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Sp-cAMPS

PKA activator
 
BML-CN136-0001 1 mg 65.00 USD
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Replaces Prod. #: ALX-480-013

Sp-cAMPS is a potent and specific activator of cAMP-dependent protein kinases. Its cell permeability and complete resistance to cyclic nucleotide phosphodiesterases make it a unique tool for studying cAMP-dependent signaling. Has a considerably higher resistance against cyclic nucleotide-dependent phosphodiesterases as compared to dibutyryl-cAMP or 8-Br-cAMP. Concentration for half-maximal activation is 1.8µM. The product is not sterile. No metabolic side effects.

Product Specification

Formula:C10H11N5O5PS . C6H16N
 
MW:446.5
 
CAS:93602-66-5
 
Purity:≥98% (HPLC)
 
Identity:Determined by UV-VIS and ESI-MS.
 
Appearance:Lyophilized solid.
 
Solubility:Soluble in water (25mg/ml), DMSO, dimethyl formamide or methanol
 
Shipping:Ambient
 
Long Term Storage:-20°C
 
Use/Stability:Store, as supplied, at -20°C for up to one year. Store solutions at -20°C for up to 3 months.
 
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Product Literature References

Effects of activators and inhibitors of protein kinase A on increases in quantal size at the frog neuromuscular junction: W. Van der Kloot & D.D. Branisteanu; Pflugers Arch. 420, 336 (1992), Abstract;
Intracellular cyclic AMP not calcium, determines the direction of vesicle movement in melanophores: direct measurement by fluorescence ratio imaging: P.J. Sammak et al.; J. Cell. Biol. 117, 57 (1992), Abstract;
Second messenger signaling in the regulation of cytosolic pH and DNA synthesis by parathyroid hormone (PTH) and PTH-related peptide in osteoblastic osteosarcoma cells: role of Na+/H+ exchange: T. Sugimoto et al.; J. Cell. Physiol. 152, 28 (1992), Abstract;
The activation of cAMP-dependent protein kinase is directly linked to the stimulation of bone resorption by parathyroid hormone: H. Kaji et al.; Biochem. Biophys. Res. Commun. 182, 1356 (1992), Abstract;
Characterization of Sp-5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole- 3’,5’-monophosphorothioate (Sp-5,6-DCl-cBiMPS) as a potent and specific activator of cyclic-AMP-dependent protein kinase in cell extracts and intact cells: M. Sandberg et al.; Biochem. J. 279 , 521 (1991), Abstract;
Cyclic AMP antagonist Rp-cAMPS inhibits amylase exocytosis from saponin-permeabilized parotid acini: T. Takuma & T. Ichida ; J. Biochem. 110, 292 (1991), 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 et al.; Biochem. J. 251, 757 (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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