Analytical Data
-
Gene name
PKACα
- Application
-
Alternative Names
/
-
Species
Dog
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8MJ44
-
Expression Region
2-350aa
-
Molecular Weight
43.2 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PKACα, the catalytic subunit of protein kinase A (PKA), plays a crucial role in cellular signaling pathways by phosphorylating various target proteins in response to elevated levels of cyclic AMP (cAMP). As a pivotal enzyme in the regulation of numerous physiological processes, including metabolism, gene expression, and cell proliferation, PKACα's activity is tightly controlled by its interaction with regulatory subunits and other signaling molecules. Dysregulation of PKA signaling has been implicated in a variety of diseases, including cancer, cardiac disorders, and neurodegenerative diseases, highlighting the importance of understanding its structure and function. Research on recombinant PKACα protein has gained momentum, enabling scientists to elucidate its biochemical properties, kinetic behavior, and regulatory mechanisms. By employing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, researchers are able to study the enzyme's conformation and binding interactions in greater detail. Furthermore, the recombinant expression of PKACα offers the opportunity to explore the effects of specific mutations on its activity, providing insights into how alterations in its function may contribute to pathological conditions. Overall, the study of recombinant PKACα is essential for deciphering the complexities of PKA signaling and developing targeted therapies for diseases associated with its dysfunction.
