| Description | Product Descriptionalpha-L-fucoside fucohydrolase, alpha-L-fucosidase, alpha-(1-6) fucosidaseRemoves non-reducing, terminal branched fucose when linked alpha-(1-6) to the core GlcNAc of a GlcNAc-GlcNAc disaccharide structure that has been labeled with a fluorescent molecule. To date, the fluorescentProduct Descriptionalpha-L-fucoside fucohydrolase, alpha-L-fucosidase, alpha-(1-6) fucosidaseRemoves non-reducing, terminal branched fucose when linked alpha-(1-6) to the core GlcNAc of a GlcNAc-GlcNAc disaccharide structure that has been labeled with a fluorescent molecule. To date, the fluorescent labels ANTS, ANDSA and 2-AA have been demonstrated to function with the fucosidase.There is no cleavage of unlabeled oligosaccharides.The one exception is that a terminal unbranched α(1-3) or α(1-4) fucose is cleaved in the absence of any reporter molecule.α(1-6) Fucosidase is useful for determining core fucosylation.ContentsAlpha-(1-6) fucosidase in 20 mM Tris-HCl, 25 mM NaCl,(pH 7.5).Included with 20 µL and 60 µL pack sizes:200 µl 5x Reaction Buffer 5.0 (250 mM sodium phosphate, pH 5.0)Molecular weight~55,000 daltonsFormulationThe enzyme is provided as a sterile-filtered solution in 20 mM Tris-HCl, 25 mM NaCl pH 7.5.Suggested usage1. Add up to 1 nmole of labeled oligosaccharide to a tube.2. Add de-ionized water to a total of 15 µl.3. Add 4 µl of 5x Reaction Buffer 5.0.4. Add 1 µl of Alpha-(1-6)-Fucosidase.5. Incubate for 3 hours at 37˚C.Specificityα(1-6) linked core fucose when covalently attached to a reporter molecule at the reducing terminal GlcNAc. The one exception is that a terminal unbranched α(1-3) ) or α(1-4) fucose is cleaved in the absence of any reporter molecule. Reporter molecules known to support cleavage are amino-napthalene disulfonic and tri- sulfonic acids and 2-aminobenzoic acid(2AA). However, 2-aminobenzamide(2-AB)will not support cleavage. Shorter oligosaccharides such as trimannosylchitobiose are more completely digested than longer derivatives which may require longer incubation times.Specific Activity AssayOne unit of Fucosidase activity is defined as the amount of enzyme required to cleave 1 µmole of fucose from 4-methylumbelliferyl-alpha-L-fucoside in 1 minute at 37˚C and pH 5.0.PurityEach lot of α(1-6) Fucosidase is tested for contaminating protease as follows: 10µg of denatured BSA is incubated for 24 hours with 2 µL of enzyme. Analysis of the BSA band after SDS-PAGE should show no evidence of degradation.The production host strain has been extensively tested and does not produce any detectable glycosidases.Stability Stable at least 12 months when stored properly. Several days exposure to ambient temperatures will not reduce activity... Read More | Purity≥95%, HPLC&SDS-PAGEFunctionSerum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in Purity≥95%, HPLC&SDS-PAGEFunctionSerum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc... Read More | Inquire | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Epitope tagging offers an easy and universalPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.Epitope tagging offers an easy and universal strategy for the identification and purification of proteins derived by recombinant DNA technology. The insertion of a Maltose Binding Protein (MBP) tag creates a stable fusion product that does not interfere with the bioactivity of the protein or with the biodistribution of the MBP tagged product... Read More | BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L,BackgroundStreptavidin is a tetrameric bacterial protein isolated from Streptomyces avidinii providing 4 high-affinity biotin binding sites. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin. With a dissociation constant on the order of ≈10⁻¹⁴ mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Unlike egg-white avidin, which has a net positive charge at neutral pH and contains about 7% carbohydrate, streptavidin has almost no net charge at neutral pH, does not contain carbohydrate, and exhibits lower non-specific background. Streptavidin conjugates are widely used together with a conjugate of biotin for specific detection of a variety of proteins, protein motifs, nucleic acids and other molecules. This FITC-streptavidin conjugate was prepared by highly purified Streptavidin and free FITC was removed. Streptavidin (FITC) is a useful second-step reagent for the indirect immunofluorescent staining of cells in combination with biotinylated primary antibodies for flow cytometric analysis. Excitation at 488nm light leads to a fluorescence emission maximum of 520 nm.Recommended Usage：Every lot of Streptavidin-FITC is tested by flow cytometry using biotinylated primary antibodies. From this testing it is recommended that between 0.02 and 0.25 µg of streptavidin be used per 106 cells in a 100 µl staining volume... Read More |