Analytical Data
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Gene name
PPIA
- Application
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Alternative Names
PPIA；CYPA；Peptidyl-prolyl cis-trans isomerase A
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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
P0AFL5
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Expression Region
25-190aa
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AA Sequence
AKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVI PGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSAT SQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQ NVPSKPVVILSAKVLP
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Molecular Weight
34 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
The study of PPIA (Peptidyl-Prolyl Isomerase A), also known as cyclophilin A, has gained significant attention in the field of molecular biology due to its crucial role in protein folding and cellular regulation. PPIA is a member of the peptidyl-prolyl isomerase family, which facilitates the cis-trans isomerization of proline residues in polypeptides, thereby influencing protein conformation and activity. Beyond its fundamental biochemical actions, PPIA has been implicated in various physiological and pathological processes, including immune response, inflammation, and viral replication, particularly in relation to HIV-1, where it acts as a cofactor for the virus's life cycle. Additionally, PPIA has been linked to several disease states, including cancer, where its overexpression is associated with increased tumor growth and poor prognosis. Given its diverse biological functions and relevance to human health, researchers are focused on exploring the potential of PPIA as a therapeutic target. Recent advances in recombinant protein technology have enabled the production of PPIA in various expression systems, allowing for in-depth structural and functional studies. This research not only enhances our understanding of PPIA's multifaceted roles but also paves the way for the development of novel pharmacological interventions aimed at modulating its activity in disease settings.
