Merck, P2645-1000UN, Protein Kinase A Catalytic Subunit from bovine heart

General description
Protein Kinase A enzyme is composed of two subunits- catalytic and regulatory. The catalytic subunit exists as a monomer in the presence of cAMP and has a molecular weight of 40,862 Da.
Application
Protein Kinase A (PKA) Catalytic Subunit from bovine heart has been used-
to study PKA-mediated inhibition of IRK1 (inwardly rectifying K⁺) channels
in in Vitro PKA pPhosphorylation assay
in Vitro affinity binding assays
to study effects of PKA on inspiratory drive currents in functionally active motorneurons

Biochem/physiol Actions
Protein Kinase A (PKA) controls the transduction of Hedgehog signaling and participates in proliferation and fate specification. It phosphorylates several neurotransmitter receptors, transcription factors and constituents of various intracellular signaling pathways.
Protein Kinase A catalyzes the transfer of terminal phosphate from ATP to threonine or serine residues present on various proteins. This protein is inactive in the absence of cAMP, where the catalytic and regulatory subunits are bound together. The regulatory subunit, in the presence of cAMP, binds to cAMP and releases the catalytic subunit.
Packaging
Package size based on phosphorylating units
Physical form
Lyophilized powder with sucrose and phosphate buffer salts as stabilizer.
Preparation Note
Prepared from protein kinase A (P 5511)
Other Notes
Phosphorylating Activity: One unit will transfer 1.0 picomole phosphate from ATP to hydrolyzed and partially dephosphorylated casein per minute at pH 6.5 at 30°C, determined by measuring the production of ADP.
Disclaimer
Please note that the pack size has been changed to align with the unit definition, while the number of phosphorylating units remain the same as before.