Recombinant rabbit monoclonal antibodies are produced using in vitro expression systems. The expression systems are developed by cloning in the specific antibody DNA sequences from immunoreactive rabbits. Then, individual clones are screened to select the best candidates for production. The advantages of using recombinant rabbit monoclonal antibodies include: better specificity and sensitivity, lot-to-lot consistency, animal origin-free formulations, and broader immunoreactivity to diverse targets due to larger rabbit immune repertoire.
cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of AMPK.
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Protein Aliases: cAMP-dependent protein kinase regulatory subunit RII alpha; cAMP-dependent protein kinase type II-alpha regulatory subunit; cAMP-dependent protein kinase, regulatory subunit alpha 2; MGC3606; protein kinase A, RII-alpha subunit; protein kinase cAMP-dependent regulatory type II alpha; protein kinase, cAMP-dependent, regulatory subunit type II alpha; protein kinase, cAMP-dependent, regulatory, type 2, alpha; unnamed protein product
Gene Aliases: 1110061A24Rik; AI317181; AI836829; PKR2; PRKAR2; PRKAR2A; RII(alpha)