Analytical Data
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Gene name
PRKX
- Application
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Alternative Names
PKX1; cAMP-dependent protein kinase catalytic subunit PRKX
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Species
Rat
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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
Q5BK52
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Expression Region
Trp49~Phe358
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Molecular Weight
43kDa
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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
PRKX, a member of the Protein Kinase family, has garnered attention in recent years due to its potential role in various biological processes and disease mechanisms. Initially identified for its involvement in cellular signaling pathways, PRKX has been implicated in fundamental processes such as cell growth, differentiation, and apoptosis. Its atypical structure and unique regulatory mechanisms set it apart from other kinases, prompting researchers to explore its functional dynamics in greater detail. Investigations into PRKX have revealed its involvement in several pathological conditions, including cancer and cardiovascular diseases, suggesting that dysregulation of PRKX activity may contribute to tumorigenesis and other disease states. The development of recombinant PRKX proteins has enabled scientists to conduct detailed biochemical and biophysical studies, facilitating the elucidation of its signaling networks. Continued research on PRKX is critical for understanding its role in health and disease, with the potential to unveil novel therapeutic targets for intervention in PRKX-associated disorders. Overall, the study of PRKX and its recombinant proteins stands at the forefront of molecular biology, promising to enhance our comprehension of kinase signaling and its implications in various physiological and pathological contexts.
