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ATP-Red 1 Sale

目录号 : GC30265

ATP-Red1是一种多位点结合可切换的荧光探针,能够选择性的快速检测活细胞中的ATP含量。

ATP-Red 1 Chemical Structure

Cas No.:1847485-97-5

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Sample solution is provided at 25 µL, 10mM.

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实验参考方法

Cell experiment:

OSCC Cells are plated in 96-well flat-bottomed plates at 1×105 cells per well and allowed to grow 3 or 24 h prior to exposure to ATP-Red 1. Then MTT reagent is added for 4 h at 37 °C and DMSO (100 μL/well) is further incubated with cells for 15 min after removing the medium. The absorbance at 570 nm and 690 nm (background signal) is recorded in a Spectra Max M2 microplate reader. The following formula is used to calculate the viability of cell growth: Cell viability (%) = (mean of A value of treatment group / mean of A value of control) × 100[1].

References:

[1]. Wang L, et al. A Multisite-Binding Switchable Fluorescent Probe for Monitoring Mitochondrial ATP Level Fluctuation in Live Cells. Angew Chem Int Ed Engl. 2016 Jan 26;55(5):1773-6

产品描述

ATP-Red 1 is a multisite-binding switchable fluorescent probe, and can selectively and rapidly responds to intracellular concentrations of ATP in living cells.

ATP-Red 1 is a multisite-binding switchable fluorescent probe, and can selectively and rapidly responds to intracellular concentrations of ATP in living cells. The maximum absorption and emission wavelength of are 570/566 nm and 590/585 nm. ATP-Red 1 has good membrane permeability, and in the presence of 5 mM ATP, the fluorescence intensity of ATP-Red 1 increases 5.6-fold. ATP-Red 1 (2.5 μM, 20 min) shows much weaker fluorescence after KCN-induced inhibition of OXPHOS, which results in reduced mitochondrial ATP levels in OSCC cells[1].

[1]. Wang L, et al. A Multisite-Binding Switchable Fluorescent Probe for Monitoring Mitochondrial ATP Level Fluctuation in Live Cells. Angew Chem Int Ed Engl. 2016 Jan 26;55(5):1773-6

Chemical Properties

Cas No. 1847485-97-5 SDF
Canonical SMILES O=C1N(C2=CC=CC=C2B(O)O)C3(C4=C(OC5=C3C=CC(N(CC)CC)=C5)C=C(N(CC)CC)C=C4)C6=C1C=CC=C6
分子式 C34H36BN3O4 分子量 561.48
溶解度 DMSO : 50 mg/mL (89.05 mM);Water : < 0.1 mg/mL (insoluble) 储存条件 Store at -20°C,protect from light
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储备液的保存方式和期限:-80°C 储存时,请在 6 个月内使用,-20°C 储存时,请在 1 个月内使用。
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溶解性数据

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1 mg 5 mg 10 mg
1 mM 1.781 mL 8.905 mL 17.8101 mL
5 mM 0.3562 mL 1.781 mL 3.562 mL
10 mM 0.1781 mL 0.8905 mL 1.781 mL
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Research Update

A Multisite-Binding Switchable Fluorescent Probe for Monitoring Mitochondrial ATP Level Fluctuation in Live Cells

Adenosine triphosphate (ATP), commonly produced in mitochondria, is required by almost all the living organisms; thus fluorescent probes for monitoring mitochondrial ATP levels fluctuation are essential and highly desired. Herein, we report a multisite-binding switchable fluorescent probe, ATP-Red 1, which selectively and rapidly responds to intracellular concentrations of ATP. Live-cell imaging indicated that ATP-Red 1 mainly localized to mitochondria with good biocompatibility and membrane penetration. In particular, with the help of ATP-Red 1, we successfully observed not only the decreased mitochondrial ATP levels in the presence of KCN and starvation state, but also the increased mitochondrial ATP levels in the early stage of cell apoptosis. These results indicate that ATP-Red 1 is a useful tool for investigating ATP-relevant biological processes.

Protecting muscle ATP: positive roles for peripheral defense mechanisms-introduction

Skeletal muscle has evolved an impressive array of mechanisms for peripherally mediated control of ATP homeostasis. Some of these mechanisms are intracellular, and others are extracellular and include influences on the cross-bridge cycle itself and substrate supply. This paper introduces three distinctly different topics that nevertheless all have ATP defense in common. The role of ADP in fatigue is controversial but has recently been more clearly delineated so that an effect on alleviating force declines during extreme fatigue is plausible. AMP plays its role by activating the protein-kinase, AMPK, which is a key sensor of cellular energy stress. AMPK has different isoforms, is not uniformly distributed in the cell, and its activation is carefully controlled. It has multiple effects including improvements in substrate supply for the metabolic pathways producing ATP and inhibition of anabolic processes to further spare ATP. Red blood cells have the capacity to sense hypoxia and to release vasodilators where there is a locally increased demand for blood supply. The papers in this series emphasize the important positive roles of metabolites and sensors of fatigue in the balance between ATP supply and demand.

