Analytical Data
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Gene name
PARL
- Application
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Alternative Names
PARL；PSARL；Presenilin-associated rhomboid-like Protein. mitochondrial
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
FRKAPRKVEPRRSDPGTSGEAYKRSALIPPVEETVFYPSPYPIRSLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVLVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYVGKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK
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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
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Protein Description
PARL (Presenilin-Associated Rhomboid-Like protein) is a mitochondria-associated protease that plays a crucial role in maintaining mitochondrial function and regulating cellular homeostasis. Research into PARL has gained momentum due to its involvement in key biological processes such as apoptosis, mitochondrial dynamics, and protein quality control. Its dysregulation has been implicated in various neurodegenerative diseases, including Alzheimer's disease, where it interacts with presenilin proteins, affecting amyloid-β production. Recent studies have focused on understanding the structural and functional characteristics of PARL, as well as its substrate specificity, to elucidate its role in pathophysiological contexts. Investigations into PARL's enzymatic activity and the regulatory mechanisms governing its function may provide new insights into potential therapeutic strategies for mitochondrial dysfunction and neurodegeneration. Given the increasing recognition of the mitochondria's role in disease processes, PARL's research is positioned at the intersection of cell biology and neurobiology, promising to uncover novel pathways for intervention in age-related and degenerative disorders.
