Mouse Anti-Human PRKACA/PKA Catalytic Clone 3B2 mAb

Store at -20C

Protein Kinase A (PKA) is a cyclic-AMP dependent kinase and a member of the serine/threonine family of protein kinases. Three catalytic isoforms of PKA have been described (alpha, beta, gamma), and isoform expression is tissue specific. PKA is expressed in the cytoplasm as an inactive holoenzyme and is translocated to the nucleus upon activation. PKA is activated by cAMP intracellular signaling, four cAMP molecules bind to inactive PKA holoenzyme to release catalytic and regulatory domains. PKA phosphorylates a large number of substrates in the nucleus and cytoplasm and is involved in cell growth, differentiation, and homeostasis. PKA can be modified by phosphorylation and myristylation. The PKA catalytic domain interacts with inflammation-responsive factor serum amyloid A-activating factor, and caveolin-1.

Peptide-KLH

Human