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Read our guarantee »Products:Signal Transduction >> Protein Phosphorylation >> Ser / Thr Kinases >> PKA
Anti-PKA 2 beta (regulatory subunit) (phospho S114) antibody
See all PKA 2 beta (regulatory subunit) products (8) ...
Rabbit polyclonal to PKA 2 beta (regulatory subunit) (phospho S114)
PKA regulatory 2 alpha subunit (75% homologous) has not been tested.
Reacts with
Mouse, Human
Predicted to work with
Rat, Rabbit, Cow
Synthetic phosphopeptide derived from a region of human PKA regulatory 2 beta subunit that contains serine 114.
3T3-L1 adipocytes or Y1 mouse adrenal cortical cells.
Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
Preservative: 0.05% Sodium Azide
Constituents: 50% Glycerol, PBS, 1mg/ml BSA. pH 7.3
Concentration information loading...
Immunogen affinity purified
The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated PKA. The final product is generated by affinity chromatography using a PKA-derived peptide that is phosphorylated at serine 114.
Polyclonal
IgG
Signal Transduction >> Protein Phosphorylation >> Ser / Thr Kinases >> PKA
Western blot - Anti-PKA 2 beta (regulatory subunit) (phospho S114) antibody (ab5829)
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Our Abpromise guarantee covers the use of ab5829 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
WB: 1/1000Detects a band of approximately 50 kDa.
PKA 2 beta (regulatory subunit or PRKAR2B) is one of the regulatory subunits of cAMP-dependent Protein Kinase (PKA), which is a serine/threonine kinase that regulates a number of cellular processes including proliferation, ion transport and gene transcription. PKA is composed of conserved catalytic subunits and regulatory subunits (R1 alpha, R1 beta, R2 alpha, and R2 beta). Upon adenylate cyclase activation, AMP binds to the regulatory subunits, and releases the catalytic subunit, which becomes active upon its dissociation from the regulatory subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity. The studies also suggest that this subunit may mediate the gene induction and cataleptic behavior induced by haloperidol.
Cytoplasmic
Western blot - Anti-PKA 2 beta (regulatory subunit) (phospho S114) antibody (ab5829)

Peptide Competition and Phosphatase Treatment: Lysates prepared from 3T3-L1 cells were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were either left untreated (1-4) or treated with lambda phosphatase (5), blocked with a 5% BSA-TBST buffer for two hours at room temperature, and incubated with ab5829 antibody for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1, 5), the non phosphopeptide corresponding to the immunogen (2), a generic phosphothreonine-containing peptide (3), or, the phosphopeptide immunogen (4). After washing, membranes were incubated with goat F(ab’ 2 anti-rabbit IgG HRP conjugate and bands were detected using the Pierce SuperSignalTM method. The data show that the peptide corresponding to PKA reg 2 beta [pS114] blocks the antibody signal. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
ab5829 has not yet been referenced specifically in any publications.
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Peptide Competition and Phosphatase Treatment: Lysates prepared from 3T3-L1 cells were resolved by SDS-PAGE on a 10% polyacrylamide gel and transferred to PVDF. Membranes were either left untreated (1-4) or treated with lambda phosphatase (5), blocked with a 5% BSA-TBST buffer for two hours at room temperature, and incubated with ab5829 antibody for two hours at room temperature in a 3% BSA-TBST buffer, following prior incubation with: no peptide (1, 5), the non phosphopeptide corresponding to the immunogen (2), a generic phosphothreonine-containing peptide (3), or, the phosphopeptide immunogen (4). After washing, membranes were incubated with goat F(ab’ 2 anti-rabbit IgG HRP conjugate and bands were detected using the Pierce SuperSignalTM method. The data show that the peptide corresponding to PKA reg 2 beta [pS114] blocks the antibody signal. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
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