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Description
The cAMP-dependent protein kinase (PKA) is a critical kinase involved in numerous biological functions. The PKA holoenzyme is composed of two regulatory and two catalytic subunits, designated PKA R and PKA C, respectively. For PKA C, three catalytic subunit isoforms, Calpha, Cbeta, and Cgamma, have been identified. On the other hand, PKA regulatory (PKA R) subunits existing as two classes, RI and RII, with each class containing two isoforms, alpha and beta are found in different levels in tissue-pecific manner. They allow a range of modifying agents to influence PKA activity and localization. Upon the binding of PKA R subunit with secondary messenger cAMP, active PKA C subunits are released, initiating a phosphorylation cascade that regulates many cellular functions including metabolism, ion transport, and gene transcription.Rabbit Anti-PKA RIbeta Polyclonal Antibody is developed in rabbit using a synthetic peptide (KLH-coupled) derived from human PKA regulatory Ibeta subunit (PKA RIbeta).
Immunogen
Synthetic peptide (KLH-coupled) derived from human PKA regulatory Iβ subunit (PKA RIβ).