Agilent, GKX-5007, α(1-3,4,6)-Galactosidase (coffee bean)

α(1-3,4,6)-Galactosidase (coffee bean). Enzyme releases nonreducing terminal α(1-3,4,6)-linked galactose from oligosaccharides. Includes 5x Reaction Buffer [500 mM sodium citrate/phosphate (pH 6.0)]
which when diluted gives 100 mM sodium citrate-phosphate pH 6.0. Specifications: Enzyme Applications: Terminal a-linked galactose residues have been reported to occur on several glycoproteins and are of increasing interest. The galactose-a-1-3Gal group is widely found in glycoconjugates from non-primate mammals and New World monkeys although it is absent from humans and Old World monkeys. The potential presence of this modification and its associated antigenicity is an important consideration in the expression of recombinant glycoproteins by mammalian cell cultures. Both a(1-3)-linked galactose and the less abundant a(1-6)-linked galactose are cleaved by this enzyme. Other workers have used the enzyme for the modification of blood group specificity. The enzyme also has diagnostic applications for the determination of raffinose in food. Enzyme Formulation: Lyophilized from 100 mM sodium phosphate pH 6.5, containing 0.25 mg/ml bovine serum albumin. See note above on BSA amount. Enzyme Source: Green coffee bean. Highly purified; β-galactosidase contaminating activity is not detectable, as determined by extended incubation with 2-AB NA2 (G2). Enzyme Specificity: Coffee bean a-galactosidase cleaves nonreducing terminal galactose residues linked a1-3, a1-4 and a1-6 to polysaccharides, glycoproteins and glycans. The precise specificity of the enzyme is dependent on the nature of the glycoconjugate.  The enzyme is stable. At 37 °C in pH 6.0 buffer, full activity is recovered after 19 hours and 70% after 48 hours.Note: The enzyme has a slow turnover. After 18 hours at 37 °C with 5 U/ml enzyme, a 40 µM solution of asialo, biantennary, fucosylated oligosaccharide with outer arm α(1-3)-galactose is 67% de-α-galactosylated. Enzyme Unit Definition: One unit is defined as the amount of enzyme required to hydrolyze 1 µmole of pNP-α-D-galactopyranoside per minute at pH 6.5 and 37oC. Molecular Weight: ~26 kD Unit: 5 U **********The following product description is generated by AI and is for reference only. If you have any questions, please contact customer service.********** α(1-3,4,6)-Galactosidase from coffee bean is a highly purified enzyme preparation designed for the selective hydrolysis of α-linked galactosyl residues. This enzyme effectively cleaves α(1-3), α(1-4), and α(1-6) galactosidic bonds, making it an essential tool for glycan structure analysis, oligosaccharide profiling, and glycoprotein characterization in both basic and advanced biochemical research. Suitable for removing galactose residues in N- and O-linked glycans, its specificity ensures accurate structural elucidation for applications in glycomics, biotechnology, and quality control processes. Optimized for laboratory workflows, this enzyme is compatible with a range of sample types including purified glycoproteins and complex biological mixtures. It integrates seamlessly with Agilent’s comprehensive glycan analysis platforms, such as HPLC and LC-MS systems, and is also suitable for use with other leading chromatography and mass spectrometry instruments. Researchers can rely on this reagent for analytical workflows including monosaccharide analysis, glycan mapping, and biomarker discovery. Related products include high-performance glycan labeling kits and a full portfolio of exoglycosidases for tailored glycan sequencing. Each batch is quality-controlled for reproducibility, ensuring consistent performance for sensitive analytical and preparative applications.