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Rp-cAMPS

PKA inhibitor
 
BML-CN135-0001 1 mg 130.00 USD
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Replaces Prod. #: ALX-480-012

Rp-cAMPS is a potent and specific competitive inhibitor of the activation of cAMP-dependent protein kinases by cAMP (IC50=4.9 µM) . Its cell permeability and complete resistance to cyclic nucleotide phosphodiesterases make it a unique tool for studying cAMP-dependent signaling. Significantly more lipophilc as compared to cAMP and thus membrane permeable in many biological systems. This product is not sterile.

Product Specification

Formula:C10H11N5O5PS . C6H16N
 
MW:446.5
 
Source:Synthetic.
 
CAS:151837-09-1
 
Purity:≥98% (HPLC)
 
Appearance:White solid.
 
Solubility:Soluble in water (25mg/ml), aqueous buffers, methanol, 100% ethanol or DMSO.
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Use/Stability:Store, as supplied, at -20°C for up to 1 year. Store solutions at -20°C for up to 3 months.
 
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Product Literature References

Biased signaling initiated by agouti-related peptide through human melanocortin-3 and − 4 receptors: Z. Yang & Y.X. Tao; Biochim. Biophys. Acta 1862, 1485 (2016), Application(s): Cell culture, Abstract;
Stimulation of the ERK pathway by GTP-loaded Rap1 requires the concomitant activation of Ras, protein kinase C, and protein kinase A in neuronal cells: T. Bouschet et al.; J. Biol. Chem. 278, 4778 (2003), Abstract;
Cell-permeable non-hydrolyzable cAMP derivatives as tools for analysis of signaling pathways controlling gene regulation in Dictyostelium: P. Schaap et al.; J. Biol. Chem. 268, 6323 (1993), Abstract;
Regulation of kainate receptors by cAMP-dependent protein kinase and phosphatases: L.Y. Wang et al.; Science 253, 1132 (1991), Abstract;
Inhibition of cGMP-dependent protein kinase by (Rp)-guanosine 3’,5’-monophosphorothioates: E. Butt et al.; FEBS Lett. 263, 47 (1990), Abstract;
Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3’,5’-cyclic phosphorothioates: W.R.G. Dostmann et al.; J. Biol. Chem. 265, 10484 (1990), Abstract;
A mechanistic and kinetic analysis of the interactions of the diastereoisomers of adenosine 3’,5’-(cyclic)phosphorothioate with purified cyclic AMP-dependent protein kinase: J.D. Rothermel & L.J. Parker Bothelo; Biochem. J. 251, 757 (1988), Abstract;
cAMP analog antagonists of cAMP action: L.H. Botelho et al.; Methods Enzymol. 159, 159 (1988), Abstract;
Hydrolysis of cyclic nucleotides by a purified cGMP-stimulated phosphodiesterase: structural requirements for hydrolysis: T. Braumann et al.; Biochim. Biophys. Acta. 871, 199 (1986), Abstract;

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