Analytical Data
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Gene name
PPIL1
- Application
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Alternative Names
PPIL1；CYPL1；Peptidyl-prolyl cis-trans isomerase-like 1
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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
Q9Y3C6
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Expression Region
1-166aa
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AA Sequence
MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSG
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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
PPIL1 (Peptidyl-Prolyl Isomerase Like 1) is a member of the parvulin-type peptidyl-prolyl isomerase family, which plays a significant role in protein folding and cellular stress responses. Its involvement in various biological processes, including T cell activation, apoptosis, and cancer progression, has garnered attention in molecular biology and pharmacology. Recent research indicates that PPIL1 may function as a regulatory factor in cellular signaling pathways, influencing key cellular functions and contributing to disease mechanisms. The interest in PPIL1 is further heightened due to its potential as a therapeutic target; inhibiting its isomerase activity might offer novel strategies for treating diseases characterized by aberrant protein folding or autoimmune disorders. Investigating the structural and functional properties of recombinant PPIL1 protein can provide insights into its mechanism of action and facilitate the development of targeted therapies. As a recombinant protein, PPIL1 can be produced in microbial or mammalian systems, allowing for biochemical studies that elucidate its role in health and disease. Understanding PPIL1's multifaceted functions is crucial, as it may lead to breakthroughs in drug design and therapeutic interventions for conditions linked to dysregulated protein folding and immune responses. This research continues to be a significant focus within the fields of cellular biology, immunology, and therapeutic development, as the implications of PPIL1's functions extend to a wide range of pathological conditions.
