Sp-cAMPS

BML-CN136

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PKA activator

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.

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Product Details

Appearance	Lyophilized solid.
CAS	93602-66-5
Couple Target	PKA
Couple Type	Activator
Formula	C₁₀H₁₁N₅O₅PS . C₆H₁₆N
Identity	Determined by UV-VIS and ESI-MS.
MW	446.5
Purity	≥98% (HPLC)
Solubility	Soluble in water (25mg/ml), DMSO, dimethyl formamide or methanol

Handling & Storage

Use/Stability	As indicated on product label or CoA when stored as recommended. Store, as supplied, at -20°C for up to one year. Store solutions at -20°C for up to 3 months.
Long Term Storage	-20°C
Shipping	Ambient Temperature

Regulatory Status	RUO – Research Use Only

LTP at Hilar Mossy Cell-Dentate Granule Cell Synapses Modulates Dentate Gyrus Output by Increasing Excitation/Inhibition Balance: Hashimotodani, Y., Nasrallah, K., et al.; Neuron 95, 928 (2017), Abstract
Effects of protein kinase A inhibitor and activator on rewarding effects of SKF-82958 microinjected into nucleus accumbens shell of ad libitum fed and food-restricted rats: de Vaca, S. C., Peng, X. X., et al.; Psychopharmacology (Berl.) 221, 589 (2012), 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
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
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
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

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Sp-cAMPS

BML-CN136

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