Analytical Data
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Gene name
PPIF
- Application
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Alternative Names
PPIF；CYP3;Peptidyl-prolyl cis-trans isomerase F. 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
P30405
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Expression Region
30-207aa
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AA Sequence
C SKGSGDPSSS SSSGNPLVYL DVDANGKPLG RVVLELKADV VPKTAENFRA LCTGEKGFGY KGSTFHRVIP SFMCQAGDFT NHNGTGGKSI YGSRFPDENF TLKHVGPGVL SMANAGPNTN GSQFFICTIK TDWLDGKHVV FGHVKEGMDV VKKIESFGSK SGRTSKKIVI TDCGQLS
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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
PPIF (peptidylprolyl isomerase F) is an important member of the cyclophilin family, which plays a critical role in various cellular processes, including protein folding, signal transduction, and apoptosis. Its involvement in the regulation of mitochondrial functions and association with diseases such as cancer and neurodegenerative disorders has spurred significant interest in studying PPIF. The protein's isomerase activity, which facilitates the trans-cis isomerization of proline residues in peptide bonds, is crucial for maintaining proper protein conformation and function. Researchers have aimed to characterize the properties of PPIF and explore its potential as a therapeutic target, especially considering its role in mitigating oxidative stress and modulating cell survival pathways. Recent advancements in recombinant protein technology have enabled the efficient expression and purification of PPIF in various systems, paving the way for detailed structural and functional analyses. Studies focusing on PPIF's biochemical activities and interaction partners have provided insights into its cellular roles, thus enhancing our understanding of its implications in health and disease. Ultimately, the exploration of PPIF as a therapeutic target could lead to novel strategies for treating conditions associated with protein misfolding and mitochondrial dysfunction.
