Protein Kinase A regulatory subunit I beta Antibody (N-term)

Synthetic Peptide

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 similari-
ty), whereas 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 transcrip-
tion 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.

Polyclonal

5575

Purified Rabbit Polyclonal Antibody (Pab)

Western blot analysis of anti-PRKAR1B Pab (Cat. #AP7051a) in mouse liver tissue lysate. PRKAR1B (arrow) was detected using purified Pab. Secondary HRP-anti-rabbit was used for signal visualization with chemiluminescence.

1:1000

IHC-P

Rabbit Ig

50-80

This Protein Kinase A regulatory subunit I beta antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 50-80 amino acids from the N-terminal region of human Protein Kinase A regulatory subunit I beta.