Effective 9/27/2022, name modified to O-Glycoprotease (IMPa)
O-Glycoprotease (IMPa) is a broad specificity protease that cleaves the peptide bonds of a glycoprotein or glycopeptide immediately N-terminal to a serine or threonine residue containing a mucin-type O-linked glycan with or without sialylation.
O-Glycoprotease (IMPa), also known as Immunomodulating protease (IMPa), is a broad specificity O-glycoprotease from Pseudomonas aeruginosa. It recognizes mucin-type O-glycans in glycoproteins or glycopeptides, including branched and sialylated structures, and cleaves the peptide bond immediately N-terminal to a glycosylated serine or threonine residue. It can be used in glycoproteomics workflows to map O-glycosylated residues and structurally profile O-glycans present at each glycosite. O-Glycoprotease (IMPa) has a 6xHis-tag for easy removal from a reaction using nickel affinity resins.
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