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Merck

557440

Sigma-Aldrich

Ru360

≥97%, solid, Ca2+ uptake blocker in mitrochondria, Calbiochem®

別名:

Ru360, (μ)[(HCO₂)(NH₃)₄Ru]₂OCl₃

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About This Item

実験式(ヒル表記法):
C2H26Cl3N8O5Ru2
分子量:
550.78
UNSPSCコード:
12352200
NACRES:
NA.77
現在、価格および在庫状況を閲覧できません。

製品名

Ru360, Ru360, is a cell-permeable oxygen-bridged dinuclear ruthenium amine complex. Binds to mitochondria with high affinity (Kd = 340 pM) and blocks Ca2+ uptake into mitochondria in vitro (IC₅₀ = 184 pM).

品質水準

アッセイ

≥97%

フォーム

solid

メーカー/製品名

Calbiochem®

保管条件

OK to freeze
desiccated (hygroscopic)
protect from light

green

溶解性

deoxygenated water: 0.5 mg/mL

輸送温度

ambient

保管温度

−20°C

詳細

A cell-permeable oxygen bridged dinuclear ruthenium amine complex that has been shown to bind to mitochondria with high affinity (Kd = 0.34 nM) and specifically blocks Ca2+ uptake into mitochondria in vitro (IC50 = 184 pM) and in situ in intact myocytes (for complete block after incubation with ~10 µM of Ru360 for 30 min. Does not affect other cellular Ca2+ transport processes involved in cardiac muscle contraction even at micromolar levels.
A cell-permeable oxygen-bridged dinuclear ruthenium amine complex that has been shown to bind to mitochondria with high affinity (Kd = 340 pM). Specifically blocks Ca2+ uptake into mitochondria in vitro (IC50 = 184 pM) and in situ in intact myocytes (complete block after incubation with ~10 µM of Ru360 for 30 min). Does not affect other cellular Ca2+ transport processes involved in cardiac muscle contraction, even at micromolar levels.
Note: 1 set = 10 x 100 µg.

生物化学的/生理学的作用

Cell permeable: yes
Primary Target
Ca2+ uptake into mitochondria in vitro
Product does not compete with ATP.
Reversible: no
Target IC50: 184 pM blocking Ca2+ uptake into mitochondria in vitro; and in situ in intact myocytes; Kd = 340 pM for binding mitochondria

包装

Packaged under inert gas

警告

Toxicity: Standard Handling (A)

再構成

Unstable in solution; reconstitute just prior to use.

その他情報

Sanchez, J.A., et al. 2001. J. Physiol. 536, 387.
Bassani, R.A., et al. 1998. Cell Calcium23, 433.
Matlib, M.A., et al. 1998. J. Biol. Chem.273, 10223.
Zhou, Z., et al. 1998. J. Physiol.507 (pt 2), 379.
Emerson, J., et al. 1993. J. Am. Chem. Soc.115, 11799.
Ying, W.-L., et al. 1991. Biochemistry30, 4949.

法的情報

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

保管分類コード

11 - Combustible Solids

WGK

WGK 1

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

557440-MG:
557440-500UG:
557440-100UG:
557440-1SET:


試験成績書(COA)

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Slide 1 of 8

1 of 8

Rachel L Doser et al.
eLife, 13 (2024-03-14)
Our understanding of mitochondrial signaling in the nervous system has been limited by the technical challenge of analyzing mitochondrial function in vivo. In the transparent genetic model Caenorhabditis elegans, we were able to manipulate and measure mitochondrial reactive oxygen species
Madison X Rodriguez et al.
STAR protocols, 2(4), 100979-100979 (2021-12-09)
The mitochondrial calcium uniporter, which mediates mitochondrial Ca2+ uptake, regulates key cellular functions, including intracellular Ca2+ signaling, cell-fate determination, and mitochondrial bioenergetics. Here, we describe two complementary strategies to quantify the uniporter's transport activity. First, we detail a mitochondrial Ca2+
Michael J Bround et al.
Scientific reports, 14(1), 6751-6751 (2024-03-22)
Mitochondrial Ca2+ overload can mediate mitochondria-dependent cell death, a major contributor to several human diseases. Indeed, Duchenne muscular dystrophy (MD) is driven by dysfunctional Ca2+ influx across the sarcolemma that causes mitochondrial Ca2+ overload, organelle rupture, and muscle necrosis. The
MCU Upregulation Overactivates Mitophagy by Promoting VDAC1 Dimerization and Ubiquitination in the Hepatotoxicity of Cadmium.
Liu, et al.
Advanced science (Weinheim, Baden-Wurttemberg, Germany), 10, e2203869-e2203869 (2023)
Peu Santra et al.
Disease models & mechanisms, 14(7) (2021-07-24)
The vacuolar-type H+-ATPase (V-ATPase) is a multi-subunit proton pump that regulates cellular pH. V-ATPase activity modulates several cellular processes, but cell-type-specific functions remain poorly understood. Patients with mutations in specific V-ATPase subunits can develop sensorineural deafness, but the underlying mechanisms

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