O-Glycoprotease, 50000u, Mass Spectra Grade

O-Glycoprotease is an immunomodulating metalloprotease (IMPa) secreted by Pseudomonas aeruginosa. It specifically cleaves at the N-terminus of serine (S) or threonine (T) residues that are O-glycosylated in glycoproteins or glycopeptides. The enzyme exhibits no preference for O-linked glycans containing or lacking sialic acids, making it suitable for broad O-glycoprotein substrate applications. It is widely used in the characterization of O-glycosylated proteins and the structural analysis of O-linked glycans.

Physical Form: 20 mM Tris-HCl (pH 7.8 at 25°C), 100 mM NaCl solution
Shelf Life: Stable for 24 months at –20°C
Optimal pH Range: Exhibits maximum activity at pH 7–8

Digestion Protocol:
· Recommended Digestion Buffer: 20 mM Tris or HEPES buffer, pH 7–8
· Sample Requirements: Non-denatured or denatured glycoprotein samples with detergents removed
· Enzyme-to-Substrate Ratio: 1:20 (w/w, protease:protein)
· Protein Concentration: 0.2–0.5 µg/µL
· Incubation Conditions: 37°C for ≥2 hours (dry bath)
· Sensitivity: O-Glycoprotease is sensitive to SDS and other detergents. The reaction buffer pH must be strictly maintained between 7 and 8 to preserve enzymatic activity.

Cleavage Sites: S, T

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