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- Sample Cell Lysates, Purified Systems
- Time to Answer 3 Hours
- Samples/Kit 42 in Duplicate
- Stability Fully Active PKA Standard Stored at -20ºC
- Readout Colorimetric, 450 nm
- Standard Curve
The expressed PKA holoenzyme, comprising of two catalytic (C) and two regulatory (R) subunits, is activated when cAMP levels rise following stimulation of G Protein-coupled receptors and adenylyl cyclase. The phosphorylation of specific substrates by the C subunit of activated PKA is regulated by the subcellular localization of the enzyme through the binding to the scaffolding A kinase-anchoring proteins (AKAPs). In its inactive state, the pseudosubstrate sequences on the R subunits stop the activity of the C subunits. Upon binding of cAMP to the R subunits, the active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC. Substrates that are phosphorylated by PKA include Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK -3β Ser9). PKA is a pivotal kinase involved in cancer, vasodilation, metabolic processes, etc.