Analytical Data
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Gene name
PARL
- Application
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Alternative Names
(Mitochondrial intramembrane cleaving protease PARL)
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Species
Human
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Source
E. coli
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Tag
C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H300
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Expression Region
53-379aa
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Molecular Weight
37.8 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
PARL (Presenilin-Associated Rhomboid-Like protein) is a mitochondrial intramembrane protease that plays a crucial role in various cellular processes, including mitochondrial dynamics, apoptosis, and the regulation of mitochondrial membrane potential. Research on PARL has gained momentum due to its involvement in crucial pathways, particularly in the context of neurodegenerative diseases like Alzheimer's. Mutations in PARL have been linked to impaired protein quality control and mitochondrial dysfunction, exacerbating pathology in neurodegenerative conditions. Additionally, PARL is implicated in the regulation of the β-secretase cleavage of APP (Amyloid Precursor Protein), a critical event in the production of amyloid-β, a key player in Alzheimer's disease progression. Understanding the structure and function of PARL, especially its enzymatic mechanisms and substrate specificity, is essential for elucidating its role in health and disease. Studies employ advanced biochemical and biophysical techniques, such as X-ray crystallography and cryo-electron microscopy, to characterize PARL's architecture and interactions with substrates and co-factors. The promise of targeting PARL in therapeutic strategies for mitochondrial-related disorders and Alzheimer’s disease underlines the importance of ongoing research in this field, as modulating its activity may pave the way for innovative treatments and a deeper comprehension of mitochondrial biology in health and disease contexts.
