PKA IIα reg (P68) polyclonal antibody

The second messenger cyclic AMP (cAMP) mediates diverse cellular responses to external signals such as proliferation, ion transport, regulation of metabolism and gene transcription by activation of the cAMP-dependent protein kinase (cAPK or PKA) . Activation of PKA occurs when cAMP binds to the two regulatory subunits of the tetrameric PKA holoenzyme resulting in release of active catalytic subunits. Three catalytic (C) subunits have been identified, designated Cα, Cβ and Cγ, that each represent specific gene products. Cα and Cβ are closely related (93% amino acid sequence similarity), where as Cγ displays 83% and 79% similarity to Cα and Cβ, respectively. Activation of transcription upon elevation of cAMP levels results from translocation of PKA to the nucleus where it phosphorylates the transcription factor cAMP response element binding protein (CREB) on serine 133 which in turn leads to TFIIB binding to TATA-box-binding protein TBP1, thus linking phospho-CREB to the pol II transcription initiation complex.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of PKA IIα reg (P68) pAb at 1:500 dilution Lane1:PC3 whole cell lysate (10ug) Lane2:U-87MG whole cell lysate (10ug) Lane3:The Uterus tissue lysate of Rat (40ug) Lane4:AML-12 whole cell lysate (40ug)