4-nitrophenyl-beta-d-fucopyranoside structure 
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        Common Name | 4-nitrophenyl-beta-d-fucopyranoside | ||
|---|---|---|---|---|
| CAS Number | 1226-39-7 | Molecular Weight | 285.25000 | |
| Density | 1.503g/cm3 | Boiling Point | 515.4ºC at 760 mmHg | |
| Molecular Formula | C12H15NO7 | Melting Point | 191-192ºC | |
| MSDS | Chinese USA | Flash Point | 265.5ºC | |
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                        The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa.
                        
                        
                         Environ. Microbiol. 8(6) , 1095-104, (2006) LecA (PA-IL) is a cytotoxic lectin and adhesin produced by Pseudomonas aeruginosa which binds hydrophobic galactosides with high specificity and affinity. By using a lecA-egfp translation fusion and immunoblot analysis of the biofilm extracellular matrix, we ...  | 
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                        AtFXG1, an Arabidopsis gene encoding alpha-L-fucosidase active against fucosylated xyloglucan oligosaccharides.
                        
                        
                         Plant Physiol. 128(1) , 247-55, (2002) An alpha-L-fucosidase (EC 3.2.1.51) able to release the t-fucosyl residue from the side chain of xyloglucan oligosaccharides has been detected in the leaves of Arabidopsis plants. Moreover, an alpha-L-fucosidase with similar substrate specificity was purified...  | 
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                        Regioselective synthesis of alpha-L-fucosyl-containing disaccharides by use of alpha-L-fucosidases of various origins.
                        
                        
                         Carbohydr. Res. 224 , 291-9, (1992) 
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                        Pooling for improved screening of combinatorial libraries for directed evolution.
                        
                        
                         Biotechnol. Prog. 22(4) , 961-7, (2006) Following diversity generation in combinatorial protein engineering, a significant amount of effort is expended in screening the library for improved variants. Pooling, or combining multiple cells into the same assay well when screening, is a means to increas...  | 
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                        Colorimetric assay for free and bound L-fucose.
                        
                        
                         Anal. Biochem. 177(1) , 172-7, (1989) A novel, rapid, and reliable colorimetric method for measuring L-fucose has been developed. This method utilizes NADH formed from the interaction of L-fucose with fucose dehydrogenase and NAD to generate color in a reaction involving CuSO4 and neocuproine. NA...  | 
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                        Cytotoxicity and enzymatic activity inhibition in cell lines treated with novel iminosugar derivatives.
                        
                        
                         Glycoconj. J. 27(2) , 277-85, (2010) Iminosugars are monosaccharide analogues that have been demonstrated to be specific inhibitors for glycosidases and are currently used therapeutically in several human disorders. N-alkylated derivatives of D-fagomine and (2R,3S,4R,5S)-2-(hydroxymethyl)-5-meth...  | 
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                        Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant.
                        
                        
                         Biochemistry 42(32) , 9525-31, (2003) We have recently reported that a functional alpha-L-fucosidase could be expressed by a single insertional mutation in the region of overlap between the ORFs SSO11867 and SSO3060 of the hyperthermophilic Archaeon Sulfolobus solfataricus [Cobucci-Ponzano et al....  | 
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                        Purification and characterization of alpha-L-fucosidases from Streptomyces sp. OH11242.
                        
                        
                         Comp. Biochem. Physiol. B Biochem. Mol. Biol. 130(3) , 375-83, (2001) alpha-L-Fucosidases were found in the culture fluid of Streptomyces sp. OH11242 grown with porcine gastric mucin (PGM) as the sole carbon source. The alpha-L-fucosidases were purified by ammonium sulfate precipitation followed by chromatography on Sepharose C...  | 
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                        Characterization of the interdependency between residues that bind the substrate in a beta-glycosidase.
                        
                        
                         Braz. J. Med. Biol. Res. 43(1) , 8-12, (2010) The manner by which effects of simultaneous mutations combine to change enzymatic activity is not easily predictable because these effects are not always additive in a linear manner. Hence, the characterization of the effects of simultaneous mutations of amin...  |