F5884
α-L-Fucosidase from bovine kidney
ammonium sulfate suspension, ≥2.0 units/mg protein (biuret)
Synonym(s):
α-L-Fucoside fucohydrolase
biological source
bovine kidney
form
ammonium sulfate suspension
specific activity
≥2.0 units/mg protein (biuret)
mol wt
210-220 kDa (Subunits: 55-60 kDa)
foreign activity
α-mannosidase and β-galactosidase ≤0.1%, β-N-acetylglucosaminidase ≤0.2%
shipped in
wet ice
storage temp.
2-8°C
General description
α-L-fucosidases is a liposomal enzyme, which belongs to glycosyl hydrolases family.
Application
α-L-fucosidase from bovine kidney has been used:
- to study their ability to alter primary cell transduction
- to examine the role of fucose residues of cell surface glycans in adhesion
- to investigate its role during fertilization
Biochem/physiol Actions
α-L-fucosidases degrades fucose-containing fucoglycoconjugates and breaks fucosidic bonds in oligosaccharides and glycoconjugates. It acts as a tumor marker for hepatic and colorectal cancer. α-L-fucosidase exhibits transglycosylation property.
Physical form
Suspension in 3.2 M (NH4)2SO4, 10 mM NaH2PO4 10 mM citrate, pH 6.0
Other Notes
One unit will hydrolyze 1.0 μmole of p-nitrophenyl α-L-fucoside to p-nitrophenol and L-fucose per min at pH 5.5 at 25°C.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
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alpha-l-Fucosidase enhances capacitation-associated events in porcine spermatozoa
Romero-Aguirregomezcorta J, et al.
The Veterinary Journal, 203(1), 109-114 (2015)
Novel alpha-l-fucosidases from a soil metagenome for production of fucosylated human milk oligosaccharides
Lezyk M, et al.
PLoS ONE, 11(1), e0147438-e0147438 (2016)
Directed evolution of the alpha-L-fucosidase from Thermotoga maritima into an alpha-L-transfucosidase
Osanjo G, et al.
Biochemistry, 46(4), 1022-1033 (2007)
Human alpha-L-fucosidase-1 attenuates the invasive properties of thyroid cancer
Vecchio G, et al.
Testing, 8(16), 27075-27075 (2017)
Markus Günl et al.
The Plant cell, 23(11), 4025-4040 (2011-11-15)
An Arabidopsis thaliana mutant with an altered structure of its hemicellulose xyloglucan (XyG; axy-8) identified by a forward genetic screen facilitating oligosaccharide mass profiling was characterized. axy8 exhibits increased XyG fucosylation and the occurrence of XyG fragments not present in
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
以硫酸铵悬浮液形式提供的酶的使用指南
Related Content
Datasheet
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