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11162306001

Roche

ATP-γ-S

=90% (HPLC), solution, pkg of 200 μL (20 μmol)

Synonym(s):

adenosine-5′-o-(3-thio-triphosphate)

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About This Item

UNSPSC Code:
12352204

Quality Level

description

C10H16N5O12P3SLi (Formula)
Lithium salt

assay

90% (HPLC)

form

solution

mol wt

523.2

packaging

pkg of 200 μL (20 μmol)

manufacturer/tradename

Roche

λmax

260 nm at 100 mmol/L

shipped in

dry ice

storage temp.

−20°C

Related Categories

General description

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

Biochem/physiol Actions

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).

Quality

Contaminants: ≤10% ADP (HPLC)

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

No data available

flash_point_c

No data available


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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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