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Peptide Competition. Lysates prepared from 3T3-L1 cells were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were either treated with lambda phosphatase (1) or left untreated (2-5), blocked with a 5% BSA-TBST buffer for two hours at room temperature, and incubated with PKA cat beta [pS338] antibody for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1, 2), the non-phosphopeptide corresponding to the immunogen (3), a generic phosphoserine-containing peptide (4), or, the phosphopeptide immunogen (5). After washing, membranes were incubated with goat F(ab"e;)2 anti-rabbit IgG HRP-conjugate (Cat. no. ALI4404) and bands were detected using the Pierce SuperSignal™ method. The data show that the peptide corresponding to PKA cat beta [pS338] blocks the antibody signal, thereby verifying the specificity of the antibody. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
|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|
|Tested Applications||Dilution *|
|ChIP assay (ChIP)||1:100|
|Western Blot (WB)||Assay Dependent|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
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.
beta-catalytic subunit; cAMP-dependent protein kinase; cAMP-dependent protein kinase C beta; cAMP-dependent protein kinase catalytic subunit beta; PKA C-beta