Analytical Data
-
Gene name
PRKACG
- Application
-
Alternative Names
PRKACG; protein kinase, cAMP-dependent, catalytic, gamma; cAMP-dependent protein kinase catalytic subunit gamma; PKACg; PKA C-gamma; serine(threonine) protein kinase; KAPG
-
Species
Human
-
Source
Baculovirus
-
Tag
Tag Free
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P22612
-
Expression Region
G2-F351
-
Protein Length
Full Length of Mature Protein
-
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
PRKACG, or Protein Kinase A Catalytic Subunit Gamma, is a member of the protein kinase A (PKA) family, which plays a crucial role in various cellular processes by mediating the effects of cyclic AMP (cAMP). Research into PRKACG has gained momentum due to its involvement in signal transduction pathways that regulate essential cellular functions, such as metabolism, gene transcription, and cell proliferation. Dysregulation of PRKACG activity has been linked to several diseases, including cancer, cardiovascular disorders, and neurological conditions, which underscores its potential as a therapeutic target. The functional characterization of PRKACG, especially in the context of recombinant protein expression, has enabled scientists to examine its enzymatic activity, substrate specificity, and role in cellular signaling cascades. Advances in recombinant DNA technology have facilitated the production of PRKACG, allowing for in-depth studies on its structure-function relationship, interactions with other signaling molecules, and modulation by various pharmacological agents. Understanding the biochemical properties and biological significance of PRKACG is pivotal for unraveling its contribution to health and disease, thus highlighting the importance of ongoing research in this area.
