beta-Amyloid 39 protein (GST tag,His tag)
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- Target
- beta-Amyloid 39
- Protein Type
- Recombinant
- Origin
- Human
- Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- GST tag,His tag
- Purpose
- Recombinant Human Beta-amyloid 39/Beta-APP39 Protein (aa 672-710, His & GST Tag)
- Sequence
- Asp672-Val710
- Characteristics
- A DNA sequence encoding the amino acids (Asp672-Val710) of human Amyloid beta A4 protein (APP770) (P05067-1), corresponding to the Beta-amyloid protein 39, was fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.
- Purity
- > 85 % as determined by reducing SDS-PAGE.
- Endotoxin Level
- Please contact us for more information.
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- Comment
-
34 kDa
- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Reconstitution
- Please refer to the printed manual for detailed information.
- Buffer
- Lyophilized from sterile 50 mM Tris, 100 mM NaCl, 20 % glycerol, 0.05 % Tween 20, pH 9.5
- 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.
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- Target
- beta-Amyloid 39
- Background
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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
- Molecular Weight
- 32.2 kDa
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