5-Hydroxyferulic acid
(Synonyms: 5-羟基阿魏酸) 目录号 : GC62809
5-Hydroxyferulic acid 是一种羟基肉桂酸，是苯丙烷途径的代谢产物。5-Hydroxyferulic acid 是芥子酸生物合成中的前体，也是 COMT 非酯化底物。
Cas No.:1782-55-4
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
5-Hydroxyferulic acid is a hydroxycinnamic acid and is a metabolite of the phenylpropanoid pathway. 5-Hydroxyferulic acid is a precursor in the biosynthesis of sinapic acid and is also a COMT non-esterifed substrate[1][2][3].
The product of the alfalfa Caffeic acid/5-hydroxyferulic acid 3/5-O-methyltransferase (COMT) catalyzed methylation of 5-Hydroxyferulic acid is sinapic acid. 5-Hydroxyferulic acid O-methyltransferase activities (pkat mg-1 protein) in stem material from COMT downregulates transgenic alfalfa[1].
[1]. K Parvathi, et al. Substrate Preferences of O-methyltransferases in Alfalfa Suggest New Pathways for 3-O-methylation of Monolignols. Plant J. 2001 Jan;25(2):193-202.
[2]. S Maury, et al. Tobacco O-methyltransferases Involved in Phenylpropanoid Metabolism. The Different Caffeoyl-Coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-methyltransferase and Caffeic acid/5-hydroxyferulic Acid 3/5-O-methyltransferase Classes Have Distinct Substrate Specificities and Expression Patterns. Plant Physiol. 1999 Sep;121(1):215-24.
[3]. Inoue, et al. Substrate Preferences of Caffeic acid/5-hydroxyferulic Acid 3/5-O-methyltransferases in Developing Stems of Alfalfa (Medicago Sativa L.). Arch Biochem Biophys. 2000 Mar 1;375(1):175-82.
| Cas No. | 1782-55-4 | SDF | |
| 别名 | 5-羟基阿魏酸 | ||
| 分子式 | C10H10O5 | 分子量 | 210.18 |
| 溶解度 | DMSO : 100 mg/mL (475.78 mM; Need ultrasonic) | 储存条件 | |
| 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 | 4.7578 mL | 23.7891 mL | 47.5783 mL |
| 5 mM | 0.9516 mL | 4.7578 mL | 9.5157 mL |
| 10 mM | 0.4758 mL | 2.3789 mL | 4.7578 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。
5-Hydroxyferulic acid methyl ester isolated from wasabi leaves inhibits 3T3-L1 adipocyte differentiation
Phytother Res 2018 Jul;32(7):1304-1310.PMID:29480572DOI:10.1002/ptr.6060.
To investigate the compounds present in wasabi leaves (Wasabia japonica Matsumura) that inhibit the adipocyte differentiation, activity-guided fractionation was performed on these leaves. 5-Hydroxyferulic acid methyl ester (1: 5-HFA ester), one of the phenylpropanoids, was isolated from wasabi leaves as a compound that inhibits the adipocyte differentiation. Compound 1 suppressed the intracellular lipid accumulation of 3T3-L1 cells without significant cytotoxicity. Gene expression analysis revealed that 1 suppressed the mRNA expression of 2 master regulators of adipocyte differentiation, PPARγ and C/EBPα. Furthermore, 1 downregulated the expression of adipogenesis-related genes, GLUT4, LPL, SREBP-1c, ACC, and FAS. Protein expression analysis revealed that 1 suppressed PPARγ protein expression. Moreover, to investigate the relationship between the structure and activity of inhibiting the adipocyte differentiation, we synthesized 12 kinds of phenylpropanoid analog. Comparison of the activity among 1 and its analogs suggested that the compound containing the substructure that possess a common functional group at the ortho position such as a catechol group exhibits the activity of inhibiting the adipocyte differentiation. Taken together, our findings suggest that 1 from wasabi leaves inhibits adipocyte differentiation via the downregulation of PPARγ.
Substrate preferences of caffeic acid/5-Hydroxyferulic acid 3/5-O-methyltransferases in developing stems of alfalfa (Medicago sativa L.)
Arch Biochem Biophys 2000 Mar 1;375(1):175-82.PMID:10683265DOI:10.1006/abbi.1999.1674.
