Analytical Data
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Gene name
Cyclophilin F/PPIF 蛋白
- Application
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Alternative Names
PPI-F; CYP3; Cyp-D; CyP-M; Peptidyl-Prolyl Cis-Trans Isomerase,Mitochondrial; Cyclophilin F; Mitochondrial cyclophilin; Rotamase F
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P30405
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Expression Region
Asn45~Lys196
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Molecular Weight
20kDa
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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
Cyclophilin F (CYPF), also known as peptidyl-prolyl isomerase F (PPIF), is a member of the cyclophilin family of proteins, which play critical roles in protein folding, signal transduction, and cellular stress responses. CYPF is particularly notable for its involvement in various cellular processes, including apoptosis, immunological responses, and mitochondrial function. Its isomerase activity facilitates the folding of polypeptides, contributing to proper protein conformation and function. Research has shown that CYPF is implicated in several diseases, including cancer and neurodegenerative disorders, linking its dysfunction to various pathological conditions. The recombinant expression of CYPF allows for detailed studies of its biochemical properties and functional roles, providing valuable insights into its mechanism of action. Furthermore, understanding the structure and function of CYPF through recombinant technology can aid in the development of therapeutic strategies targeting its pathways. Given its involvement in critical cellular processes and potential as a drug target, the study of recombinant CYPF not only enhances our fundamental understanding of protein biology but also opens avenues for therapeutic intervention in diseases where CYPF is implicated.
