Adenosine 5'-[γ-thio]triphosphate TetralithiuM Salt

White Solid

ATP-γ-S is a substrate and inhibitor of ATP-dependent enzyme systems. It is hydrolyzed very slowly by phosphatases and most ATPases. Once thiophosphorylated, proteins are resistant to protein phosphatases.

Adenosine 5′-[γ-thio]triphosphate tetralithium salt has been used to treat the pollen grains to determine the inhibitory effect of adenosine triphosphate (ATP) or its hydrolysis product. It has also been used to select thiophosphorylate target protein.

Adenosine 5’[γ-thio]triphosphate Tetralithium Salt is used as a reagent in the synthesis of DNA N-acetylglucosamine analogs.

atpγs tetralithium salt is an analogue of atp, acting as a potent agonist of g protein-coupled p2y2 and p2y11 receptors (pec50 = 5.52 for p2y11) [1].the p2y receptors consist of 8 human subtypes, i.e. p2y1, p2y2, p2y4, p2y6, p2y11, p2y12, p2y13, and p2y14, coupled to g protein-dependent and -independent signaling pathways, including ion channels. the p2y receptors are involved in controlling levels of extracellular nucleotides and nucleosides, and intracellular signaling pathways [1].in pc 12 cells, preincubation of the cells with norepinephrine (ne) and atpγs tetralithium salt (1 μm) resulted in a persistent increase in uptake of ne, whilst similar pretreatment with atp did not show this increase. in the presence of atp, the activation effect produced by atpγs tetralithium salt on ne uptake was blocked [2]. in tea3a1 cells, atpγs tetralithium salt (0 ~ 200 μm) increased ca2+ influx in a dose-dependent manner, with ed50 value of about 50 μm. a maximum level of ca2+ influx was observed when cells were treated with atpγs tetralithium salt at concentrations above 100 μm. similar dose-dependent increases in the production of prostaglandin e2 (pge2) were also observed after atpγs tetralithium salt treatment [3].[1]. jacobson k a, ivanov a a, de castro s, et al. development of selective agonists and antagonists of p2y receptors. purinergic signal, 2009, 5(1): 75-89.[2]. hardwick j c, ehrlich y h, hendley e d. extracellular atp stimulates norepinephrine uptake in pc12 cells. journal of neurochemistry, 1989, 53(5):1512-1518.[3]. liu p, lalor d, bowser s s, et al. regulation of arachidonic acid release and prostaglandin e2 production in thymic epithelial cells by atpgammas and transforming growth factor-alpha. cellular immunology, 1998, 188(2): 81-88.

Adenosine 5′-[γ-thio]triphosphate (ATP-γ-S) is widely used as a non-hydrolyzed ATP analogue for studies on the effects of ATP binding to ATP sites in a wide range of processes including extracellular functions. ATP- γ-S is a P2 purinergic agonist which increases the activity of Ca2+-activated K+ channels. ATP- γ-S can substitute for ATP in kinase reactions yielding thiophosphorylated proteins that are resistant to protein phosphatases and modulate the ATP-dependent steps in the binding of ubiquitin conjugates to the 26S proteasome. ATP-γ -S differentially modulates Toll-like receptor 4-mediated cell survival and death.

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