Recombinant human cAMP-dependent protein kinase: PKA, RI beta, 25 µg

Background: cAMP-dependent protein kinase (PKA) is an ubiquitous serine/theonine protein kinase present in a variety of tissues (e.g. brain, skeletal muscle, heart). The intracellular cAMP level regulates cellular responses by altering the interaction between the catatytic C and regulatory R subunits of PKA. The inactive tetrameric PKA holoenzyme R2C2 is activated when cAMP binds to R2, which dissociates the tetramer to R2*cAMP4 and two active catalytic subunits. Free Catalytic subunits of PKA can phosphorylate a wide variety of intracellular target proteins. In response to hormone-induced high cAMP levels, PKA phosphorylates glycogen synthetase (inhibition of the enzyme activity) and phosphorylase kinase to block glycogen synthesis. Different isoforms of catalytic and regulatory subunits suggest specific functions. The recombinant RIβ regulatory subunit supplied by Biaffin is a 86 kDa dimeric protein (monomer 43 kD).

Theoretical MW: 86 kDA (dimeric protein)
Expression system: E. coli
Storage buffer: 20 mM Mops (pH 7.0), 150 mM NaCl, 20% glycerol
Purity:  >95% (SDS-PAGE)
Protein concentration:  1.7 mg/ml (Bradford method using BSA as standard protein)

Inhibitory Activity:
The cAMP-dependent protein kinase, regulatory subunit RIβ reversibly inhibits the catalytic subunit Cα of the cAMP-dependent protein kinase PKA. The inhibition of the catalytic subunit can be reversed by the addition of the second messenger cAMP (> 1µM).

Ordering information: shipped on dry ice

Entrez Gene ID: 5575
UniProtKB:  P31321

Product specific literature references:

Solberg R, Tasken K, Keiserud A, Jahnsen T. (1991) “Molecular cloning, cDNA structure and tissue-specific expression of the human regulatory subunit RI beta of cAMP-dependent protein kinases.” Biochem Biophys Res Commun. 15;176(1):166-72.

Solberg, R., Sistonen, P., Traskelin, A.L., Berube, D.,Simard, J., Krajci, P., Jahnsen, T. and de la Chapelle, A.(1992). “Mapping of the regulatory subunits RI beta and RII beta of cAMP-dependent protein kinase genes on human chromosome 7”. Genomics 14(1): 63-9.

Solberg, R., Tasken, K., Wen, W., Coghlan, V.M., Meinkoth, J.L., Scott, J.D., Jahnsen, T. and Taylor, S.S. (1994). “Human regulatory subunit RI beta of cAMPdependent protein kinases: expression, holoenzyme formation and microinjection into living cells”. Experimental Cell Research 214(2): 595-605.

Tasken, K., Skalhegg, B.S., Solberg, R., Andersson, K.B., Taylor, S.S., Lea, T., Blomhoff, H.K., Jahnsen, T. and Hansson, V. (1993). “Novel isozymes of cAMPdependent protein kinase exist in human cells due to formation of RI alpha-RI beta heterodimeric complexes.” Journal of Biological Chemistry 268(28): 21276-83.

Clegg, C.H., H.S. Haugen, and L.F. Boring. (1996) “Promoter sequences in the RI beta subunit
gene of cAMP-dependent protein kinase required for transgene expression in mouse
brain.” J Biol Chem. 271:1638-44.