Agilent, GKX-5013, β(1-3,4)-Galactosidase (bovine testis)

β(1-3,4)-Galactosidase (bovine testis). Enzyme hydrolyzes nonreducing terminal galactose β(1-3) and β(1-4) linkages. Can be used with other β-galactosidases for exoglycosidase sequencing. Includes  5x reaction buffer (500 mM sodium citrate/phosphate pH 4.0).

Specifications:
Concentration: 5 U/mL
Enzyme Applications: The enzyme has applications in the analysis of a wide variety of glycoconjugates. It is particularly useful for ensuring the complete removal of ß(1-3) and ß(1-4)-linked non-reducing terminal galactose residues of oligosaccharides. Gal ß(1-6) GlcNAc is hydrolyzed more slowly, however this linkage is not normally encountered in native complex glycans. This activity towards ß(1-3) and ß(1-4)-linked galactose contrasts with that of our other ß-galactosidases (e.g. from S. pneumoniae, GKX-5014, or Jack bean, GKX-5012) which exhibit a preference for Gal ß(1-4), and cleave the Gal ß(1-3) linkage relatively slowly, if at all. Used in conjunction, these enzymes provide a powerful means to determine linkage positions of non-reducing ß galactose residues.
Enzyme Formulation: 20 mM sodium citrate phosphate, 150 mM NaCl (pH 4.0)
Enzyme Source: Bovine testis.
Enzyme Unit Definition: One unit is defined as the amount of enzyme required to hydrolyze 1 µmole of pNP-ß-D-galactopyranoside per minute at pH 4.0 and 37°C.
Molecular Weight: ~68 kD
Unit: 0.5 U
Volume: 100 µL
pH Optimum: 4

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Agilent’s β1-3,4-Galactosidase, sourced from bovine testis, is a high-purity enzyme designed for the selective hydrolysis of β1-3 and β1-4 linked galactosyl residues from complex carbohydrates, glycoproteins, and glycolipids. This reliable reagent supports precise characterization of carbohydrate structures in glycobiology, molecular biology, and biochemistry research. The enzyme is instrumental in the study of glycan remodeling, elucidating protein glycosylation patterns, and facilitating the analysis of glycoprotein function and metabolism. It is particularly valuable for applications involving structural analysis of N- and O-linked glycans by releasing terminal galactose residues, thus enabling accurate mass spectrometry and chromatographic profiling. The product performs efficiently under standard laboratory buffer conditions and is validated for use with Agilent’s suite of HPLC and LC-MS platforms, including glycan analysis workflow kits and sample preparation systems. This enzyme is suitable for academic, pharmaceutical, and biotechnology laboratories focused on glycomics, biomarker discovery, or therapeutic protein development. Recommendations for assay protocols, substrate compatibility, and storage conditions are included to ensure optimal activity and reproducibility, supporting advanced research in carbohydrate chemistry and glycoprotein analysis.