4-Methylumbelliferyl Oleate
(Synonyms: 4-甲基伞形酮油酸酯) 目录号 : GC42444A fluorogenic lipase substrate
Cas No.:18323-58-5
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
4-Methylumbelliferyl (4-MU) oleate is a fluorogenic substrate for acid and alkaline lipases. It is cleaved by lipases, liberating 4-MU, which has an emission maximum at 445-454 nm. The excitation maximum for 4-MU is pH-dependent: 330, 370, and 385 nm at pH 4.6, 7.4, and 10.4, respectively.
| Cas No. | 18323-58-5 | SDF | |
| 别名 | 4-甲基伞形酮油酸酯 | ||
| Canonical SMILES | O=C1C=C(C)C2=C(C=C(OC(CCCCCCC/C=C\CCCCCCCC)=O)C=C2)O1 | ||
| 分子式 | C28H40O4 | 分子量 | 440.6 |
| 溶解度 | Chloroform: 20 mg/ml,DMF: 10 mg/ml,DMSO: 0.1 mg/ml | 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 | 2.2696 mL | 11.3482 mL | 22.6963 mL |
| 5 mM | 0.4539 mL | 2.2696 mL | 4.5393 mL |
| 10 mM | 0.227 mL | 1.1348 mL | 2.2696 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。
Purification and properties of rabbit liver acid-lipase (4-Methylumbelliferyl Oleate hydrolase)
Biochim Biophys Acta 1981 Aug 24;665(2):322-30.PMID:6895183DOI:10.1016/0005-2760(81)90017-5.
An acid lipase was purified from rabbit liver lysosomes by, in sequence, osmotic treatment of the lysosomal fraction, Sephadex LH-20, DEAE-Sephadex A-50, Bio-Gel A-5m, hydroxyapatite and, finally, Sephadex G-200 column chromatography. The substrate was 4-Methylumbelliferyl Oleate. The enzyme was solubilized by Sephadex LH-20 column chromatography instead of detergents and organic solvents, to obtain an intrinsic macromolecule. 4-Methylumbelliferyl Oleate hydrolase, osmotically released from lysosomal particles, had a very high molecular weight (greater than 800 000) which was reduced by gel filtration on a Sephadex LH-20 column; the final molecular weight of the purified enzyme was 58 000. The specific activity of 4-Methylumbelliferyl Oleate hydrolase increased at almost the same rate as acid cholesterol esterase and triacylglycerol lipase after Sephadex LH-20 column chromatography; the thermal stability of the activity of the three enzymes was almost identical. We also discuss the properties of the enzyme molecule and the interaction between the enzyme and the lysosomal membrane.
Proanthocyanidins as the main pancreatic lipase inhibitors in chokeberry fruits
Food Funct 2022 May 23;13(10):5616-5625.PMID:35506494DOI:10.1039/d1fo04429j.
Pancreatic lipase inhibitors are recognized as important in strategies for the management of overweight and obesity. The phytocompounds in chokeberry fruit show multidirectional pro-health effects, including anti-obesity activity. The aims of this study were to fractionate and identify the phenolic compounds of chokeberry fruit phenolic-rich extract that are active as pancreatic lipase inhibitors. Phenolic compounds were fractionated using Sephadex LH-20 resin, followed by polyphenol profile analysis using chromatographic and spectrophotometric methods, while pancreatic inhibitory activity was determined using 4-Methylumbelliferyl Oleate and emulsified triolein as enzyme substrates. Among the six fractions isolated from extract, two fractions rich in highly polymerized proanthocyanidins showed the greatest ability to inhibit pancreatic lipase activity. In comparison, fractions containing mainly low-molecular-weight phenolic compounds, such as phenolic acids, flavonols and anthocyanins, were 11-64 times less active. The most active fraction showed a mixed mode of pancreatic lipase inhibition, as determined by Lineweaver-Burk plot analysis, and exhibited a cumulative effect with orlistat. This study shows that black chokeberry polyphenols, particularly highly polymerized procyanidins, can effectively inhibit pancreatic lipase activity determined by in vitro methods.
Pancreatic lipase inhibitory constituents from Fructus Psoraleae
Chin J Nat Med 2020 May;18(5):369-378.PMID:32451094DOI:10.1016/S1875-5364(20)30043-1.
