Analytical Data
-
Gene name
Amyloid Precursor/APP-770
-
简介
There is no specific Pubmed ID mentioned in the paragraph. Amyloid Precursor/APP-751 Protein, Human (Active, HEK293, His) is the recombinant human-derived Amyloid Precursor/APP-751 protein, expressed by HEK293, with C-His labeled tag.
- Application
-
Alternative Names
Amyloid-beta precursor protein; APP; CVAP; PN-II; PreA4; A4; AD1
-
Species
Human
-
Source
HEK293
-
Tag
C-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P05067-1
-
Expression Region
L18-M687
-
Protein Length
Full Length of Soluble APP-alpha
-
Molecular Weight
95-130 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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) plays a crucial role in the pathogenesis of Alzheimer's disease (AD), primarily through its cleavage by secretases, leading to the formation of amyloid-beta (Aβ) peptides, which aggregate to form plaques in the brains of AD patients. APP exists in various isoforms, with APP-770 being the most abundant in the central nervous system. Research on APP-770 recombinant protein has gained significant attention due to its potential to elucidate the mechanisms underlying Aβ production and the cellular functions of APP itself. Studies have indicated that the processing of APP is tightly regulated and influenced by multiple factors, including post-translational modifications and cellular environments. By generating recombinant APP-770, researchers can investigate its structural properties, binding interactions, and functional roles in neuronal health and disease. Understanding the dynamics of APP-770 and its contributions to Aβ pathology may provide insights into novel therapeutic strategies aimed at preventing or mitigating the progression of Alzheimer's disease. This research not only holds promise for advancing our understanding of AD but also offers a pathway for the development of biomarker approaches and targeted interventions for affected individuals.