Caffeic acid/5-Hydroxyferulic acid 3/5-O-methyltransferase (COMT, EC 1.2.1.68) catalyzes at least two reactions in lignin biosynthesis. Of its two supposed substrates in the lignin pathway, COMT from most sources methylates 5-Hydroxyferulic acid (5HFA) with two to three times higher activity than caffeic acid (CafA). The ratio of activity for 5HFA compared with CafA increases with the developmental age of alfalfa (Medicago sativa L.) stem internodes, from approximately 1:1 in young (third and fourth) internodes to 2:1 in mature (seventh and eighth) internodes. This observation, together with immunoblot analysis using antiserum raised against recombinant alfalfa COMT, suggests the presence of a different form of COMT, having preference for CafA compared with 5HFA, in young internodes. This apparently new O-methyltransferase (COMT II) was separated from the previously characterized COMT (COMT I) by anion exchange and hydrophobic interaction chromatography. COMT I, but not COMT II, was found in mature internodes. COMT II was not recognized by anti-(COMT I) serum. Furthermore, in addition to substrate preference, COMT II differed from COMT I in native relative molecular mass, pH optimum, and its very low K(m) for CafA. The possible physiological role of COMT II is discussed.
Characterization of bispecific caffeic acid/5-Hydroxyferulic acid O-methyltransferase from aspen
Phytochemistry 1992 May;31(5):1495-8.PMID:1368360DOI:10.1016/0031-9422(92)83093-e.
Bispecific O-methyltransferase (OMT, EC 2.1.1.68) which catalyses the meta-specific methylation of caffeic acid and 5-Hydroxyferulic acid was purified to homogeneity from the developing secondary xylem of aspen (Populus tremuloides). The enzyme was purified by conventional techniques and affinity chromatography on S-adenosyl-L-homocysteine agarose using substrate elution. The enzyme has a M(r) of 40,000 as determined by SDS-PAGE. Amino acid sequences of three peptides produced from a proteolytic digest of bispecific OMT were obtained by automated Edman degradation. Polyclonal antibodies raised against the purified OMT reacted strongly to OMT in both purified and unpurified fractions in western blots. Addition of an equal concentration of anti-OMT IgG to crude extract protein inhibited OMT activity by more than 70%.
Tobacco O-methyltransferases involved in phenylpropanoid metabolism. The different caffeoyl-coenzyme A/5-hydroxyferuloyl-coenzyme A 3/5-O-methyltransferase and caffeic acid/5-Hydroxyferulic acid 3/5-O-methyltransferase classes have distinct substrate specificities and expression patterns
Plant Physiol 1999 Sep;121(1):215-24.PMID:10482677DOI:10.1104/pp.121.1.215.
The biosynthesis of lignin monomers involves two methylation steps catalyzed by orthodiphenol-O-methyltransferases: caffeic acid/5-Hydroxyferulic acid 3/5-O-methyltransferases (COMTs) and caffeoyl-coenzyme A (CoA)/5-hydroxyferuloyl-CoA 3/5-O-methyltransferases (CCoAOMTs). Two COMT classes (I and II) were already known to occur in tobacco (Nicotiana tabacum) and three distinct CCoAOMT classes have now been characterized. These three CCoAOMT classes displayed a maximum level of expression at different stages of stem development, in accordance with their involvement in the synthesis of lignin guaiacyl units. Expression profiles upon tobacco mosaic virus infection of tobacco leaves revealed a biphasic pattern of induction for COMT I, COMT II, and CCoAOMTs. The different isoforms were expressed in Escherichia coli and our results showed that CCoAOMTs and, more surprisingly, COMTs efficiently methylated hydroxycinnamoyl-CoA esters. COMT I was also active toward 5-hydroxyconiferyl alcohol, indicating that COMT I that catalyzes syringyl unit synthesis in planta may operate at the free acid, CoA ester, or alcohol levels. COMT II that is highly inducible by infection also accepted caffeoyl-CoA as a substrate, thus suggesting a role in ferulate derivative deposition in the walls of infected cells. Tobacco appears to possess an array of O-methyltransferase isoforms with variable efficiency toward the diverse plant o-diphenolic substrates.
An Arabidopsis gene encoding a putative 14-3-3-interacting protein, caffeic acid/5-Hydroxyferulic acid O-methyltransferase
Biochim Biophys Acta 1997 Sep 12;1353(3):199-202.PMID:9349713DOI:10.1016/s0167-4781(97)00096-1.
AFT1, a 14-3-3 protein from Arabidopsis thaliana, was used as a 'bait' in the two-hybrid system to identify its interacting proteins. A caffeic acid/5-Hydroxyferulic acid O-methyltransferase, OMT1, was identified as one of the several proteins that specifically interacts with AFT1 in yeast cells. The physical interaction between AFT1 and a partial OMT1 polypeptide can be demonstrated in vitro by using bacterially expressed proteins. A single copy gene was found to encode OMT1 in Arabidopsis, and its expression is both spatially and temporally regulated.