1,2-Dihexanoyl-sn-glycerol
目录号 : GC41796
An analog of DAG
Cas No.:30403-47-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >95.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
1,2-Dihexanoyl-sn-glycerol is an analog of the protein kinase C (PKC)-activating second messenger diacylglycerol (DAG). Although the biological activities of 1,2-Dihexanoyl-sn-glycerol have not been well characterized, it is expected to behave similarly to 1,2-dioctanoyl-sn-glycerol .
| Cas No. | 30403-47-5 | SDF | |
| Canonical SMILES | OC[C@H](OC(CCCCC)=O)COC(CCCCC)=O | ||
| 分子式 | C15H28O5 | 分子量 | 288.4 |
| 溶解度 | DMF: 20 mg/ml,DMSO: 7 mg/ml,Ethanol: 30 mg/ml,PBS (pH 7.2): 0.25 mg/ml | 储存条件 | Store at -80°C; protect from light |
| 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 | 3.4674 mL | 17.337 mL | 34.6741 mL |
| 5 mM | 0.6935 mL | 3.4674 mL | 6.9348 mL |
| 10 mM | 0.3467 mL | 1.7337 mL | 3.4674 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。
Activation of phospholipase C and protein kinase C has little involvement in ADP-induced primary aggregation of human platelets: effects of diacylglycerols, the diacylglycerols, the diacylglycerol kinase inhibitor R59022, staurosporine and okadaic acid
Biochem J 1993 Mar 15;290 ( Pt 3)(Pt 3):849-56.PMID:8384448DOI:10.1042/bj2900849.
The primary phase of ADP-induced aggregation of human platelets does not involve appreciable formation of thromboxane A2 or release of granule contents; lack of formation of inositol trisphosphate has also been noted. Because these responses of platelets to ADP differ so markedly from their responses to other aggregating agents, the roles in ADP-induced aggregation of diacylglycerol, protein kinase C, increases in cytosolic [Ca2+], phosphorylation of pleckstrin (47 kDa) and phosphatases 1 and 2a were investigated. Washed human platelets, prelabelled with [14C]5-hydroxytryptamine and suspended in Tyrode solution (2 mM Ca2+, 1 mM Mg2+), were used for comparisons between the aggregation induced by 2-4 microM ADP, in the presence of fibrinogen, and that induced by 0.05 units/ml thrombin. The diacylglycerol kinase inhibitor 6-(2-[(4-fluorophenyl)phenyl-methylene]-1-piperidinylethyl)-7-meth yl-5H-thiazolo[3,2-a]-pyrimidin-5-one (R59022; 25 microM) had no, or only a slight, enhancing effect on ADP-induced aggregation, but potentiated thrombin-induced responses to a much greater extent. 1,2-Dihexanoyl-sn-glycerol or 1-oleoyl-2-acetyl-sn-glycerol (25 microM) added with or 30-90 s before ADP greatly potentiated aggregation without formation of thromboxane; staurosporine, an inhibitor of protein kinase C, reduced this potentiation. Staurosporine (25 nM) did not inhibit ADP-induced aggregation, although it strongly inhibited thrombin-induced aggregation and release of [14C]5-hydroxytryptamine. All these observations indicate little or no dependence of primary ADP-induced aggregation on the formation of diacylglycerol or on the activation of protein kinase C. At 2-4 microM, ADP did not significantly increase the phosphorylation of pleckstrin (studied with platelets prelabelled with [32P]orthophosphate), but 1,2-dihexanoyl-sn-glycerol- induced phosphorylation of pleckstrin was increased by ADP. Surprisingly, the diacylglycerols strongly inhibited the ADP-induced rise in cytosolic [Ca2+] concurrently with potentiation of ADP-induced aggregation; thus the extent of primary aggregation is independent of the level to which cytosolic [Ca2+] rises. Incubation of platelets with 1,2-Dihexanoyl-sn-glycerol or 1-oleoyl-2-acetyl-sn-glycerol for several minutes reversed their potentiating effects on aggregation, and inhibition was observed. Incubation of platelets with okadaic acid, an inhibitor of phosphatases 1 and 2a, inhibited ADP- and thrombin-induced aggregation; although the reason for this effect is unknown, it is unlikely to involve inhibition of phospholipase C, since formation of diacylglycerol appears to have little involvement in the primary phase of ADP-induced aggregation.
Kinetic selectivity of cholinephosphotransferase in mouse liver: the Km for CDP-choline depends on diacylglycerol structure
Biochem J 1993 Feb 1;289 ( Pt 3)(Pt 3):815-20.PMID:8382052DOI:10.1042/bj2890815.
The effects of different 1,2-diacyl-sn-glycerols on the kinetic properties of CDP-choline:1,2-diacylglycerol cholinephosphotransferase (EC 2.7.8.2) from mouse liver microsomes have been studied. Initial-velocity experiments were carried out with various concentrations of several species of diacylglycerol at different fixed concentrations of CDP-choline. Kinetic analysis of these data showed a family of intersecting lines consistent with a sequential kinetic mechanism of catalysis. The Km and Vmax. values derived from rate data revealed a pronounced effect of diacylglycerol species utilization on the Km value for CDP-choline. There was a biphasic relationship between diacylglycerol chain length and the Km for CDP-choline. Substitution of an unsaturated fatty acid in the sn-2 position of distearin also dramatically increased the CDP-choline Km value as well as the Vmax. 1,2-Dipalmitoyl-sn-glycerol was the preferred substrate over other disaturated species, but 1,2-Dihexanoyl-sn-glycerol could not be utilized. These results demonstrate the kinetic mechanism of in vitro catalysis and suggest a regulatory role for CDP-choline concentration in the diacylglycerol species selectivity of cholinephosphotransferase resulting in the de novo biosynthesis of different molecular species of phosphatidylcholine.
