Analytical Data
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Gene name
PSARL
- Application
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Alternative Names
PARL; PSARL; PRO2207; Presenilins-associated rhomboid-like protein. mitochondrial; Mitochondrial intramembrane cleaving protease PARL
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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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
1-379 aa
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AA Sequence
MAWRGWAQRGWGCGQAWGASVGGRSCEELTAVLTPPQLLGRRFNFFIQQKCGFRKAPRKVEPRRSDPGTSGEAYKRSALIPPVEETVFYPSPYPIRSLIKPLFFTVGFTGCAFGSAAIWQYESLKSRVQSYFDGIKADWLDSIRPQKEGDFRKEINKWWNNLSDGQRTVTGIIAANVLVFCLWRVPSLQRTMIRYFTSNPASKVLCSPMLLSTFSHFSLFHMAANMYVLWSFSSSIVNILGQEQFMAVYLSAGVISNFVSYVGKVATGRYGPSLGASGAIMTVLAAVCTKIPEGRLAIIFLPMFTFTAGNALKAIIAMDTAGMILGWKFFDHAAHLGGALFGIWYVTYGHELIWKNREPLVKIWHEIRTNGPKKGGGSK
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Molecular Weight
68.6 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
The study of PSARL (proline-serine-rich alkaline protein) recombinant protein emerges from the growing interest in understanding the functional roles of proline-rich proteins in cellular processes. PSARL is characterized by its unique structure, which includes proline and serine-rich domains, making it a subject of interest in various biological contexts, particularly in cell signaling, stress response, and development. Research has indicated that PSARL may play a critical role in modulating protein interactions and cellular functions due to its distinctive biochemical properties. The recombinant expression of PSARL allows for detailed studies of its structure-function relationships and its potential implications in health and disease. Furthermore, insights gained from PSARL research could aid in the development of novel therapeutic strategies for conditions related to protein misfolding or dysregulation, given the increasing recognition of the significance of post-translational modifications in cellular physiology. The exploration of PSARL is poised to contribute valuable knowledge to the fields of molecular biology and biochemistry, enhancing our understanding of complex cellular mechanisms.











