2F-Peracetyl-Fucose
(Synonyms: 2,6-二脱氧-2-氟-L-吡喃半乳糖三乙酸酯,1,3,4-Tri-O-acetyl-2-deoxy-2-fluoro-L-fucopyranos) 目录号 : GC46549
An inhibitor of protein fucosylation
Cas No.:188783-78-0
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
2F-Peracetyl-fucose is an inhibitor of protein fucosylation.[1] It inhibits fucosylation of IgG1 monoclonal antibodies produced by CHO-DG44 cells when used at a concentration of 50 µM. It reduces intracellular GDP-fucose levels in CHO-DG44 cells in a concentration-dependent manner. 2F-Peracetyl-fucose (100 µM) also decreases intracellular fucose levels in A. thaliana seedlings.[2] 2F-Peracetyl-fucose decreases root length in A. thaliana seedlings in a concentration-dependent manner.
Reference:
[1].Okeley, N.M., Alley, S.C., Anderson, M.E., et al.Development of orally active inhibitors of protein and cellular fucosylationProc. Natl. Acad. Sci. USA110(14)5404-5409(2013)
[2].Villalobos, J.A., Yi, B.R., and Wallace, I.S.2-Fluoro-L-fucose is a metabolically incorporated inhibitor of plant cell wall polysaccharide fucosylationPLoS One10(9)e0139091(2015)
| Cas No. | 188783-78-0 | SDF | |
| 别名 | 2,6-二脱氧-2-氟-L-吡喃半乳糖三乙酸酯,1,3,4-Tri-O-acetyl-2-deoxy-2-fluoro-L-fucopyranos | ||
| Canonical SMILES | O=C(C)O[C@@H]([C@H]([C@@H]1F)OC(C)=O)[C@@H](OC1OC(C)=O)C | ||
| 分子式 | C12H17FO7 | 分子量 | 292.3 |
| 溶解度 | Chloroform: soluble,Methanol: soluble,DMSO: 10 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 | 3.4211 mL | 17.1057 mL | 34.2114 mL |
| 5 mM | 0.6842 mL | 3.4211 mL | 6.8423 mL |
| 10 mM | 0.3421 mL | 1.7106 mL | 3.4211 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。
The role of altered glycosylation in human nucleus pulposus cells in inflammation and degeneration
Eur Cell Mater 2021 Mar 28;41:401-420.PMID:33774812DOI:10.22203/eCM.v041a26.
Intervertebral disc (IVD) degeneration causes low-back pain through disc compression, prolapse and herniation. Inflammation of the IVD and subsequent degeneration produce altered glycosylation profiles in several animal models of IVD injury and ageing, although the function of this altered glycosylation pattern in a human is unknown. Altered N-glycome, specifically sialylated and fucosylated N-glycosylation motif expression, might play a role in inflammation and disease progression. Healthy (foetal and adolescent idiopathic scoliosis) and degenerated (lumbar degeneration) human IVD glycosylation patterns were studied using lectin histochemistry. Small-molecule fluorinated sugar analogues (3Fax-Peracetyl Neu5Ac; 2F-Peracetyl-Fucose) were used to inhibit sialylation and fucosylation in an in vitro model of inflammation, to investigate their effects on the glycosignature, cell metabolism, extracellular matrix synthesis and cell migration. The effects of interleukin (IL)-1β, tumour necrosis factor (TNF)-α and IL-6 on glycosylation in human nucleus pulposus cells were investigated by lectin histochemistry, PCR and enzyme-linked immunosorbent assay (ELISA). In the in vitro model of IVD degeneration, cytokine-induced inflammation-induced hypersialylation was observed, as indicated by Sambucus nigra I binding. However, this modification was inhibited by the sialyltransferase inhibitor. Inhibition of sialylation and fucosylation modulates cell migration and protein translation of catabolic enzymes in response to inflammation. The altered patterns of glycosylation in human tissue in degeneration was consistent with previous IVD studies in murine, bovine and ovine models. The present study was the first functional investigation of glycosylation in human degenerated IVD, elucidating the role of the glycome in disease progression and identified potential therapeutic targets for future regenerative therapies.
Protein Core Fucosylation Regulates Planarian Head Regeneration via Neoblast Proliferation
Front Cell Dev Biol 2021 Jul 16;9:625823.PMID:34336817DOI:10.3389/fcell.2021.625823.
Protein glycosylation is an important posttranslational modification that plays a crucial role in cellular function. However, its biological roles in tissue regeneration remain interesting and primarily ambiguous. In this study, we profiled protein glycosylation during head regeneration in planarian Dugesia japonica using a lectin microarray. We found that 6 kinds of lectins showed increased signals and 16 kinds showed decreased signals. Interestingly, we found that protein core fucosylation, manifested by Lens culinaris agglutinin (LCA) staining, was significantly upregulated during planarian head regeneration. Lectin histochemistry indicated that the LCA signal was intensified within the wound and blastemal areas. Furthermore, we found that treatment with a fucosylation inhibitor, 2F-Peracetyl-Fucose, significantly retarded planarian head regeneration, while supplement with L-fucose could improve DjFut8 expression and stimulate planarian head regeneration. In addition, 53 glycoproteins that bound to LCA were selectively isolated by LCA-magnetic particle conjugates and identified by LC-MS/MS, including the neoblast markers DjpiwiA, DjpiwiB, DjvlgA, and DjvlgB. Overall, our study provides direct evidence for the involvement of protein core fucosylation in planarian regeneration.
Fucosyltransferase 8 modulates receptor tyrosine kinase activation and temozolomide resistance in glioblastoma cells
Am J Cancer Res 2021 Nov 15;11(11):5472-5484.PMID:34873473doi
Alteration of extracellular glycosylation is a hallmark of malignant characteristics. In this study, we revealed that fucosyltransferase 8 (FUT8), an enzyme that mediates the core fucosylation of N-linked glycosylation, is an important regulator of malignant characteristics in human glioma that acts by modifying the activities of both the HGF receptor (MET) and epidermal growth factor receptor (EGFR). mRNA and protein expression levels of FUT8 were frequently upregulated in gliomas, and these events were showed positive correlations with advanced tumor grade, recurrence, and decreased overall survival. Silencing FUT8 expression in glioma cells suppressed cell growth, migration, and invasion, whereas overexpression of FUT8 was sufficient to enhance these phenotypes. Mechanistic investigations revealed that FUT8 was involved in the alteration of fucosylation status that was attached to MET and EGFR, changing MET responses after HGF stimulation, as well as in the transactivation of EGFR. Importantly, altering FUT8 expression or using the fucosylation inhibitor 2F-Peracetyl-Fucose sensitized the efficacy of of temozolomide (TMZ) therapy. Collectively, these results suggested that FUT8 dysregulation contributed to the malignant behaviors of glioma cells and provide novel insights into the significance of fucosylation in receptor tyrosine kinase activity and TMZ resistance.