Pancreatic lipase (PL), a crucial enzyme in the digestive system of mammals, has been proven as a therapeutic target to prevent and treat obesity. The purpose of this study is to evaluate and characterize the PL inhibition activities of the major constituents from Fructus Psoraleae (FP), one of the most frequently used Chinese herbs with lipid-lowering activity. To this end, a total of eleven major constituents isolated from Fructus Psoraleae have been obtained and their inhibition potentials against PL have been assayed by a fluorescence-based assay. Among all tested compounds, isobavachalcone, bavachalcone and corylifol A displayed strong inhibition on PL (IC50 < 10 μmol·L-1). Inhibition kinetic analyses demonstrated that isobavachalcone, bavachalcone and corylifol A acted as mixed inhibitors against PL-mediated 4-Methylumbelliferyl Oleate (4-MUO) hydrolysis, with the Ki values of 1.61, 3.77 and 10.16 μmol·L-1, respectively. Furthermore, docking simulations indicated that two chalcones (isobavachalcone and bavachalcone) could interact with the key residues located in the catalytic cavity of PL via hydrogen binding and hydrophobic interactions. Collectively, these finding provided solid evidence to support that Fructus Psoraleae contained bioactive compounds with lipid-lowering effects via targeting PL, and also suggested that the chalcones in Fructus Psoraleae could be used as ideal leading compounds to develop novel PL inhibitors.
Measuring Lipolytic Activity to Support Process Improvements to Manage Lipase-Mediated Polysorbate Degradation
Pharm Res 2020 Jun 3;37(6):118.PMID:32495187DOI:10.1007/s11095-020-02812-0.
Purpose: Polysorbates are critical stabilizers in biopharmaceutical protein formulations. However, they may degrade in drug substance (DS) or drug product (DP) during storage. Degradation catalyzed by lipases present in host cell proteins (HCPs) is one suspected root cause. The purpose of this study was to develop an assay to detect lipolytic activity in biopharmaceutical DS and DP formulations. Methods: The assay is based on the hydrolysis of the lipase substrate 4-Methylumbelliferyl Oleate to yield the fluorescent product 4-methylumbelliferone. Results: First, the assay components and their concentrations (buffer salts and pH, solvent and inhibitor Orlistat) were established and optimized using a model lipase (Porcine pancreatic lipase) and cell culture harvest fluid that exhibited lipolytic activity. The assay was then successfully applied and thereby qualified in protein formulations and at lipase concentrations possibly encountered in actual biopharmaceutical DS and DP formulations. Conclusion: The lipase assay can be used to detect lipolytic activity in intermediate and final DS, for example during process optimization in downstream purification, to better and specifically reduce the level, or deplete, lipases from HCPs. The assay is also suitable to be applied during root cause investigations related to polysorbate degradation in biopharmaceutical DP.
Design, Synthesis, and Structure-Activity Relationship Study of Pyrazolones as Potent Inhibitors of Pancreatic Lipase
ChemMedChem 2021 May 18;16(10):1600-1604.PMID:33527731DOI:10.1002/cmdc.202000850.
Pancreatic lipase (PL), a key target for the prevention and treatment of obesity, plays crucial roles in the hydrolysis and absorption of in dietary fat. In this study, a series of pyrazolones was synthesized, and their inhibitory effects against PL were assayed by using 4-Methylumbelliferyl Oleate (4-MUO) as optical substrate for PL. Comprehensive structure-activity relationship analysis of these pyrazolones led us to design and synthesize a novel compound P32 (5-(naphthalen-2-yl)-2-phenyl-4-(thiophen-2-ylmethyl)-2,4-dihydro-3H-pyrazol-3-one) as a potent mixed-competitive inhibitor of PL (IC50 =0.30 μM). In addition, P32 displayed some selectivity over other known serine hydrolases. A molecular docking study for P32 demonstrated that the inhibitory activity of P32 towards PL could be attributed to the π-π interactions of 2-naphthyl unit (R1 ) and hydrophobic interactions of phenyl moiety (R3 ) with the active site of PL. Thus, P32 could serve as promising lead compound for the development of more efficacious and selective pyrazolones-type PL inhibitors for biomedical applications.