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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. PKA regulatory (PKA R) subunits exist as two classes, RI and RII, with each class containing two isoforms, alpha and beta. Three catalytic subunit isoforms, Calpha, Cbeta, and Cgamma, have been identified. The PKA R subunits allow a range of modifying agents to influence PKA activity and localization, and are found in different levels in a tissue-specific manner. Upon PKA R subunit binding to the second messenger cAMP, active PKA C subunits are released, initiating a phosphorylation cascade that regulates such cellular functions as metabolism, ion transport, and gene transcription.Rabbit Anti-PKA RIIbeta Polyclonal Antibody is developed in rabbit using a synthetic peptide (KLH-coupled) derived from human PKA regulatory IIbeta subunit (PKA RIIbeta).
Immunogen
Synthetic peptide (KLH-coupled) derived from human PKA regulatory IIβ subunit (PKA RIIβ)