Analytical Data
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Gene name
Amyloid Precursor/Beta-APP40
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简介
There is no specific Pubmed ID mentioned in the paragraph. Amyloid Precursor/Beta-APP40 Protein, Human (His-GST) is the recombinant human-derived Amyloid Precursor/Beta-APP40 protein, expressed by E. coli , with N-His, N-GST labeled tag.
- Application
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Alternative Names
Amyloid-beta precursor protein; APP; Protease Nexin II; PreA4
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Species
Human
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Source
E. coli
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Tag
N-His;N-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P05067-1
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Expression Region
D672-V711
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Protein Length
Full Length of APP40
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Molecular Weight
33 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Amyloid precursor protein (APP) is a key protein implicated in the development of Alzheimer's disease (AD), primarily through its role in the production of amyloid-beta (Aβ) peptides, including Aβ40 and Aβ42. The pathology of AD is characterized by the accumulation of these amyloid plaques in the brain, which are believed to contribute to neurodegeneration and cognitive decline. Aβ40, the more abundant and less toxic form, and Aβ42, which is more prone to aggregation, have drawn considerable attention for their differential roles in disease progression. Research on recombinant proteins of beta-APP40 is essential for understanding its biological functions, interactions, and the mechanisms driving amyloidogenic processing. By generating and studying these recombinant proteins, scientists aim to explore the structural and functional properties of APP and its cleavage products, facilitating the identification of potential therapeutic targets and strategies to mitigate AD pathology. Furthermore, studying Aβ40 in the context of APP processing can provide insights into the molecular pathways involved in protein misfolding, aggregation, and subsequent neuroinflammatory responses associated with Alzheimer’s disease, thus paving the way for innovative approaches in diagnosis and treatment.
