cAMP-dependent protein kinase catalytic subunit gamma, PKA C-gamma, PRKACG
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. This protein, the gamma-catalytic subunit, is a member of the Ser/Thr protein kinase family. The gene is intronless and is thought to be a retrotransposon derived from the gene for the alpha form of the catalytic subunit.
Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
Target:
The synthetic peptide sequence used to generate the antibody AP7014a was selected from the N-term region of human PKA/C gamma . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
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