ab59218 was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific phosphopeptide. The antibody against
non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
1/50 - 1/100.
1/500 - 1/1000. Detects a band of approximately 41 kDa (predicted molecular weight: 41 kDa).
PRKACA and PRKACB are members of the Ser/Thr protein kinase family and are a catalytic subunit of cAMP-dependent protein kinase. cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme 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.
Cytoplasm. Nucleus. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm
ab59218 at 1/50 dilution staining PKA alpha + beta (catalytic subunit) in human colon carcinoma by Immunohistochemistry, Paraffin embedded tissue, in the absence (left) or presence (right) of the immunising peptide.
Western blot - Anti-PKA alpha + beta (catalytic subunits) (phospho T197) antibody (ab59218)
All lanes : Anti-PKA alpha + beta (catalytic subunits) (phospho T197) antibody (ab59218) at 1/500 dilution
Lane 1 : mouse brain cell extract Lane 2 : mouse brain cell extract with immunising peptide
Predicted band size: 41 kDa Observed band size: 41 kDa