Analytical Data
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Gene name
Peptidyl-prolyl cis-trans isomerase A/CYPA
- Application
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Alternative Names
PPIA; CyP-A; CYPH; Peptidylprolyl Isomerase A; Peptidyl-Prolyl Isomerase A; Peptidyl-prolyl cis-trans isomerase A; Cyclosporin A-binding protein
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Species
Bovine
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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
P62935
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Expression Region
Val2~Ile164
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Molecular Weight
19kDa
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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
Peptidyl-prolyl cis-trans isomerase A (CYPA) is a crucial enzyme that catalyzes the isomerization of proline residues in polypeptides, thereby facilitating protein folding and conformational changes. This isomerization process plays a significant role in the maturation of various proteins, including those involved in key cellular processes such as signal transduction and immune response. The study of CYPA has gained importance due to its implications in several diseases, including cancers and viral infections, as it has been shown to assist in the lifecycle of various viruses, including HIV. Moreover, CYPA functions as a chaperone that assists in the stabilization of certain proteins under stress conditions. Research into the recombinant form of CYPA not only provides insights into its biochemical properties and mechanisms but also opens avenues for therapeutic applications. The ability to produce recombinant CYPA in a laboratory setting allows for detailed studies on its enzymatic activity, interaction with ligands, and role in protein-protein interactions. Such investigations can lead to the identification of novel inhibitors that may serve as potential therapeutic agents against diseases where CYPA is implicated. Overall, the study of recombinant CYPA is fundamental to understanding its pivotal role in cellular biology and its potential as a target for drug development.
