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 Details
Formula: | C10H11N5O5PS . C6H16N |
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MW: | 446.5 |
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CAS: | 93602-66-5 |
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Purity: | ≥98% (HPLC) |
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Identity: | Determined by UV-VIS and ESI-MS. |
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Appearance: | Lyophilized solid. |
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Solubility: | Soluble in water (25mg/ml), DMSO, dimethyl formamide or methanol |
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Shipping: | Ambient Temperature |
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Long Term Storage: | -20°C |
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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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Regulatory Status: | RUO - Research Use Only |
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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;