11162306001
Roche
ATP-γ-S
=90% (HPLC), solution, pkg of 200 μL (20 μmol)
Synonyme(s) :
adenosine-5′-o-(3-thio-triphosphate)
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About This Item
Produits recommandés
Niveau de qualité
Description
C10H16N5O12P3SLi (Formula)
Lithium salt
Essai
90% (HPLC)
Forme
solution
Poids mol.
523.2
Conditionnement
pkg of 200 μL (20 μmol)
Fabricant/nom de marque
Roche
λmax
260 nm at 100 mmol/L
Conditions d'expédition
dry ice
Température de stockage
−20°C
Catégories apparentées
Description générale
Adenosine 5′-O-(3-thiotriphosphate), lithium salt, solution.
Application
ATP-γ-S has been used:
- to treat THP-1 macrophage cell lines for testing if endoplasmic reticulum (ER) stress causes the production of interleukin (IL)-1β
- in amide hydrogen exchange (HX) experiments coupled to mass spectrometry and study the cyclomarin A (CymA)-induced structural changes in NMtb-ClpC
- as a supplement in CMG-binding buffer for gel-based DNA unwinding assays
Actions biochimiques/physiologiques
Adenosine 5′-O-(3-thiotriphosphate) (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. ATP-γ-S serves as a damage-associated molecular pattern molecule (DAMP) and NLR family pyrin domain containing 3 (NLRP3) inflammasome activator. ATP-γ-S may serve as a substrate for RNA-stimulated nucleotide hydrolysis and RNA unwinding activities of eukaryotic initiation factor-4A (eIF4A).
Qualité
Contaminants: ≤10% ADP (HPLC)
Autres remarques
For life science research only. Not for use in diagnostic procedures.
Code de la classe de stockage
12 - Non Combustible Liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
No data available
Point d'éclair (°C)
No data available
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Les clients ont également consulté
Cell metabolism, 16(2), 250-264 (2012-08-14)
When unfolded proteins accumulate to irremediably high levels within the endoplasmic reticulum (ER), intracellular signaling pathways called the unfolded protein response (UPR) become hyperactivated to cause programmed cell death. We discovered that thioredoxin-interacting protein (TXNIP) is a critical node in this "terminal UPR."
Cell chemical biology, 26(8), 1169-1179 (2019-06-18)
ATP-driven bacterial AAA+ proteases have been recognized as drug targets. They possess an AAA+ protein (e.g., ClpC), which threads substrate proteins into an associated peptidase (e.g., ClpP). ATPase activity and substrate selection of AAA+ proteins are regulated by adapter proteins
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