 500 mM NaCl, pH 7.5
- 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.
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- Target
- Abeta 1-40 (Amyloid beta 1-40 (Abeta 1-40))
- Andere Bezeichnung
- Beta-amyloid 40 (Abeta 1-40 Produkte)
- Synonyme
- AAA Protein, ABETA Protein, ABPP Protein, AD1 Protein, APPI Protein, CTFgamma Protein, CVAP Protein, PN-II Protein, PN2 Protein, amyloid beta precursor protein Protein, APP Protein
- Hintergrund
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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
- 31.8 kDa
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