A23187 (calcium magnesium salt)
(Synonyms: Calcimycin) 目录号 : GC42659A cation ionophore
Sample solution is provided at 25 µL, 10mM.
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- Purity: >98.00%
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- SDS (Safety Data Sheet)
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A23187 is a divalent cation ionophore. While more selective for Mn2+, it is commonly used to facilitate the movement of Ca2+ into cells, triggering the activation of intracellular calcium-dependent pathways.[1] A23187 is also used to produce apoptosis through calcium overload, as occurs during hypoxic or oxidative stress.[2],[3]
Reference:
[1]. Sullivan, T.J., and Parker, C.W. Pharmacologic modulation of inflammatory mediator release by rat mast cells. Am. J. Pathol. 85(2), 437-464 (1976).
[2]. Maecker, H.T., Hedjbeli, S., Alzona, M., et al. Comparison of apoptosis signaling through T cell receptor, Fas, and calcium ionophore. Exp. Cell Res. 222(1), 95-102 (1996).
[3]. Cho, S.Y., Lee, J.H., Bae, H.D., et al. Transglutaminase 2 inhibits apoptosis induced by calcium-overload through down-regulation of Bax. Exp. Mol. Med. 42(9), 639-650 (2010).
| Cas No. | SDF | ||
| 别名 | Calcimycin | ||
| 化学名 | 5-(methylamino)-2-[[(2R,3R,6S,8S,9R,11R)-3,9,11-trimethyl-8-[(1S)-1-methyl-2-oxo-2-(1H-pyrrol-2-yl)ethyl]-1,7-dioxaspiro[5.5]undec-2-yl]methyl]-4-benzoxazolecarboxylic acid, calcium salt (2:1) 5-(methylamino)-2-[[(2R,3R,6S,8S,9R,11R)-3,9,11-trimethyl-8-[( | ||
| 分子式 | [C29H36N3O6]2 Ca •[C29H36N3O6]2 Mg | 分子量 | 523.6 |
| 溶解度 | 3mg/mL in ethanol or DMF | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 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。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.9099 mL | 9.5493 mL | 19.0985 mL |
| 5 mM | 0.382 mL | 1.9099 mL | 3.8197 mL |
| 10 mM | 0.191 mL | 0.9549 mL | 1.9099 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Tonic contraction of canine gastric muscle during long-lasting calcium removal and its dependence on magnesium
J Physiol 1987 Dec;393:375-97.PMID:3128659DOI:10.1113/jphysiol.1987.sp016828.
1. Tonic contractions induced by acetylcholine (ACh) in canine gastric fundus preparations were shown to persist during long-lasting exposure to Ca2+-free solution containing EGTA (1 mmol/l). These EGTA-resistant contractions amounted to up to more than 50% of maximal ACh-control responses in physiological salt solution. They could be evoked repeatedly for more than 20 h without reduction in size, each contraction lasting as long as ACh was present. 2. During prolonged exposure to Ca2+-free solution at normal Mg2+ concentration ([Mg2+]O = 1.2 mmol/l), the preparations exhibited a slowly developing contracture (elevation of the baseline of contraction), which was particularly pronounced in strips taken from the circular layer of the muscular wall (44% of control ACh-maximum after 4 h in Ca2+-free solution). Contracture could be suppressed either by increasing [Mg2+]O to 6-10 mmol/l or by depolarizing the cell membrane (replacement of external Na+ by K+). However, contracture also developed if, at physiological [Na+]O and [K+]O, [Mg2+]O was further increased to 50 mmol/l. 3. The combined effects of [Mg2+]O and membrane potential suggest that contracture is caused by a gain of Mg2+ by the cells. This conclusion is based on the assumption that (a) the cytoplasmic Mg2+ concentration is determined by the transmembrane electrochemical gradient acting on Mg2+, the magnesium permeability of the cell membrane (PMg) and an active extrusion mechanism, and that (b) Ca2+ removal leads to an increase of PMg which is (partly) prevented by an appropriate increase of [Mg2+]O. 4. 45Ca efflux experiments, performed at [Mg2+]O = 10 mmol/l to avoid interference of ACh responses with contracture, showed that the cellular 45Ca content decreased from some 200 mumol/kg wet wt. to less than 10 mumol/kg wet wt. within 10-20 h in Ca2+-free solution. Activations by ACh did not produce any detectable increase in 45Ca efflux. 5. The calcium ionophore A23187 (10(-5) mol/l), applied in order to increase the calcium permeability of the cell membrane, did not reduce the EGTA-resistant contractions. 6. Experimental procedures conducted to replace calcium within intracellular stores by strontium or barium did not affect the EGTA-resistant ACh response. However, prior uptake of manganese by the cells had an amplifying effect. 7. Caffeine (30 mmol/l) failed to produce contraction in Ca2+-free solution, whereas ACh evoked contractile responses, both in the presence of and after application of caffeine.(ABSTRACT TRUNCATED AT 400 WORDS)
Zinc-mediated hatching of eggs of soybean cyst nematode,Heterodera glycines
J Chem Ecol 1984 Feb;10(2):361-72.PMID:24318504DOI:10.1007/BF00987863.
Egg hatching of the soybean cyst nematode,Heterodera glycines, was not affected by millimolar concentrations of calcium sulfate or calcium chloride. However, zinc chloride and zinc sulfate caused strong and moderate increases in hatching, respectively. The inhibitors of calcium transport, ruthenium red and lanthanum chloride, and calcium ionophore A23187 had no effect on hatching in the presence or absence of 3 mM zinc chloride. Selected chelators decreased the zinc-induced hatching ofH. glycines eggs. Eggs exhibited a formation constant with zinc between 5.5 and 11.2. The addition of zinc chloride after chelation with EDTA and rinsing caused expected hatching rates. Concentrations of calcium chloride, manganese chloride, and magnesium chloride had no effect on hatching of eggs in zinc chloride, but reduced hatching at higher concentrations, possibly by osmotic influences. Hatching of eggs was increased as the time of exposure to zinc chloride was increased and was maximal at 28 °C and a pH of 5.3. Picrolonic acid, a known hatching stimulant, increasedH. glycines hatching, while sodium metavanadate had no effect. Analysis of seasonal hatching during 1981-1982 in untreated control eggs indicated that hatching was most pronounced in May.
