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α-(1-2,3,4,6)-L-Fucosidase (Homo sapiens)

Product code: E-FUCHS

10 Units at 25oC (~ 34 Units at 37oC)

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Content: 10 Units at 25oC (~ 34 Units at 37oC)
Shipping Temperature: Ambient
Storage Temperature: 2-8oC
Formulation: In 3.2 M ammonium sulphate
Physical Form: Suspension
Stability: > 1 year under recommended storage conditions
Enzyme Activity: α-Fucosidase
EC Number:
CAZy Family: GH29
CAS Number: 9037-65-4
Synonyms: alpha-L-fucosidase; alpha-L-fucoside fucohydrolase
Source: Homo sapiens
Molecular Weight: 52,000
Concentration: Supplied at ~ 50 U/mL
Expression: Recombinant from Homo sapiens
Specificity: Broad specificity; hydrolysis of terminal non-reducing α-(1-2,3,4,6)-linked L-fucose residues from glycoproteins and oligosaccharides
Specific Activity: ~ 3 U/mg protein (pH 4.0, 25°C on pNP-α-L-fucopyranoside);
~ 14 U/mg protein (pH 4.0, 37°C on pNP-α-L-fucopyranoside);
~ 41 U/mg protein (pH 4.0, 50°C on pNP-α-L-fucopyranoside)
Unit Definition: One Unit of α-L-fucosidase activity is defined as the amount of enzyme required to release one µmole of p-nitrophenol (pNP) per minute from p-nitrophenyl-α-L-fucopyranoside (1 mM) in sodium acetate buffer (100 mM) at pH 4.0 at the temperatures indicated.
Temperature Optima: 50oC
pH Optima: 4
Application examples: For use in glycobiology research.

High purity α-(1-2,3,4,6)-L-Fucosidase (Homo sapiens) for use in research, biochemical enzyme assays and in vitro diagnostic analysis.

Display full list of our enzyme products for Carbohydrate Active enZYmes and glycobiology research.

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Safety Data Sheet
Data Sheet

Root-knot nematode chemotaxis is positively regulated by L-galactose sidechains of mucilage carbohydrate rhamnogalacturonan-I.

Tsai, A. Y. L., Iwamoto, Y., Tsumuraya, Y., Oota, M., Konishi, T., Ito, S., Kotake, T., Ishikawa, H. & Sawa, S. (2021). Science Advances, 7(27), eabh4182.

Root-knot nematodes (RKNs) are plant parasites and major agricultural pests. RKNs are thought to locate hosts through chemotaxis by sensing host-secreted chemoattractants; however, the structures and properties of these attractants are not well understood. Here, we describe a previously unknown RKN attractant from flaxseed mucilage that enhances infection of Arabidopsis and tomato, which resembles the pectic polysaccharide rhamnogalacturonan-I (RG-I). Fucose and galactose sidechains of the purified attractant were found to be required for attractant activity. Furthermore, the disaccharide α-L-galactosyl-1,3-L-rhamnose, which forms the linkage between the RG-I backbone and galactose sidechains of the purified attractant, was sufficient to attract RKN. These results show that the α-L-galactosyl-1,3-L-rhamnose linkage in the purified attractant from flaxseed mucilage is essential for RKN attraction. The present work also suggests that nematodes can detect environmental chemicals with high specificity, such as the presence of chiral centers and hydroxyl groups.

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Development of a 1, 2-difluorofucoside activity-based probe for profiling GH29 fucosidases.

Luijkx, Y. M., Jongkees, S., Strijbis, K. & Wennekes, T. (2021). Organic & Biomolecular Chemistry, 19(13), 2968-2977.

GH29 α-L-fucosidases catalyze hydrolysis of terminal α-L-fucosyl linkages with varying specificity and are expressed by prominent members of the human gut microbiota. Both homeostasis and dysbiosis at the human intestinal microbiota interface have been correlated with altered fucosidase activity. Herein we describe the development of a 2-deoxy-2-fluoro fucosyl fluoride derivative with an azide mini-tag as an activity-based probe (ABP) for selective in vitro labelling of GH29 α-L-fucosidases. Only catalytically active fucosidases are inactivated by this ABP, allowing their functionalization with a biotin reporter group via the CuAAC reaction and subsequent in-gel detection at nanogram levels. The ABP we present here is shown to be active against a GH29 α-L-fucosidase from Bacteroides fragilis and capable of labeling two other GH29 α-L-fucosidases with different linkage specificity, illustrating its broader utility. This novel ABP is a valuable addition to the toolbox of fucosidase probes by allowing identification and functional studies of the wide variety of GH29 fucosidases, including those in the gut microbiota.

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Characterization of polysaccharides from different species of brown seaweed using saccharide mapping and chromatographic analysis.

Chen, S., Sathuvan, M., Zhang, X., Zhang, W., Tang, S., Liu, Y. & Cheong, K. L. (2021). BMC Chemistry, 15(1), 1-11.

Brown seaweed polysaccharides (BSPs) are one of the primary active components from brown seaweed that has a range of pharmaceutical and biomedical applications. However, the quality control of BSPs is a challenge due to their complicated structure and macromolecule. In this study, saccharide mapping based on high-performance liquid chromatography (HPLC), multi-angle laser light scattering, viscometer, and refractive index detector (HPSEC-MALLS-Vis-RID), and Fourier transform infrared (FT-IR) were used to discriminate the polysaccharides from nine different species of brown algae (BA1-9). The results showed that BSPs were composed of β-D-glucans and β-1,3−1,4-glucan linkages. The molecular weight, radius of gyration, and intrinsic viscosity of BSPs were ranging from 1.718 × 105 Da to 6.630 × 105 Da, 30.2 nm to 51.5 nm, and 360.99 mL/g to 865.52 mL/g, respectively. Moreover, α values of BSPs were in the range of 0.635 to 0.971, which indicated a rigid rod chain conformation. The antioxidant activities of BSPs exhibited substantial radical scavenging activities against DPPH (1,1-diphenyl-2-picrylhydrazyl) and ABTS (2, 2’-azino-bis-3-ethylbenzothiazoline-6-sulfonic acid) radicals, which indicated that the use of BSPs might be a potential approach for antioxidant supplements. Thus, this study gives insights about the structure-function relationship of BSPs, which will be beneficial to improve the quality of polysaccharides derived from marine algae.

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Symbol : Not Applicable
Signal Word : Not Applicable
Hazard Statements : Not Applicable
Precautionary Statements : Not Applicable
Safety Data Sheet
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