Analytical Data
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Gene name
PPIase A
- Application
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Alternative Names
Cyclophilin ACyclosporin A-binding proteinRotamase A
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62937
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Expression Region
2-165aa
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Molecular Weight
17.9 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
Related Products
Protein Description
PPIase A, also known as peptidyl-prolyl isomerase A, is an important enzyme that catalyzes the cis-trans isomerization of prolyl bonds in peptides and proteins, which is a crucial step in protein folding and function. Its role in various biological processes, including cell signaling, immune responses, and disease mechanisms, has attracted significant research interest. Aberrant PPIase A activity is implicated in several pathological conditions, such as neurodegenerative diseases, cancer, and autoimmune disorders. The recombinant expression of PPIase A has enabled researchers to study its structure-function relationships and investigate its potential as a therapeutic target. By producing PPIase A in heterologous systems, scientists can obtain larger quantities of the enzyme for biochemical assays, structural biology studies, and drug screening. Recent advancements in recombinant DNA technology and protein engineering have further facilitated the exploration of PPIase A’s mechanisms of action, interactions with other biomolecules, and its regulatory pathways. These studies provide insights into the enzyme's potential as a drug target and its application in biotechnological innovations, thus underscoring the significance of recombinant PPIase A research in both basic science and applied fields.