Effect of diacylglycerols on osteoclastic bone resorption
Calcif Tissue Int 1996 Aug;59(2):105-8.PMID:8687978DOI:10.1007/s002239900095.
We studied the effect of various synthetic diacylglycerols (DAGs) on bone resorption by rat and chick osteoclasts. 1-stearoyl-2-arachidonoyl-sn-glycerol (DAG IV), at a concentration of 100 microM, caused a significant reduction in resorption pit number in both species at 6 and 24 hours without any toxic effect. Over a 6-hour incubation period, a significant inhibition was seen at 10 and 100 microM in both species. 1,2-dioctanoyl-sn-glycerol (DAG I) and 1,2-Dihexanoyl-sn-glycerol (DAG III) caused a marked inhibition of resorption by rat osteoclasts at 6 hours, but there was recovery of bone-resorptive ability over a 24-hour incubation period. DAGs with the -rac conformation failed to have any effect on bone resorption. In time-lapse video studies, osteoclast motility was not influenced by any of the DAGs at any of the concentrations used. Our results indicate that DAGs with the -sn conformation inhibit bone resorption, and DAGs with the -rac conformation do not. The finding that DAGs, the physiological activators of protein kinase C (PKC), inhibit bone resorption provides further evidence for an important role of the PKC pathway in the regulation of osteoclast activity.
Substrate Specificity Analysis of Dihydrofolate/Dihydromethanopterin Reductase Homologs in Methylotrophic α-Proteobacteria
Front Microbiol 2018 Oct 11;9:2439.PMID:30364315DOI:10.3389/fmicb.2018.02439.
Methane-producing archaea and methylotrophic bacteria use tetrahydromethanopterin (H4MPT) and/or tetrahydrofolate (H4F) as coenzymes in one-carbon (C1) transfer pathways. The α-proteobacterium Methylobacterium extorquens AM1 contains a dihydromethanopterin reductase (DmrA) and two annotated dihydrofolate reductases (DfrA and DfrB). DmrA has been shown to catalyze the final step of H4MPT biosynthesis; however, the functions of DfrA and DfrB have not been examined biochemically. Moreover, sequence alignment (BLAST) searches have recognized scores of proteins that share up to 99% identity with DmrA but are annotated as diacylglycerol kinases (DAGK). In this work, we used bioinformatics and enzyme assays to provide insight into the phylogeny and substrate specificity of selected Dfr and DmrA homologs. In a phylogenetic tree, DmrA and homologs annotated as DAGKs grouped together in one clade. Purified histidine-tagged versions of the annotated DAGKs from Hyphomicrobium nitrativorans and M. nodulans (respectively, sharing 69 and 84% identity with DmrA) showed only low activity in phosphorylating 1,2-Dihexanoyl-sn-glycerol when compared with a commercial DAGK from Escherichia coli. However, the annotated DAGKs successfully reduced a dihydromethanopterin analog (dihydrosarcinapterin, H2SPT) with kinetic values similar to those determined for M. extorquens AM1 DmrA. DfrA and DfrB showed little or no ability to reduce H2SPT under the conditions studied; however, both catalyzed the NADPH-dependent reduction of dihydrofolate. These results provide the first evidence that DfrA and DfrB function as authentic dihydrofolate reductases, while DAGKs with greater than 69% identity to DmrA may be misannotated and are likely to function in H4MPT biosynthesis.
Control of phosphate transport in flounder renal proximal tubule primary cultures
Am J Physiol 1989 Apr;256(4 Pt 2):R850-7.PMID:2468299DOI:10.1152/ajpregu.1989.256.4.R850.
Unidirectional mucosal-to-serosal (Jm----s) and serosal-to-mucosal (Js----m) transepithelial phosphate fluxes across monolayers of flounder (Pseudopleuronectes americanus) renal proximal tubule cells in primary culture were examined for effects of diacylglycerols, phorbol ester, A23187, forskolin, and extracellular phosphate availability. Tissues were cultured on floating collagen rafts and studied short circuited in Ussing chambers. Transepithelial electrical properties were continuously monitored and were unaffected by any of the treatments compared with paired controls. Under usual conditions (phosphate = 0.4 mM) tissues invariably displayed net phosphate reabsorption [Js----m = 2.3 +/- 0.52; Jm----a = 7.1 +/- 1.77; Jnet = 4.9 +/- 1.45 (SE) nmol.cm-2.h-1]. Acute elevation of bath phosphate concentration above 0.5 mM stimulated net secretion. Exposure to 100 microM 1,2-Dihexanoyl-sn-glycerol stimulated net phosphate secretion within 30 min, the result of a fivefold increase in Js----m. Phorbol-12,13-didecanoate stimulated net phosphate secretion by increasing Js----m and decreasing Jm----s. The inactive diacylglycerol, 1,3-didecanoyl-rac-glycerol (100 microM), had no effect on phosphate fluxes. A23187 stimulated net phosphate secretion; Jm----s was reduced almost fourfold while Js----m was increased threefold. Forskolin (10 microM) stimulated net reabsorption more than threefold after a long latency (2 h). These data indicate that renal phosphate secretion and reabsorption may be regulated by several putative intracellular messengers. In addition, extracellular phosphate availability may modulate renal phosphate handling.