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Merck
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Key Documents

11162306001

Roche

ATP-γ-S

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

동의어(들):

adenosine-5′-o-(3-thio-triphosphate)

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About This Item

UNSPSC 코드:
12352204

Quality Level

설명

C10H16N5O12P3SLi (Formula)
Lithium salt

분석

90% (HPLC)

형태

solution

분자량

523.2

포장

pkg of 200 μL (20 μmol)

제조업체/상표

Roche

λmax

260 nm at 100 mmol/L

배송 상태

dry ice

저장 온도

−20°C

관련 카테고리

일반 설명

Adenosine 5′-O-(3-thiotriphosphate), lithium salt, solution.

애플리케이션

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

생화학적/생리학적 작용

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).

품질

Contaminants: ≤10% ADP (HPLC)

기타 정보

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

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point (°F)

No data available

Flash Point (°C)

No data available


시험 성적서(COA)

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문서 라이브러리 방문

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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