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PKA C-α Antibody

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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年08月15日
  • W, IP, IF-IC, F
  • Rabbit
  • H,M,R
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 抗体英文名

      PKA C-α Antibody

    • 抗原

      synthetic peptide corresponding to the carboxy terminal sequence of human PKA C-α

    • 应用范围

      W, IP, IF-IC, F

    • 宿主

      Rabbit

    • 适应物种

      H,M,R

    • 库存

      大量

    • 级别

      详见MSDS文件

    • 保质期

      详见说明书

    • 供应商

      CST

    • 是否单克隆

      2

    • 保存条件

      -20°c

    • 规格

      100 ul (10 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-IC=Immunofluorescence (Immunocytochemistry)  F=Flow Cytometry
    Reactivity Key:  H=Human  M=Mouse  R=Rat
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Source
    W IP IF-IC F H M R Endogenous 42 Rabbit
    Protocols
    Specificity / Sensitivity

    PKA C-α Antibody detects endogenous levels of total PKA C-α.

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminal sequence of human PKA C-α. Antibodies are purified by protein A and peptide affinity chromatography.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from HeLa, C6, PC12 and NIH/3T3 cells, using PKA C-α Antibody.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from HeLa cells transfected with non-targeted (-) or PKA C-α (+) siRNA. PKA C-α was detected using the PKA C-α Antibody #4782, and Akt1 was detected using Akt1 (2H10) Monoclonal Antibody #2967. The PKA C-α Antibody confirms silencing of PKA C-α expression, and the Akt1 Antibody is used to control for loading and specificity of PKA C-α siRNA.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from HeLa cells, transfected with either 100 nM SignalSilence® Control siRNA (Fluorescein Conjugate) #6201 (-), SignalSilence® PKA C-α siRNA II (+) or SignalSilence® PKA C-α siRNA I #6406 (+), using PKA C-α Antibody #4782 and α-Tubulin (11H10) Rabbit mAb #2125. The PKA C-α antibody confirms silencing of PKA C-α expression and α-Tubulin (11H10) Rabbit mAb is used to control for loading and specificity of PKA C-α siRNA.


    Flow Cytometry

    Flow Cytometry

    Flow cytometric analysis of HeLa cells, using PKA C-α Antibody (blue) compared to a nonspecific negative control antibody (red).

    IF-IC

    IF-IC

    Confocal immunofluorescent analysis of HeLa cells using PKA C-alpha Antibody (green). Actin filaments have been labeled with DY-554 phalloidin (red). Blue pseudocolor = DRAQ5™ (fluorescent DNA dye).

    Background

    The second messenger cyclic AMP (cAMP) activates cAMP-dependent protein kinase (PKA or cAPK) in mammalian cells and controls many cellular mechanisms such as gene transcription, ion transport, and protein phosphorylation (1). Inactive PKA is a heterotetramer composed of a regulatory subunit (R) dimer and a catalytic subunit (C) dimer. In this inactive state, the pseudosubstrate sequences on the R subunits block the active sites on the C subunits. Three C subunit isoforms (C-α, C-β, and C-γ) and two families of regulatory subunits (RI and RII) with distinct cAMP binding properties have been identified. The two R families exist in two isoforms, α and β (RI-α, RI-β, RII-α, and RII-β). Upon binding of cAMP to the R subunits, the autoinhibitory contact is eased and active monomeric C subunits are released. PKA shares substrate specificity with Akt (PKB) and PKC, which are characterized by an arginine at position -3 relative to the phosphorylated serine or threonine residue (2). Substrates that present this consensus sequence and have been shown to be phosphorylated by PKA are Bad (Ser155), CREB (Ser133), and GSK-3 (GSK-3α Ser21 and GSK-3β Ser9) (3-5). In addition, combined knock-down of PKA C-α and -β blocks cAMP-mediated phosphorylation of Raf (Ser43 and Ser259) (6). Autophosphorylation and phosphorylation by PDK-1 are two known mechanisms responsible for phosphorylation of the C subunit at Thr197 (7).

    1. Montminy, M. (1997) Annu. Rev. Biochem. 66, 807-822.
    2. Dell'Acqua, M.L. and Scott, J.D. (1997) J. Biol. Chem. 272, 12881-12884.
    3. Tan, Y. et al. (2000) J. Biol. Chem. 275, 25865-25869.
    4. Gonzalez, G.A. and Montminy, M.R. (1989) Cell 59, 675-680.
    5. Fang, X. et al. (2000) Proc. Natl. Acad. Sci. USA 97, 11960-11965.
    6. Dumaz, N. and Marais, R. (2003) J. Biol. Chem. 278, 29819 -29823.
    7. Moore, M.J. et al. (2002) J. Biol. Chem. 277, 47878-47884.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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      zhanghai123 大家好!我最近在做一种GPCR的信号通路的分析 目前能够确定的是我的这种受体在我所用的细胞系中是与Gαi相偶联,以前公认是与Gq相偶联, 然后我用H89处理细胞,确定PKA 参与其中的调控。 可是,我用环腺苷酸环化酶抑制剂SQ22536处理,却没有发现能够干预这条通路。 目前公认的PKA是cAMP依赖的一种激酶,可是现在的结果却是矛盾的。 我想问一下大家:是否存在不依赖cAMP的PKA的活化方式

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