Analytical Data
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Gene name
PKIa
- Application
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Alternative Names
PKI-A; PRKACN1; CAMP-Dependent Protein Kinase Inhibitor Alpha; cAMP-dependent protein kinase inhibitor, muscle/brain isoform
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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 90% as determined by SDS-PAGE.
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Uniprot
P61925
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Expression Region
Ala13~Ala71
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Molecular Weight
14kDa
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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
PKIa (Protein Kinase A type I alpha) is a pivotal serine/threonine kinase that plays a critical role in various cellular processes, including metabolism, gene expression, and cell survival. It is a member of the Protein Kinase A (PKA) family, which is regulated by cyclic AMP (cAMP) levels in the cell. The dysregulation of PKIa has been implicated in several pathological conditions, including cancer, cardiovascular diseases, and neurodegenerative disorders, making it a significant focus of biomedical research. Researchers are particularly interested in the functional mechanisms of PKIa and its regulatory pathways to understand how its activity influences cellular signaling. Recent advancements in molecular biology and protein engineering have facilitated the study of PKIa through the development of recombinant proteins, enabling scientists to investigate its structure, function, and interaction with various substrates. This research not only enhances our understanding of PKA signaling but also opens potential therapeutic avenues for targeting PKIa in diseases associated with its dysfunction. The structural characterization and biochemical analysis of recombinant PKIa can provide insights into its activation mechanisms and substrate specificity, which are essential for drug design and the development of targeted therapies. Overall, the study of recombinant PKIa is a promising area of research that holds significant implications for both basic biology and clinical applications.
