Agilent, GK80075, α(1-2)-Mannosidase, Recombinant

α(1-2)-Mannosidase, Recombinant

Specifications:
Concentration: 0.025 U/mL
Enzyme Applications: Glycan analysis, glycan digestion
Enzyme Formulation: Sterile-filtered solution in 10 mM sodium acetate, 250 µg/mL BSA (pH 5.0)
Enzyme Source: Recombinant, expressed in Pichia pastoris, from Aspergillus phoenicis
Enzyme Specificity: Cleaves nonreducing terminal α(1‑2)‑linkedmannose residues from complex carbohydrates and glycoproteins
Enzyme Unit Definition: One unit of AdvanceBio α(1-2)-Mannosidase is defined as theamount of enzyme required to catalyze the release of 1 μmolof mannose from methyl-2-O-α-D-mannopyranosyl-α-D-mannopyranoside per minute at pH 5.0 and 37 °C
Storage Temp Conditions: Refrigeration required, 2-8°C
UNSPSC Code: 12352200
Volume: 80 µL

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This recombinant enzyme specifically hydrolyzes terminal alpha(1-2)-linked mannose residues from the non-reducing ends of glycoproteins and oligosaccharides. By enabling precise removal of distinct mannose linkages, it is an essential tool for advanced glycan structural studies, biotherapeutic glycoprotein characterization, and glycoengineering research. The enzyme offers high specificity and reproducibility, ideal for workflows requiring detailed analysis of mannose-rich N-glycans, including mapping, sequencing, and troubleshooting glycosylation patterns in monoclonal antibodies and other proteins.

Optimized for in vitro applications, this alpha-mannosidase integrates seamlessly into glycoprofiling and analytical pipelines, supporting platforms such as mass spectrometry, HPLC, and capillary electrophoresis. It is compatible with Agilent’s glycan labeling kits, sample prep solutions, and analytical columns, enabling streamlined workflows from sample preparation to data acquisition. Carefully validated expression and purification protocols ensure batch-to-batch consistency and activity, making this enzyme a robust component for academic, clinical, and biopharmaceutical labs. Suitable for use with a wide variety of mammalian, yeast, and insect glycoproteins, it supports in-depth glycosylation analysis, biosimilar comparability studies, and development of therapeutic candidates.