Synthetic phosphopeptide derived from human PKAalpha around the phosphorylation site of Threonine 197.
Conjugation:
Unconjugated
Alternative Names:
cAMP-dependent protein kinase catalytic subunit alpha, PKA C-alpha, PRKACA, PKACA, PKA Ca, cAMP-dependent protein kinase catalytic subunit beta, PKA C-beta, PRKACB, PKACB, PKA Cb,
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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200
Application Notes:
p-PKAalpha/beta cat (T197) polyclonal antibody detects endogenous levels of PKAalpha/betacat protein when phosphorylated at Thr197.
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