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Recombinant human cAMP-dependent protein kinase: PKA, C beta1, 25 µg  

Recombinant human cAMP-dependent protein kinase: PKA, C beta1, 25 µg

Recombinant human PKA catalytic subunit type beta,(PKA C beta1), active enzyme

Alternate names: PKA, cAMP-dependent protein kinase, PKA C-beta1, PKA Cbeta1, PRKCB, PKA-Cb1, cAMP dependent protein kinase, PKA catalytic subunit beta, cAMP-kinase, protein kinase A

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Availability: on stock

295,00 €

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.
Three principal genes, PRKACA, PRKACB and PRKX encode the catalytic subunits of PKA Cα, Cβ and PRKX, respectively. Whereas Cα1 is ubiquitously expressed in man, Cα2 is exclusively expressed in the sperm cell. The human Cβ gene encodes six splice variants, designated Cβ1, Cβ2, Cβ3, Cβ4, Cβ4ab and Cβ4abc. The Cβ splice variants differ in their N-terminal ends due to differential splicing and are expressed in the brain of higher primates. Human PKA Cα1 and Cβ1 have the same length (350 residues) and share 93% sequence identity.

Theoretical MW: 41 kDA
Expression system: E. coli
Storage buffer: 20mM MOPS pH7, 150mM NaCl, 1mM DTT, 50% Glycerin
Purity:  >95% (SDS-PAGE)
Protein concentration:  0.65 mg/ml (Bradford method using BSA as standard protein)
Specific activity : >10,000,000 U/mg  (based on kemptide phosphorylation, 1 unit is defined as 1 pmol phosphate per mg and minute.)

Entrez Gene ID: 5579 
UniProtKB: P05771

Ordering information: shipped on dry ice

Product specific literature references:

Maldonado, F., and S.K. Hanks. (1988) A cDNA clone encoding human cAMP-dependent protein kinase catalytic subunit C alpha. Nucleic Acids Res. 16:8189-90.

Olsen, S.R., and M.D. Uhler. 1989. Affinity purification of the C alpha and C beta isoforms of the catalytic subunit of cAMP-dependent protein kinase. J Biol Chem. 264:18662-6.

Shuntoh, H., N. Sakamoto, S. Matsuyama, M. Saitoh, and C. Tanaka. 1992. Molecular structure of the C beta catalytic subunit of rat cAMP-dependent protein kinase and differential expression of C alpha and C beta isoforms in rat tissues and cultured cells. Biochim Biophys Acta. 1131:175-80.

Funderud A, Aas-Hanssen K, Aksaas AK, Hafte TT, Corthay A, Munthe LA, Orstavik S, Skålhegg BS (2009).”Isoform-specific regulation of immune cell reactivity by the catalytic subunit of protein kinase A (PKA).” Cell Signal.21(2):274-81

Søberg K, Jahnsen T, Rognes T, Skålhegg BS, Laerdahl JK.(2013) “Evolutionary paths of the cAMP-dependent protein kinase (PKA) catalytic subunits.” PLoS One. 12;8(4):e60935.

Guthrie CR1, Skâlhegg BS, McKnight GS.(1997) “Two novel brain-specific splice variants of the murine Cbeta gene of cAMP-dependent protein kinase.” J Biol Chem. 21;272(47):29560-5.

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