Product Description
β(1-4)-Galactosidase (streptococcus pneumoniae). Enzyme releases nonreducing terminal β(1-4)-linked galactose from oligosaccharides and glycoproteins. This specificity is only evident at enzyme concentrations < 100mU/mL. At higher concentrations, hydrolysis of β(1-3)-linked galactose occurs. Includes 5x reaction buffer B (250 mM sodium phosphate, pH 6.0).
Specifications:
Concentration: 2 U/mL
Enzyme Applications: Due to its high selectivity the enzyme is an extremely useful reagent for the identification of nonreducing terminal ß(1-4)-linked galactose residues. As such the enzyme has been extensively used for detailed structural analysis with broader specificity bovine testes ß-galactosidase (GKX-5013) or jack bean ß-galactosidase (GKX-5012).
Enzyme Formulation: 20 mM Tris-HCl, 25 mM NaCl (pH 7.5)
Enzyme Source: Streptococcus pneumoniae.
Enzyme Unit Definition: One unit is defined as the amount of enzyme required to hydrolyze 1 µmole pNP-ß-D-galactopyranoside per min at pH 6.0 and 37°C.
Molecular Weight: 220-247 kDa
Unit: 200 mU
Volume: 100 µL
pH Optimum: 6
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Agilent’s beta(1-4)-Galactosidase derived from Streptococcus pneumoniae is a high-purity enzyme ideal for precise glycoanalysis workflows. This enzyme specifically hydrolyzes terminal, non-reducing beta1-4-linked galactose residues from oligosaccharides, glycoproteins, and glycolipids. Its substrate specificity makes it a powerful tool for structural characterization and profiling of complex N- and O-glycan moieties in biopharmaceutical development, disease biomarker research, and glycobiology studies.
Optimized for compatibility with Agilent’s renowned glycan analysis platforms, this reagent integrates seamlessly with HPLC, LC-MS, and capillary electrophoresis systems for quantitative and qualitative glycan assessment. The enzyme’s robust performance enables detailed mapping of glycosylation patterns, vital for antibody characterization, therapeutic protein development, and biosimilar comparability studies. It is suited for workflows employing fluorescent or mass-based glycan labeling, facilitating in-depth analysis and high-throughput screening.
The product is supplied with detailed usage instructions, and recommended controls enhance experimental consistency and reproducibility. It pairs well with Agilent glycosidase kits, labeling reagents, and sample preparation solutions, providing a comprehensive suite for advanced glycomics research. This enzyme is an essential component for researchers seeking reliable, reproducible results in glycan structure analysis.
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Collaboration
Tony Tang
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