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Autres documents

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

Code UNSPSC :
12352204

Niveau de qualité

100

Description

C10H16N5O12P3SLi (Formula)
Lithium salt

Pureté

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

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

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Alana G Lerner et al.
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."
Michael Maurer et al.
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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