Western blot: 0.5-4 μg/mL, Jukat cell lysate can be used as a positive control. Immunoprecipitation: 20-30 μg/mL. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Protein kinase A (PKA) also known as cAMP-dependent protein kinase, is a 40 kDa protein kinase that phosphorylates serine or threonine residues in target proteins in response to elevated levels of cAMP. The second messenger cAMP is produced in response to a wide variety of hormones & neurotransmitters and regulates cellular processes such as cell growth and differentiation, ion channel conductivity, synaptic release of neurotransmitters & gene transcription. The principle intracellular target for cAMP is PKA. Inactive PKA exists as a tetrameric protein composed of two regulatory (R) subunits and two catalytic (C) subunits. Activation occurs when two cAMP molecules bind to each R subunit which causes a conformational change that releases the active C subunits. Two major PKA isozymes, type I (PKAI) and type II (PKAII) consist of RI and RII respectively, complexed with C. Three different C subunits (alpha, beta, and gamma) and four different R subunits (RI-alpha, RI-beta, RII-alpha, and RII-beta) have been identified. It has been suggested that the complex structure of PKA may be necessary for it to accomplish such diverse functions.Synonyms: PKA C-alpha, cAMP-dependent protein kinase catalytic subunit alpha