Agilent, GK80085, AdvanceBio α(1-3,4,6)-Galactosidase, Recombinant

AdvanceBio α(1-3,4,6)-Galactosidase, Recombinant

Specifications:
Concentration: ≥80 U/mL
Enzyme Applications: Glycan analysis, glycan digestion, alpha gal identification
Enzyme Source: Recombinant, expressed in E. coli, from Green Coffee Bean
Enzyme Specificity: α(1-3,4,6)-Galactosidase
Enzyme Unit Definition: One unit of AdvanceBio α-Galactosidase is defined as the amount of enzyme required to catalyze the release of 1 μmol of p-nitrophenyl (pNP) from p-nitrophenyl-α-D-galactopyranoside per minute at pH 6 and 37 °C.
Storage Temp Conditions: Refrigeration required, 2-8°C
UNSPSC Code: 12352200
Volume: 62.5 µL

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AdvanceBio α(1-3,4,6)-Galactosidase, Recombinant is a highly specific enzyme designed for precise removal of alpha-linked galactose residues from complex glycoconjugates, including N-glycans, O-glycans, and glycoproteins. This recombinant galactosidase offers reliable and efficient cleavage of α(1-3), α(1-4), and α(1-6) galactosyl linkages, making it essential for structural characterization and in-depth analysis of carbohydrate moieties in biopharmaceutical research.

The enzyme is ideal for glycan profiling, quality control in therapeutic protein development, and detailed glycoprotein mapping. It facilitates streamlined workflows in laboratories focused on structural elucidation, offering consistent performance for both analytical and preparative purposes. This product is optimally compatible with Agilent AdvanceBio columns and LC-MS-based glycan analysis systems, enhancing data quality and reproducibility. It integrates seamlessly into established Agilent sample preparation protocols and is suitable for use with a range of glycan labeling kits and exoglycosidase digestion workflows. This galactosidase is a trusted reagent for scientists working in glycomics, bioprocessing, and biosimilar characterization, ensuring robust results across multiple analytical platforms and supporting comprehensive glycan structure identification with high specificity.