Analytical Data
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Gene name
APH1A
- Application
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Alternative Names
Aph-1alpha Presenilin-stabilization factor
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96BI3
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Expression Region
235-265aa
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Molecular Weight
11.1 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
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Protein Description
APH1A, a critical component of the γ-secretase complex, plays a pivotal role in the processing of type I membrane proteins, including the amyloid precursor protein (APP), which is associated with Alzheimer's disease. The γ-secretase complex is responsible for the intramembrane cleavage of various substrates, and APH1A specifically contributes to the stability and proper assembly of this multi-subunit enzyme. Research on APH1A recombinant protein has gained significant attention due to its potential implications in understanding Alzheimer's pathology and the development of therapeutic interventions. Dysregulation of γ-secretase activity, often linked with abnormal APP processing, leads to the formation of amyloid-beta peptides, which aggregate and form plaques in the brains of Alzheimer's patients. Consequently, studying the functional properties of APH1A and its interactions within the γ-secretase complex could provide valuable insights into the molecular mechanisms underlying neurodegenerative diseases. Moreover, recombinant APH1A can be used to investigate the complex's structural dynamics and facilitate the screening of small molecules that could modulate γ-secretase activity. As a result, ongoing research efforts are focused on optimizing the expression and purification of APH1A to explore its biochemical properties and functional roles in health and disease, ultimately paving the way for innovative approaches in the treatment of Alzheimer's and other related conditions. Understanding APH1A's involvement in γ-secretase function is crucial not only for elucidating the biological processes in the central nervous system but also for identifying potential therapeutic targets that could intervene in the progression of Alzheimer's disease.
