Anti-PKA beta (catalytic subunit) (phospho S338)抗体
参阅全部 PKA beta (catalytic subunit) 一抗
兔多克隆抗体to PKA beta (catalytic subunit) (phospho S338)
Rabbit
Peptide competition data indicate that this antibody cross-reacts with the PKA nu subunit (64% homologous) and partially with the alpha subunit (82% homologous).
适用于: WBmore details
与反应: Mouse
预测可用于: Cow, Pig
Synthetic peptide corresponding to Human PKA beta (catalytic subunit) (phospho S338).
3T3-L1 adipocytes.
c-AMP-dependent Protein Kinase (PKA) 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 that dissociate upon activation by cAMP. The catalytic subunit of PKA contains the activation loop and mediates DNA binding and substrate recognition. The catalytic subunit is assembled and expressed as an active form and is phosphorylated on threonine 197 by PDK 1 in the activation loop and serine 338 in the carboxyl terminus. Phosphorylation of serine 338 plays a key role in stabilizing PKA and activating its substrates, and hence mediating its biological functions.
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Liquid
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
pH: 7.30
Preservative: 0.05% Sodium azide
Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.1% BSA
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 338.
c-AMP-dependent Protein Kinase (PKA) 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 that dissociate upon activation by cAMP. The catalytic subunit of PKA contains the activation loop and mediates DNA binding and substrate recognition. The catalytic subunit is assembled and expressed as an active form and is phosphorylated on threonine 197 by PDK 1 in the activation loop and serine 338 in the carboxyl terminus. Phosphorylation of serine 338 plays a key role in stabilizing PKA and activating its substrates, and hence mediating its biological functions.
多克隆
IgG
Abpromise™承诺保证使用ab5816于以下的经测试应用
“应用说明”部分 下显示的仅为推荐的起始稀释度；实际最佳的稀释度/浓度应由使用者检定。
| 应用 | Ab评论 | 说明 |
|---|---|---|
| WB | 1/1000. Detects a band of approximately 42 kDa. |
Entrez Gene: 18749 Mouse
SwissProt: P68181 Mouse
Unigene: 16766 Mouse
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Western blot - Anti-PKA beta (catalytic subunit) (phospho S338) antibody (ab5816)
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-TBSTbuffer for two hours at room temperature, and incubated with ab5816 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’)2 anti-rabbit IgG HRP-conjugate and bands were detected using the Pierce SuperSignalTM 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.
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-TBSTbuffer for two hours at room temperature, and incubated with ab5816 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’)2 anti-rabbit IgG HRP-conjugate and bands were detected using the Pierce SuperSignalTM 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.
