推荐产品
质量水平
方案
≥98%
表单
powder
技术
thin layer chromatography (TLC): suitable
溶解性
H2O: soluble 50 mg/mL, clear, colorless
储存温度
−20°C
SMILES字符串
NC1CCCCC1.NC2CCCCC2.C[C@@H]3O[C@H](OP(O)(O)=O)[C@@H](O)[C@H](O)[C@@H]3O
InChI
1S/2C6H13N.C6H13O8P/c2*7-6-4-2-1-3-5-6;1-2-3(7)4(8)5(9)6(13-2)14-15(10,11)12/h2*6H,1-5,7H2;2-9H,1H3,(H2,10,11,12)/t;;2-,3+,4+,5-,6+/m..0/s1
InChI key
FQMPFZHILABVMA-PEJHDPODSA-N
应用
β-L-Fucose 1-phosphate is suitable as both substrate and product to identify, differentiate and characterize GTP fucose pyrophosphorylase(s) (GFPP; fucose-1-phosphate guanylyltransferases) involved in the formation of the nucleotide-sugar GDP-beta-l-fucose and other fucosylation donor substrates such as 3,3′-Diaminobenzidine (GDP)-β-l-fucose. β-L-Fucose 1-phosphate may be used to generate new fucosylation donor substrates for use in glycan fucosylation research.
其他说明
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
监管及禁止进口产品
历史批次信息供参考:
分析证书(COA)
Lot/Batch Number
Toshihisa Kotake et al.
The Journal of biological chemistry, 283(13), 8125-8135 (2008-01-18)
Monomeric sugars generated during the metabolism of polysaccharides, glycoproteins, and glycolipids are imported to the cytoplasm and converted to respective nucleotide sugars via monosaccharide 1-phosphates, to be reutilized as activated sugars. Because L-fucose (L-Fuc) is activated mainly in the form
Bing Ma et al.
Glycobiology, 16(12), 158R-184R (2006-09-16)
Fucosylated carbohydrate structures are involved in a variety of biological and pathological processes in eukaryotic organisms including tissue development, angiogenesis, fertilization, cell adhesion, inflammation, and tumor metastasis. In contrast, fucosylation appears less common in prokaryotic organisms and has been suggested
GDP-L-fucose pyrophosphorylase. Purification, cDNA cloning, and properties of the enzyme.
Pastuszak I, Ketchum C, Hermanson G, et al.
The Journal of Biological Chemistry, 4273, 30165-30174 (1998)
Stephen Quirk et al.
Biochemistry, 44(32), 10854-10863 (2005-08-10)
GTP-l-fucose pyrophosphorylase (GFPP, E. C. 2.7.7.30) catalyzes the reversible condensation of guanosine triphosphate and beta-l-fucose-1-phosphate to form the nucleotide-sugar GDP-beta-l-fucose. The enzyme functions primarily in the mammalian liver and kidney to salvage free l-fucose during the breakdown of glycolipids and
Stephen Quirk et al.
Biochemistry, 44(39), 13172-13178 (2005-09-28)
GTP-l-fucose pyrophosphorylase(GFPP) catalyzes the reversible formation of the nucleotide-sugar GDP-beta-l-fucose from guanosine triphosphate and beta-l-fucose-1-phosphate. The enzyme functions primarily in the mammalian liver and kidney to salvage free fucose during the breakdown of glycoproteins and glycolipids. GFPP shares little primary
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