Analytical Data
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Gene name
PSEN1
- Application
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Alternative Names
FAD; AD3; PS1; PSNL1; S182; Alzheimer Disease 3; Protein S182; Presenilin-1 CTF12
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49768
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Expression Region
Ser254~Arg377
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Molecular Weight
20kDa
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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
The study of PSEN1 (Presenilin-1), a key component of the γ-secretase complex, is pivotal in understanding Alzheimer's disease (AD), particularly familial forms of the disorder. PSEN1 mutations are among the most common genetic factors linked to early-onset AD, as they disrupt normal amyloid precursor protein (APP) processing, leading to the accumulation of neurotoxic amyloid-beta (Aβ) peptides in the brain. As a result, researchers are investigating PSEN1 recombinant proteins to elucidate the molecular mechanisms underlying its function and the impact of pathogenic mutations. By expressing and characterizing PSEN1 variants in vitro, scientists aim to explore how specific mutations alter the protein's conformation, enzymatic activity, and interaction with other components of the γ-secretase complex. Such studies are essential for designing targeted therapeutic strategies and potential interventions to mitigate the destructive pathways activated by aberrant Aβ accumulation. Additionally, the ability to produce recombinant PSEN1 proteins in sufficient quantities allows for further biochemical assays and drug screening efforts, promoting advancements in the development of effective treatments for Alzheimer's disease and related neurodegenerative disorders.
