MyBioSource.com's PRKAR1A Polyclonal Antibody is a Rabbit Polyclonal antibody. This antibody has been shown to work in applications such as: Immunofluorescence, Immunohistochemistry, and Western Blot. The PRKAR1A Polyclonal Antibody was generated using CNC1, PRKAR1A, and protein kinase cAMP-dependent type 1 regulatory subunit alpha as the antigen and it reacts with Human, Mouse, and Rat.
Description
The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-alpha, C-beta, and C-gamma) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, alpha and beta (RI-alpha, RI-beta, RII-alpha, and RII-beta). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3alpha Ser21 and GSK-3beta Ser9) (3-5). In addition, combined knock-down of PKA C-alpha and -beta blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7)