cAMP-Dependent Protein Kinase A regulatory subunit-II A, PKA-RII alpha.
Introduction
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.
Description
The recombinant PKA regulatory subunit II-a is a dimeric 90 kDa protein.
Protein Kinase A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered clear solution.
Formulation
PKA regulatory subunit-II alpha is supplied at a concentration of 0.37mg/ml in 20mM MES, 150mM NaCl, 2mM EDTA, 2mM EGTA, 1mM BME and 50% glycerol.
Inhibitory Activity
The cAMP-Dependent Protein Kinase, regulatory subunit RIIa reversibly inhibits the catalytic subunit Ca of the cAMP-dependent protein kinase PKA. The inhibition of the catalytic subunit can be reversed by the addition of the second messenger cAMP (> 1uM).
Stability
PKA should be stored at 4°C if entire vial will be used within 1 week. For long term storage below -20°C.
Prospecs products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.