Potassium- and ionophore A23187-induced discharge of secretory protein in guinea pig pancreatic lobules. Role of extracellular calcium
J Biol Chem 1980 May 25;255(10):4918-27.PMID:6246088doi
Elevated concentrations of potassium chloride (50 to 120 mM) in the incubation medium stimulated in vitro discharge of secretory protein from guinea pig pancreatic lobules. The effect of potassium was not inhibited by 10(-4) M atropine, sodium substitutes, or 10(-5) M tetrodotoxin. Exposure of lobules to elevated concentrations of potassium chloride did not increase the release of tissue lactic dehydrogenase and resulted in the appearance of exocytotic images detected by electron microscopy. The time course and extent of discharge due to 75 mM KCl were similar to those caused by the ionophore A23187 and the secretory effect of both agents depended on extracellular calcium and intracellular energy reserves. Potassium chloride stimulation of 75 mM increased the influx of extracellular calcium by 49%, as measured by net 45Ca uptake. Optimal carbamylcholine chloride or pancreozymin stimulation consistently showed a greater effect on discharge than optimal KCl or A23187 stimulation and the additional effect depended on the ability of these physiological secretagogues to recruit calcium from intracellular sources. Potassium chloride stimulation did not result in cyclic GMP elevations in the presence of atropine and those elevations due to A23187 stimulation were small (21 to 30%) and dissimilar both in character (calcium dependence) and time course compared to those resulting from the physiological secretagogues. These findings allow us to define two interrelated pathways which couple hormonal stimulation and discharge of secretory protein in the exocrine pancreas.
The role of calcium in the regulation of [3H]hemicholinium-3 binding sites in rat brain
Neuropharmacology 1988 Dec;27(12):1301-8.PMID:3149725DOI:10.1016/0028-3908(88)90034-2.
The role of calcium in the regulation of sodium-dependent high-affinity uptake of choline was assessed in vitro in slices of the rat brain, by measuring the specific binding of [3H]hemicholinium-3 ([3H]HCh-3) and the uptake of [3H]choline. Depolarization with potassium of slices of hippocampus, cortex, or striatum significantly increased the specific binding of [3H]HCh-3 when compared to control slices. However, the observed potentiation of specific binding of [3H]HCh-3 was markedly inhibited by the removal of calcium from the incubation medium in cortex or hippocampus, but not in slices of striatum. Alterations in the uptake of [3H]choline directly paralleled the observed changes in the specific binding of [3H]HCh-3 in striatum of the rat and were unaffected by the reduction of calcium in the incubation medium. The inorganic calcium channel antagonists, cadmium and cobalt, but not magnesium, zinc, manganese or lanthanum, significantly inhibited the 40 mM potassium chloride-induced stimulation of the binding of [3H]HCh-3 in the striatum. Finally, the calcium ionophore A23187 significantly increased the binding of [3H]HCh-3 in slices of striatum, either in the presence or absence of calcium in the bathing medium. This study demonstrates regional differences in the role of extracellular calcium in the regulation of the uptake of choline and suggests the involvement of intracellular release of calcium in the in vitro regulation of the sodium-dependent high-affinity uptake of choline in the striatum.
Biochemical characterization of phospholipase D activity from human neutrophils
Eur J Biochem 1989 Dec 22;186(3):717-24.PMID:2558015DOI:10.1111/j.1432-1033.1989.tb15265.x.
We have found a phospholipase D activity in the postnuclear fraction of human neutrophils, employing phosphatidylinositol as exogenous substrate. This phospholipase D activity was assessed by both phosphatidate formation and by free inositol release in the presence of 15 mM LiCl in the reaction mixture and in the absence of Mg2+ ions to prevent inositol-1-phosphate phosphatase activity. To assess further the phospholipase D activity, we studied its capacity to catalyze a transphosphatidylation reaction, as a unique feature of the enzyme. It was detected as [14C]phosphatidylethanol formation when the postnuclear fraction was incubated with [14C]phosphatidylinositol in the presence of ethanol. The phospholipase D showed a major optimum pH at 7.5 and a minor one at pH 5.0. Neutral and acid phospholipase D activities were differentially located in subcellular fractionation studies of resting neutrophils, namely in the cytosol and in the azurophilic granules, respectively. Neutral phospholipase D required Ca2+ ions to the active, whereas the acid enzyme activity was Ca2(+)-independent. The neutral phospholipase D activity showed a certain specificity for phosphatidylinositol, as it was able to hydrolyze phosphatidylinositol at a much higher rate than phosphatidylcholine, in the absence and in the presence of different detergents. This neutral phospholipase D activity behaved as a protein of high molecular mass (350-400 kDa) by gel filtration chromatography. Moreover, neutral phospholipase D activity was detected in the postnuclear fraction of human monocytes, by measuring free inositol release from phosphatidylinositol as exogenous substrate, under the same experimental conditions as those used with neutrophils. The enzyme displayed similar specific activities in both cell types as well as the same degree of activation after cell stimulation with the calcium ionophore A23187. These results demonstrate the existence of two phospholipase D activities with different pH optima and intracellular location in human neutrophils. Furthermore, these results suggest that this phospholipase D can play a role in signal-transducing processes during cell stimulation in human phagocytes.