Description
Recombinant full-length human PRKAR1B was expressed in Sf9 insect cells using a C-terminal His tag.
Scientific Background: PRKAR1B is the type I-beta regulatory subunit of cyclic AMP-dependent protein kinase A (PKA) which is an essential enzyme in the cAMP signaling pathway. PKA holoenzyme is composed of 2 regulatory and 2 catalytic subunits and dissociates from the regulatory subunits upon binding of cAMP. PKA controls many biochemical events in the cell including regulation of metabolism, ion transport, and gene transcription. PKA undergoes a dramatic conformational change upon complex formation with the catalytic subunit (1). PRKAR1B subunits can dimerize through an N-terminal motif and this dimerization is necessary for binding to PKA anchoring proteins (AKAPs) and targeting of PKA to its site of action