Home > Compound List > Product Information
Adenosine 5′-[γ-thio]triphosphate tetralithium salt_Molecular_structure_CAS_93839-89-5)
Click picture or here to close

Adenosine 5′-[γ-thio]triphosphate tetralithium salt

Catalog No. A1388 Name Sigma Aldrich
CAS Number 93839-89-5 Website http://www.sigmaaldrich.com
M. F. C10H12Li4N5O12P3S Telephone 1-800-521-8956
M. W. 546.978863 Fax
Purity ≥75% Email
Storage Chembase ID: 105256

SYNONYMS

IUPAC name
tetralithium(1+) ion [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl {[dioxido(sulfanylidene)-λ5-phosphanyl phosphonato]oxy}phosphonate
IUPAC Traditional name
tetralithium(1+) ion [(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methyl [dioxido(sulfanylidene)-λ5-phosphanyl phosphonato]oxyphosphonate
Synonyms
Ado-5′-PPP[S]
ATP-γ-S
Adenosine 5′-(3-thiotriphosphate) tetralithium salt

DATABASE IDS

Beilstein Number 6265083
MDL Number MFCD00077293
EC Number 298-862-8
PubChem SID 24890536
CAS Number 93839-89-5

PROPERTIES

Purity ≥75%
Shipped in dry ice
Apperance white powder
Solubility H2O: soluble25 mg/mL
GHS Pictograms GHS07
GHS Signal Word Warning
GHS Hazard statements H315-H319-H335
European Hazard Symbols Irritant Irritant (Xi)
Personal Protective Equipment dust mask type N95 (US), Eyeshields, Gloves
GHS Precautionary statements P261-P305 + P351 + P338
Risk Statements 36/37/38
Safety Statements 26-36
Storage Temperature -20°C
German water hazard class 3

DETAILS

Description (English)
Biochem/physiol Actions
P2 purinergic agonist; increases activity of Ca2+-activated K+ channels; can substitute for ATP in kinase reactions yielding thiophosphorylated proteins that are resistant to protein phosphatases.
Other Notes
Non-hydrolyzable ATP analog
Application
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.

REFERENCES