PKA, Catalytic Subunit, Bovine Heart

Protein kinases are crucial for integrating signaling networks within eukaryotic cells. It plays an essential role in regulating proliferation and fate determination by influencing Hedgehog signaling transduction. Upon binding of cAMP to the PKA regulatory subunits, the catalytic subunit of PKA dissociates from the PKA holoenzyme and proceeds to phosphorylate target proteins at serine and/or threonine within the recognition motif, Arg-Arg-X-Ser*-X. The purified monomeric catalytic subunit is capable of activation without the need for cAMP and is well-suited for in vitro studies of PKA phosphorylation with purified substrates or when introduced into intact cells or cell extracts.

Toxicity: Standard Handling (A)

Research area: Cell Signaling

Native PKA catalytic subunit purified from bovine heart. Protein Kinase A (PKA) is a serine protein kinase that targets serine and threonine residues.

Corbin, J.D., et al. 1988. Methods Enzymol159, 74.
Rannels, S.R., et al 1983. Methods Enzymol99, 55.
Witt, J.J. and Roskoski, R. Jr. 1975. Anal Biochem.66, 253.

One unit is defined as the amount of enzyme required to incorporate 1 pmol phosphate into Kemptide substrate (Cat. No. 05-23-4900) per min at 30°C.

Please refer to vial label for lot-specific concentration.

In 350 mM K₂HPO₄, 100 µM DTT, pH 6.8.

Following initial thaw, aliquot and freeze (-70°C).

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany