Agilent, GKX-5012, β(1-4,6)-Galactosidase (jack bean)

β(1-4,6)-Galactosidase (jack bean). Enzyme hydrolyses nonreducing terminal Galβ(1-6)GlcNAc and Galβ(1-4)GlcNAc. Galβ(1-3)GlcNAc is hydrolyzed slowly. The relative rates of hydrolysis are: β(1-6), 100%; β(1-4) 75%; and β(1-3), 1%. Galβ(1-6) and Galβ(1-3) can also be released from other aglycones although the rates of hydrolysis are variable. Includes 5x reaction buffer [250 mM sodium citrate phosphate (pH 3.5)]

Specifications:
Enzyme Applications: The enzyme has been extensively used for the study of isolated glycans, glycolipids and glycoproteins.
Enzyme Formulation: Lyophilized from 20 mM sodium citrate/phosphate pH 6.0.
Enzyme Source: Jack bean.
Enzyme Specificity: Galβ(1-3)GlcNAc is hydrolyzed slowly. The relative rates of hydrolysis are: β(1-6), 100%; β(1-4) 75%; and β(1-3), 1%. Galβ(1-6) and Galβ(1-3) can also be released from other aglycones although the rates of hydrolysis are variable.
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 3.5 and 37°C.
Molecular Weight: ~75 kDa
Unit: 5 U
pH Range: 3.5-4.5

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This highly purified β(1-4,6)-Galactosidase is derived from jack bean, offering precise and efficient hydrolysis of β-1,4 and β-1,6 galactosidic linkages in complex carbohydrates. Designed for advanced glycoprotein and oligosaccharide analysis, this enzyme enables detailed structural elucidation of glycan branching, crucial for characterizing biotherapeutics, diagnosing glycosylation disorders, and supporting insightful academic research in glycobiology. Optimized for robust performance across various buffer conditions, it ensures compatibility with HPLC, UHPLC, and mass spectrometry workflows, including Agilent’s acclaimed LC-MS systems. This reagent can be employed in qualitative or quantitative assays for glycan profiling, enzymatic deglycosylation experiments, and functional carbohydrate analysis in bioprocess development. Its specificity makes it ideal for mapping N- and O-linked glycan structures when used in combination with other exoglycosidases, such as sialidases, mannosidases, and fucosidases, available from Agilent’s glycan analysis product portfolio. Each lot is quality controlled for consistent activity, providing reliable results for high-throughput laboratory environments. The product is supplied as a lyophilized powder for convenient storage and reconstitution, making it a valuable tool for analytical, clinical, and biopharmaceutical laboratories focused on carbohydrate research.