3-(3-Hydroxyphenyl)propionic acid
(Synonyms: 3-(3-羟基苯基)丙酸) 目录号 : GC60488
3-(3-Hydroxyphenyl)propionic acid (m-Hydroxyphenylpropionic acid, 3-Hydroxyhydrocinnamic acid) is one of the major metabolites of ingested caffeic acid and of the phenolic degradation products of proanthocyanidins by the microflora in the colon.
Cas No.:621-54-5
Sample solution is provided at 25 µL, 10mM.
;)
,-1-7$$$37316672.jpg');)
;)
;)
$$$36806353.jpg');)
;33(7)%EF%BC%9A546-561$$$37156877.jpg');)
;)
;)
;)
%201124-1138.$$$35908550.jpg');)
%20766-780.$$$37100057.jpg');)
%20418-432.$$$36893736.jpg');)
%EF%BC%9A-240-255.$$$35108512.jpg');)
533-545$$$36543525.jpg');)
%201-13.$$$36600053.jpg');)
;)
Quality Control & SDS
- View current batch:
- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
3-(3-Hydroxyphenyl)propionic acid (m-Hydroxyphenylpropionic acid, 3-Hydroxyhydrocinnamic acid) is one of the major metabolites of ingested caffeic acid and of the phenolic degradation products of proanthocyanidins by the microflora in the colon.
| Cas No. | 621-54-5 | SDF | |
| 别名 | 3-(3-羟基苯基)丙酸 | ||
| Canonical SMILES | O=C(O)CCC1=CC=CC(O)=C1 | ||
| 分子式 | C9H10O3 | 分子量 | 166.17 |
| 溶解度 | 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。 |
||
| 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 | |||
 |
1 mg | 5 mg | 10 mg |
| 1 mM | 6.0179 mL | 30.0897 mL | 60.1793 mL |
| 5 mM | 1.2036 mL | 6.0179 mL | 12.0359 mL |
| 10 mM | 0.6018 mL | 3.009 mL | 6.0179 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。
3-(3-Hydroxyphenyl)propionic acid, a microbial metabolite of quercetin, inhibits monocyte binding to endothelial cells via modulating E-selectin expression
Fitoterapia 2022 Jan;156:105071.PMID:34743931DOI:10.1016/j.fitote.2021.105071.
Adhesion of monocytes to endothelial cells is an important initiating step in atherogenesis. One of the most abundant flavonoids in the diet, quercetin has been reported to inhibit monocyte adhesion to endothelial cells. However, it is poorly absorbed in the upper gastrointestinal tract during oral intake but rather is metabolized by the intestinal microbiota into various phenolic acids. Since the biological properties of the microbial metabolites of quercetin remain largely unknown, herein, we investigated how the microbial metabolite of quercetin, 3-(3-Hydroxyphenyl)propionic acid (3HPPA) impact monocyte adhesion to endothelial cells. Direct treatment with 3HPPA for 24 h was not cytotoxic to human aortic endothelial cells (HAECs). Cotreatment with 3HPPA inhibited tumor necrosis factor α (TNFα)-induced adhesion of THP-1 monocytes to HAECs, and suppressed the upregulation of cell adhesion molecule E-selectin but not intercellular adhesion molecule 1 or vascular cell adhesion molecule 1. Furthermore, 3HPPA was found to inhibit TNFα-induced nuclear translocation and phosphorylation of the p65 subunit of nuclear factor κB (NF-κB). We conclude that 3HPPA mitigates the adhesion of monocytes to endothelial cells by suppressing the expression of the cell adhesion molecule E-selectin in HAECs via inhibition of the NF-κB pathway, providing additional evidence for the health benefits of dietary flavonoids and their microbial metabolites as therapeutic agents in atherosclerosis.
Flavonoid metabolite 3-(3-Hydroxyphenyl)propionic acid formed by human microflora decreases arterial blood pressure in rats
Mol Nutr Food Res 2016 May;60(5):981-91.PMID:26790841DOI:10.1002/mnfr.201500761.
There are reports of positive effects of quercetin on cardiovascular pathologies, however, mainly due to its low biovailability, the mechanism remains elusive. Here, we report that one metabolite formed by human microflora (3-(3-Hydroxyphenyl)propionic acid)relaxed isolated rat aorta and decreased arterial blood pressure in rats.
A 3-(3-Hydroxyphenyl)propionic acid catabolic pathway in Rhodococcus globerulus PWD1: cloning and characterization of the hpp operon
J Bacteriol 1997 Oct;179(19):6145-53.PMID:9324265DOI:10.1128/jb.179.19.6145-6153.1997.
