Agilent, GK80090, AdvanceBio O-Glycanase

AdvanceBio O-Glycanase. Enzyme releases unsubstituted Ser/Thr-linked GalGalNAc from proteins and can be used with additional enzymes to remove more complex O-linked structures. Also known as Endo-O-Glycosidase, Endo-α N-acetylgalactosaminidase, O-Glycosidase. Includes 5X reaction buffer A [250 mM sodium phosphate pH 5.0]

Specifications:
Application: Detection of O-glycosylation in proteins
Concentration: ≥1.25 U/mL
Enzyme Applications: Analysis of biosynthesis of glycoproteinsBioactivity in O-glycansDetection of O-glycosylation in proteinsEpitope and binding site analysisGlycoprotein deglycosylationStructural analysis of O-glycan
Enzyme Formulation: 20 mM Tris HCl pH 7.5 containing 25 mM NaCl.
Enzyme Source: Recombinant gene from Streptococcus pneumoniae, expressed in E.coli.
Enzyme Specific Activity: ≥12 units/mg
Enzyme Specificity: The enzyme is highly specific, liberating Galß1-3GalNAc from serine or threonine residues alone or as part of glycopeptides or glycoproteins. There is no apparent preference for serine over threonine. Substitution of the disaccharide core with sialic acid, fucose, N-acetylglucosamine or N-acetylgalactosamine residues, prevents cleavage of the Galß1-3GalNAc-Ser/Thr linkage. Absence of the galactose residue or the acetamido group on the innermost N-acetylgalactosamine residue also prevents cleavage of the Galß1-3GalNAc-Ser/Thr linkage. O-Glycanase is included in the Agilent Enzymatic Deglycosylation kit for N-linked and simple O-linked glycans (GK80110), which may be used in conjunction with our the Agilent Extender kit for complex O-linked glycans (GK80115).
Enzyme Unit Definition: One unit is defined as the amount of enzyme required to catalyze the release of 1 µmole of Galß1-3GalNAca1-p-nitrophenol per minute at 37°C, pH 5.5.
Molecular Weight: ~180 kD
Unit: 50 mU
Volume: 40 µL
pH Optimum: 5.5
pH Range: 5-7

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AdvanceBio O-Glycanase is a highly specific enzyme designed to remove O-linked glycans from glycoproteins, facilitating streamlined glycan analysis in biopharmaceutical and academic research. This reagent enables efficient and reproducible deglycosylation of O-glycosylated proteins under gentle conditions, preserving protein integrity and ensuring compatibility with both qualitative and quantitative downstream analyses. It is particularly suited for characterizing glycoprotein therapeutics, profiling glycan structures in biological samples, and supporting detailed studies of post-translational protein modifications. The enzyme is optimized for use in workflows incorporating HPLC, LC-MS, and related analytical techniques, delivering reliable results across a variety of sample types. Compatible with Agilent AdvanceBio LC columns and instrumentation, it integrates seamlessly into established workflows for glycan mapping and characterization. The high purity and performance of this enzyme reduce background activity and promote clean, interpretable data, supporting both routine glycan analysis and advanced research into glycoprotein function. Additionally, it offers an efficient alternative to labor-intensive chemical release methods, improving throughput and repeatability in glycomics laboratories. This product is an essential tool for scientists conducting detailed glycosylation studies or developing quality control protocols for biopharmaceutical products.