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About This Item
Empirical Formula (Hill Notation):
C6H11O8P · 2C6H14N
Molecular Weight:
442.48
MDL number:
UNSPSC Code:
12352201
PubChem Substance ID:
NACRES:
NA.25
Quality Level
assay
≥98%
form
powder
technique(s)
thin layer chromatography (TLC): suitable
solubility
H2O: soluble 50 mg/mL, clear, colorless
storage temp.
−20°C
SMILES string
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
Application
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.
Other Notes
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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
Leonie Engels et al.
Glycobiology, 24(2), 170-178 (2013-11-20)
Fucosyltransferases (FucTs) are essential tools for the synthesis of fucosylated glycoconjugates. Multistep enzyme catalysis of fucosylated glycans is not limited as long as isolated and well-characterized FucTs are available. The present paper introduces a novel bacterial α1,2-FucT of the glycosyltransferase
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)
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
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
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