Analytical Data
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Gene name
PPIAL4A
- Application
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Alternative Names
Chromosome one-amplified sequence 2 Short name: COAS-2 Cyclophilin homolog overexpressed in liver cancer
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y536
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Expression Region
1-164aa
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Molecular Weight
34.2 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
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Protein Description
PPIAL4A, a member of the peptidylprolyl isomerase family, has garnered significant interest due to its potential roles in various biological processes and diseases. This protein is known to facilitate the folding of proteins by catalyzing the isomerization of prolyl bonds, a critical step in the proper assembly of polypeptides. Recent studies have linked PPIAL4A to cancer biology, where its overexpression has been associated with tumor progression and poor prognosis in several types of malignancies. Additionally, PPIAL4A’s involvement in cellular stress responses and regulatory pathways suggests it may play a role in the maintenance of protein homeostasis. Understanding the structure and function of PPIAL4A through the generation of recombinant proteins is crucial for elucidating its biological mechanisms and potential applications in targeted therapies. Precise manipulation of this protein could pave the way for developing novel strategies to combat diseases characterized by protein misfolding and dysregulation. Therefore, ongoing research focuses on the characterization of PPIAL4A’s enzymatic activity, interaction with other cellular proteins, and its impact on cellular signaling pathways, providing insights into its functional significance and therapeutic potential.
