|ChIP assay (ChIP)||1:100|
|Western Blot (WB)||Assay Dependent|
|Tested Species reactivity||Mouse|
|Host / Isotype||Rabbit / IgG|
|Immunogen||The antiserum was produced against a chemically synthesized phosphopeptide derived from a region of human PKA catalytic b subunit that contains serine 338. The sequence is conserved in cow and pig.|
|Purification||Antigen affinity chromatography|
|Storage buffer||Dulbecco's PBS, pH 7.3, with 1mg/ml BSA, 50% glycerol|
|Contains||0.05% sodium azide|
44-992G has been used successfully in the ChIP analysis of PKA beta pS338.
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. PRKACB is a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: beta-catalytic subunit; cAMP-dependent protein kinase; cAMP-dependent protein kinase C beta; cAMP-dependent protein kinase catalytic subunit beta; PKA C-beta
Gene Aliases: Pkacb; Prkacb
UniProt ID: (Mouse) P68181
Entrez Gene ID: (Mouse) 18749
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