Analytical Data
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Gene name
PPIE
- Application
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Alternative Names
PPIE;CYP33;Peptidyl-prolyl cis-trans isomerase E
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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
Q9UNP9
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Expression Region
1-301aa
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AA Sequence
MATTKRVLYV GGLAEEVDDK VLHAAFIPFG DITDIQIPLD YETEKHRGFA FVEFELAEDA AAAIDNMNES ELFGRTIRVN LAKPMRIKEG SSRPVWSDDD WLKKFSGKTL EENKEEEGSE PPKAETQEGE PIAKKARSNP QVYMDIKIGN KPAGRIQMLL RSDVVPMTAE NFRCLCTHEK GFGFKGSSFH RIIPQFMCQG GDFTNHNGTG GKSIYGKKFD DENFILKHTG PGLLSMANSG PNTNGSQFFL TCDKTDWLDG KHVVFGEVTE GLDVLRQIEA QGSKDGKPKQ KVIIADCGEY V
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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 PPIE (Peptidyl-Prolyl Isomerase E) protein plays a crucial role in various cellular processes, including cell signaling, protein folding, and stress responses. Recent research has shown that PPIE is involved in critical biological functions, such as cell cycle regulation and immune response modulation. Dysregulation of PPIE has been linked to various diseases, including cancer and neurodegenerative disorders. Given the increasing awareness of its significance, scientists are focusing on understanding the molecular mechanisms underlying its function. Studies involving the reconstituted form of PPIE have enabled researchers to investigate its structure-function relationship more thoroughly. This includes exploring how alterations in its conformation can affect cellular pathways and influence disease progression. The development of recombinant PPIE proteins has allowed for detailed biochemical assays, high-throughput screening, and potential therapeutic applications. Moreover, the integration of advanced technologies such as cryo-electron microscopy and nuclear magnetic resonance has provided deeper insights into the protein's dynamics. By elucidating the role of PPIE in cellular homeostasis and disease, researchers aim to identify novel therapeutic targets and strategies to combat associated pathologies. Overall, the study of PPIE and its reconstituted protein forms represents a promising frontier in molecular biology, with significant implications for understanding and treating various human diseases.
