货号 | 6574S |
描述 | SignalSilence® PKA C-α siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit PKA C-α expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce target protein expression by western analysis. |
反应种属 | Human |
应用 | TFN |
目标/特异性 | SignalSilence® PKA C-α siRNA II will inhibit human, mouse and rat PKA C-α exoression. |
供应商 | CST |
背景 | 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). |
存放说明 | -20C |
参考文献 | Montminy, M. (1997) Annu. Rev. Biochem. 66, 807-822. DellAcqua, M.L. and Scott, J.D. (1997) J. Biol. Chem. 272, 12881-12884. Tan, Y. et al. (2000) J. Biol. Chem. 275, 25865-25869. Gonzalez, G.A. and Montminy, M.R. (1989) Cell 59, 675-680. Fang, X. et al. (2000) Proc. Natl. Acad. Sci. USA 97, 11960-11965. Dumaz, N. and Marais, R. (2003) J. Biol. Chem. 278, 29819 -29823. Moore, M.J. et al. (2002) J. Biol. Chem. 277, 47878-47884. |