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| Alternative Name : |
cAMP-Dependent Protein Kinase A regulatory subunit-II A, PKA-RII alpha. |
| Amount : |
3 µg |
Source : Escherichia Coli.
The recombinant PKA regulatory subunit II-a is a dimeric 90 kDa protein. Protein Kinase A is purified by proprietary chromatographic techniques.
cAMP-dependent PKA is a 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 cAMP 4 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.