Prospective Validation of a Novel Triage System Developed in a Middle Income Country - AIIMS Triage Protocol

Introduction: Triage is a crucial process not only to identify sick patients and prioritize prompt management but also to foster efficient resource utilization. In low-and middle-income countries (LMICs) most emergency departments (ED) still have an informal triage process. Although an important element of emergency care, triage research has not been a priority in LMICs, and hence, very few triage systems have been validated. The All India Institute of Medical Sciences (AIIMS) triage protocol or ATP for adult patients was developed by expert consensus at AIIMS using the Delphi method. We attempted a prospective validation of the ATP in terms of mortality and intensive care unit (ICU)/hospital admission at 24 h.
Methods: Patients presenting to the ED, who were 14 years and above were included in the study. The patients were followed up at 24 h and their outcome documented on a standardized data collection form. Mortality and ICU admission were noted at 24 h.
Results: A total of 15,505 patients were recruited. After exclusion, among 13,754 patients, 6303 (45.83%) were triaged red and 7451 (54.17%) were triaged yellow. Mortality at 24 h was 10.31% (650) in red triaged patients and 0.35% (26) in yellow triaged patients. The 24-h mortality of red triaged patients was significantly higher (P <0.001) than that of yellow triaged patients. The presence of one or more ATP "Red" criteria was 96.2% (95% confidence interval [CI]: 94.42%-97.47%) sensitive and 56.8% (95% CI: 55.92%-57.63%) specific in predicting 24-h mortality. The sensitivity and specificity of ATP "Red" criteria for 24-h ICU admission were 98.5% (95% CI: 97.7%-99.1%) and 59.6% (95% CI: 58.8%-60.5%), respectively.
Conclusion: When applied to adult nontrauma patients, ATP had a high accuracy in recognizing sick patients presenting to the ED. A time-tested and validated triage system like ATP may be a good starting point for public hospital EDs in LMICs.

Ecto-ATPase activity of vertebrate blood cells

Ecto-ATPase activity was measured for red blood cells, white blood cells, and whole blood from a variety of vertebrates. A large range of red blood cell ecto-ATPase activity was observed; for example, at 10 degrees C, red blood cells from a catastomid fish (Catostomus macrocheilus) and a newt (Taricha rivularis) had activities of 56 +/- 9 and 25,000,000 +/- 14,000,000 pmol ATP per 10(6) red blood cells per hour, respectively (mean +/- SD). Several control experiments verified that the measured ATPase activity was not the result of intracellular ATPases released due to cell damage or lysis nor due to the release of intracellular nucleoside triphosphate or uptake of extracellular ATP. Red blood cell ecto-ATPase activity was relatively low within the teleosts, was high within the reptiles, and had the greatest range and single highest value within the amphibians. Within the endotherms, avian red blood cell ecto-ATPase activities were greater than mammalian red blood cell ecto-ATPase activities, which were the lowest for all vertebrates examined. The lowest ecto-ATPase activities measured were for human and skunk red blood cells, which had activities of 13 +/- 1 and 11 +/- 2 pmol ATP per 10(6) red blood cells per hour, respectively, at 35 degrees C. Ecto-ATPase activity was measured in white blood cells of several vertebrate species and appeared generally high and less variable than red blood cell ecto-ATPase activity. Measured whole blood ecto-ATPase activity showed a range of three orders of magnitude and correlated positively with red blood cell ecto-ATPase activities. Ecto-ATPase activity was also determined for red blood cells from fetal, 1-3 d old neonatal, and pregnant garter snakes (Thamnophis elegans); these activities were not significantly different from the activity of red blood cells from nonpregnant adult females. Overall, the data from the present study demonstrate a wide range of red blood cell and whole blood ecto-ATPase activities among vertebrates and include some of the highest ecto-ATPase activities reported to date.

Ca2+-activated Na+ fluxes in human red cells. Amiloride sensitivity

The effect of Ca2+ on the ouabain- and bumetanide-resistant Na+ fluxes in intact red cells was studied at relatively constant internal Ca2+, membrane potential, and cell volume. The red cell calcium concentration was modified using the ionophore A23187. In fresh red cells, the Na+ influx and efflux (1.2 +/- 0.13 and 0.26 +/- 0.07 mmol/liter cells x h, respectively) were not affected by amiloride (1 mM). When external Ca2+ was raised from 0 to 150 microM, in the presence of A23187, both the Na+ influx and efflux were stimulated (about 3.5-fold). The Ca2+-activated Na+ efflux and influx had an apparent Km for activation by Ca2+o of about 25 microM. The Ca2+-dependent Na+ transport was inhibited 30-60% by amiloride (ID50 = 17.3 +/- 8 microM). Amiloride, however, had no effect on the Ca2+-dependent K+ influx. The amiloride-sensitive (AS) transport pathway was a linear function of the Na+o concentration in the range from 0 to 75 mM. The Ca2+i activation seems to depend on the metabolic integrity of red cells. 1) It does not take place in ATP-depleted red cells; 2) ATP-repletion of ATP-depleted red cells fully restored AS Na influx; and 3) ATP-enrichment (ATP-red cells) enhanced the AS Na influx by about 100%. The Ca2+-activated AS Na+ influx was not affected by either DIDS or trifluoperazine. The present results indicate that in human erythrocytes an increase in internal Ca2+ activates on otherwise silent AS Na+-transport system, which is dependent on the metabolic integrity of the red cells.