
2',5'-dideoxy AdenosineP-site inhibitor of adenylate cyclase |
Sample solution is provided at 25 µL, 10mM.
































Quality Control & MSDS
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- Purity = 98.00%
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- MSDS (Material Safety Data Sheet)
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Chemical structure


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Cas No. | 6698-26-6 | SDF | Download SDF |
Synonyms | 2ʹ,5ʹ-dd-Ado,NSC 95943 | ||
Chemical Name | 2",5"-dideoxy-adenosine | ||
Canonical SMILES | C[C@@H]1[C@@H](O)C[C@H](N2C=NC3=C2N=CN=C3N)O1 | ||
Formula | C10H13N5O2 | M.Wt | 235.2 |
Solubility | ≤20mg/ml in DMSO;5mg/ml in dimethyl formamide | Storage | Store at -20°C |
Physical Appearance | A crystalline solid | Shipping Condition | Evaluation sample solution : ship with blue ice.All other available size:ship with RT , or blue ice upon request |
General tips | For obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.Stock solution can be stored below -20℃ for several months. |
2",5"-dideoxy Adenosine, a nucleoside analog, is one of the first identified cell-permeable, P-site inhibitors of adenylate cyclase [1].
Adenylyl cyclase is an enzyme with key regulatory roles in almost all cells. Adenylyl cyclases have been involved in catalyzing the conversion of ATP to cAMP) and pyrophosphate [2]. 2",5"-dideoxy Adenosine inhibits forskolin-induced activation of a cAMP-dependent reporter gene in HEK293 cells with an IC50 value of 33 μM.
In vitro: In HEK293 cells expressing a cAMP response element (CRE) reporter gene, 2",5"-dideoxy Adenosine (ddAd) effectively and potently inhibited the activity of adenylate cyclase (AC). The ddAd effectively inhibited the effect of forskolin, an AC activator, with IC50 value of 33 μM [1]. Pretreatment with graded concentrations of ddAd effectively inhibited PACAP-induced reporter gene activation with IC50 value of ~35 μM [1]. The ddAd inhibited forskolin-induced Elk-1 transactivation with an IC50 of 10 μM. The ddAd at concentrations greater than 500 mM failed to completely inhibit PACAP-induced cAMP elevation[1].
References:[1] Emery A C, Eiden M V, Eiden L E. A new site and mechanism of action for the widely used adenylate cyclase inhibitor SQ22, 536[J]. Molecular pharmacology, 2013, 83(1): 95-105.[2] Gilman A G. G proteins and dual control of adenylate cyclase[J]. Cell, 1984, 36(3): 577-579.
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