Rhodococcus globerulus PWD1, a soil isolate from a polluted site in The Netherlands, is able to degrade a broad range of aromatic compounds. A novel gene cluster which appears to encode a pathway for the degradation of phenolic acids such as 3-(3-hydroxyphenyl)propionate (3HPP) has been cloned from the chromosome of this organism. Sequence analysis of a 7-kb region identified five open reading frames (ORFs). Analysis of mRNA showed that the genes were expressed during growth on 3HPP and 3-hydroxyphenylacetate (3HPA) but not during growth on m-cresol or succinate. The first ORF, hppA, which appears to be separately transcribed, had considerable amino acid identity with a number of hydroxylases. Transcriptional analysis indicates that the next four ORFs, hppCBKR, which are tightly clustered, constitute a single operon. These genes appear to encode a hydroxymuconic semialdehyde hydrolase (HppC), an extradiol dioxygenase (HppB), a membrane transport protein (HppK), and a member of the IclR family of regulatory proteins (HppR). The activities of HppB and HppC have been confirmed by enzyme assay of Escherichia coli hosts. The substrate specificity of HppB expressed from the cloned gene matches that of the meta-cleavage dioxygenase expressed from wild-type Rhodococcus grown on both 3HPP and 3HPA and is considerably more active against acid than against neutral catechols. The deduced amino acid sequences of the gene products have a recognizable homology with a broad range of enzymes and proteins involved in biodegradation and appear most similar to the mhp operon from E. coli K-12, which also encodes the degradation of 3HPP.
Genetic organization and characteristics of the 3-(3-Hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni TA441
Microbiology (Reading) 1999 Oct;145 ( Pt 10):2813-20.PMID:10537203DOI:10.1099/00221287-145-10-2813.
Comamonas testosteroni TA441 degrades 3-(3-hydroxyphenyl)propionate (3HPP) via the meta pathway. A gene cluster required for degradation of 3HPP was cloned from strain TA441 and sequenced. The genes encoding six catabolic enzymes, a flavin-type hydroxylase (mhpA), extradiol dioxygenase (mhpB), 2-keto-4-pentenoate hydratase (mhpD), acetaldehyde dehydrogenase (acylating) (mhpF), 4-hydroxy-2-ketovalerate aldolase (mhpE) and the meta cleavage compound hydrolase (mhpC), were found in this cluster, encoded in this order. mhpD and mhpF were separated by two genes, orf4 and orf5, which were not necessary for growth on 3HPP. The gene mhpR, encoding a putative transcriptional activator of the IcIR family, was located adjacent to mhpA in the opposite orientation. Disruption of the mhpB or mhpR genes affected growth on 3HPP or trans-3-hydroxycinnamate. The mhpB and mhpC gene products showed high specificity for 3-(2,3-dihydroxyphenyl)propionate (DHPP) and the meta cleavage compound produced from DHPP, respectively.
Regulation of the mhp cluster responsible for 3-(3-Hydroxyphenyl)propionic acid degradation in Escherichia coli
J Biol Chem 2003 Jul 25;278(30):27575-85.PMID:12748194DOI:10.1074/jbc.M303245200.
The mhp gene cluster from Escherichia coli constitutes a model system to study bacterial degradation of 3-(3-Hydroxyphenyl)propionic acid (3HPP). In this work the regulation of the inducible mhp catabolic genes has been studied by genetic and biochemical approaches. The Pr and Pa promoters, which control the expression of the divergently transcribed mhpR regulatory gene and mhp catabolic genes, respectively, show a peculiar arrangement leading to transcripts that are complementary at their 5'-ends. By using Pr-lacZ and Pa-lacZ translational fusions and gel retardation assays, we have shown that the mhpR gene product behaves as a 3HPP-dependent activator of the Pa promoter, being the expression from Pr constitutive and MhpR-independent. DNase I footprinting experiments and mutational analysis mapped an MhpR-protected region, centered at position -58 with respect to the Pa transcription start site, which is indispensable for MhpR binding and in vivo activation of the Pa promoter. Superimposed in the specific MhpR-mediated regulation of the Pa promoter, we have observed a strict catabolite repression control carried out by the cAMP receptor protein (CRP) that allows expression of the mhp catabolic genes when the preferred carbon source (glucose) is not available and 3HPP is present in the medium. Gel retardation assays revealed that the specific activator, MhpR, is essential for the binding of the second activator, CRP, to the Pa promoter. Such peculiar synergistic transcription activation has not yet been observed in other aromatic catabolic pathways, and the MhpR activator becomes the first member of the IclR family of transcriptional regulators that is indispensable for recruiting CRP to the target promoter.