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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 (lambda) phosphatase (5), blocked with a 5% BSA-TBST buffer for two hours at room temperature, and incubated with PKA regIIbeta[pS114] 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 SuperSignal method. The data show that the peptide corresponding to PKA regIIbeta[pS114] blocks the antibody signal. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
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 (lambda) phosphatase (5), blocked with a 5% BSA-TBST buffer for two hours at room temperature, and incubated with PKA regIIbeta[pS114] 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 SuperSignal method. The data show that the peptide corresponding to PKA regIIbeta[pS114] blocks the antibody signal. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.
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 (lambda) phosphatase (5), blocked with a 5% BSA-TBST buffer for two hours at room temperature, and incubated with PKA regIIbeta[pS114] 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 SuperSignal method. The data show that the peptide corresponding to PKA regIIbeta[pS114] blocks the antibody signal. The data also show that phosphatase stripping eliminates the signal, verifying that the antibody is phospho-specific.

PKA 2 beta (phospho Ser114) antibody

GTX60925
GeneTex
ApplicationsWestern Blot
Product group Antibodies
ReactivityHuman, Mouse
TargetPRKAR2B
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Overview

  • Supplier
    GeneTex
  • Product Name
    PKA 2 beta (phospho Ser114) antibody
  • Delivery Days Customer
    9
  • Applications
    Western Blot
  • Certification
    Research Use Only
  • Clonality
    Polyclonal
  • Conjugate
    Unconjugated
  • Gene ID5577
  • Target name
    PRKAR2B
  • Target description
    protein kinase cAMP-dependent type II regulatory subunit beta
  • Target synonyms
    cAMP-dependent protein kinase type II-beta regulatory chain; cAMP-dependent protein kinase type II-beta regulatory subunit; H_RG363E19.2; PRKAR2; protein kinase, cAMP-dependent, regulatory subunit type II beta; protein kinase, cAMP-dependent, regulatory, type II, beta; RII-BETA; WUGSC:H_RG363E19.2
  • Host
    Rabbit
  • Isotype
    IgG
  • Protein IDP31323
  • Protein Name
    cAMP-dependent protein kinase type II-beta regulatory subunit
  • Scientific Description
    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. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic 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 adi
  • Reactivity
    Human, Mouse
  • Storage Instruction
    -20°C or -80°C,2°C to 8°C
  • UNSPSC
    12352203