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Recombinant human cAMP-dependent protein kinase: PKA, C alpha, 50 µg  

Recombinant human cAMP-dependent protein kinase: PKA, C alpha, 50 µg

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

Alternate names: PKA, cAMP-dependent protein kinase, PKA C-alpha, PKA Calpha, PKAC, PKACA, PKA-Ca, cAMP dependent protein kinase, PKA catalytic subunit alpha, cAMP-kinase, protein kinase A

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Availability: on stock

255,00 €

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) regulating several 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 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.
The α-isoform is the predominant form with a broad tissue distribution and can be used for in vitro enzymological studies of neural and hormonal signal transduction or to phosphorylate target proteins in vivo (via microinjection) including ion channels, transcriptional activator proteins and regulatory enzymes of glycogen metabolism.
Highly active PKA catalytic subunit recombinantly expressed in E. coli and purified using several chromatographic steps. Preferred peptide substrate is  kemptide (LRRASLG).

Theoretical MW: 41 kDA
Expression system: E. coli
Storage buffer: 20mM MOPS pH7, 150mM NaCl, 1mM DTT, 1mM EDTA, 50% Glycerin
Purity:  >95% (SDS-PAGE)
Protein concentration:  0.16 mg/ml (Bradford method using BSA as standard protein)
Specific activity : >8,000,000 U/mg  (based on kemptide phosphorylation, 1 unit is defined as 1 pmol phosphate per mg and minute.)

Entrez Gene ID: 5566 
UniProtKB: P17612

Ordering information: shipped on dry ice

Also available  for in vitro enzymological studies as component in our PKA in vitro set


Use the PKA - SPR Binding Assay of BIAFFINfor comprehensive kinetic characterization of your small molecule kinase inhibitors. 


Figure: Real-time kinetic analysis of kinase inhibitor H-89 binding to PKA Cα using surface plasmon resonance.

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Product specific literature references:

Taylor SS (1989) "cAMP-dependent protein kinase. Model for an enzyme family" J. Biol. Chem. 264(15):8443-6

Taylor SS, Buechler JA, Yonemoto W (1990) "cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes" Annu. Rev. Biochem. 59:971-1005

Walsh DA, Glass DB, Mitchell RD (1992) "Substrate diversity of the cAMP-dependent protein kinase: regulation based upon multiple binding interactions" Curr. Opin. Cell Biol. 4(2):241-51

Sculptoreanu A, Rotman E, Takahashi M, Scheuer T, Catterall WA (1993) "Voltage-dependent potentiation of the activity of cardiac L-type calcium channel alpha 1 subunits due to phosphorylation by cAMP-dependent protein kinase" Proc. Natl. Acad. Sci. U S A 90 (21): 10135-9

Walsh DA, Van Patten SM (1994) "Multiple pathway signal transduction by the cAMP-dependent protein kinase" FASEB J. 8(15):1227-36

Tasken K, Skalhegg BS, Jahnsen T et al. (1997) "Structure, function, and regulation of human cAMP-dependent protein kinases" Adv. Second Messenger Phosphoprotein Res. 31:191-204

Gray PC, Scott JD, Catterall WA (1998) "Regulation of ion channels by cAMP-dependent protein kinase and A-kinase anchoring proteins" Curr. Opin. Neurobiol. 8(3):330-4

Product Citations:

Leandro J1, Simonsen N, Saraste J, Leandro P, Flatmark T. (2011) "Phenylketonuria as a protein misfolding disease: The mutation pG46S in phenylalanine hydroxylase promotes self-association and fibril formation." Biochim Biophys Acta. 2011 Jan;1812(1):106-20.

Fischer JJ, Dalhoff C, Schrey AK, Graebner OY, Michaelis S, Andrich K, Glinski M, Kroll F, Sefkow M, Dreger M, Koester H. (2011) "Dasatinib, imatinib and staurosporine capture compounds - Complementary tools for the profiling of kinases by Capture Compound Mass Spectrometry (CCMS)." J Proteomics. 75(1):160-8.

Krüger M1, Kötter S, Grützner A, Lang P, Andresen C, Redfield MM, Butt E, dos Remedios CG, Linke WA. (2009) "Protein kinase G modulates human myocardial passive stiffness by phosphorylation of the titin springs." Circ Res. 2009 Jan 2;104(1):87-94.

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