Analytical Data
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Gene name
PPIL1
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简介
The PPIL1 protein is a spliceosome component that coordinates pre-mRNA splicing and controls RNA processing. As a peptidylprolyl cis-trans isomerase (PPIase), PPIL1 accelerates protein folding by catalyzing the cis-trans isomerization of proline imide peptide bonds. PPIL1 Protein, Human (His) is the recombinant human-derived PPIL1 protein, expressed by E. coli , with N-6*His labeled tag.
- Application
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Alternative Names
Peptidyl-Prolyl Cis-Trans Isomerase-Like 1; PPIase; Rotamase PPIL1; PPIL1; CYPL1
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Species
Human
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Source
E. coli
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Tag
N-6*His
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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
M1-G166
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Protein Length
Full Length
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Molecular Weight
19-24 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
PPIL1, or peptidylprolyl isomerase-like 1, is a member of the cyclophilin protein family known for its role in protein folding and chaperone activity. Recent studies have highlighted PPIL1's involvement in various cellular processes, including cell proliferation, apoptosis, and response to stress. Its unique isomerase activity, which catalyzes the cis-trans isomerization of proline residues in polypeptides, is crucial for proper protein conformation and function. Dysregulation of PPIL1 has been linked to several diseases, including cancer, where it may influence tumor progression and metastasis. This has attracted interest in developing PPIL1 as a potential therapeutic target. Moreover, the expression patterns of PPIL1 in different tissues and its interactions with other proteins suggest that it may play a significant role in cellular signaling pathways. Recent advances in recombinant protein technology have enabled the production of PPIL1 in laboratory settings, facilitating detailed studies on its structure and function. Understanding the biochemical properties and physiological roles of PPIL1 through its recombinant form could provide insights into its mechanisms of action and contribute to broader applications in biotechnology and medicine. Research into PPIL1 is expanding our knowledge of essential cellular processes and may pave the way for new strategies in treating diseases associated with protein misfolding and dysfunction.
