Highly specific digestion of IgA, with no activity on IgG or IgM, enabling targeted middle-level characterization of IgA1 and IgA2 subclasses.
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Highly specific arginine-specific protease with limited off-target digestion, enabling clean peptide maps and high-confidence LC-MS data analysis.
Above-hinge digesiton of human IgG antibodies and Fc-fusion proteins, enabling robust characterization of engineered and hinge-mutated biotherapeutics.
Simple and direct O-glycan site identification by site-specific digestion, generating fragments which can be used for high-resolution middle-level analysis.
Precise O-glycan site mapping by generating small, MS-friendly O-glycopeptides and improved confidence through overlapping sequence coverage.
Broad O-glycan substrate acceptance efficiently generating informative O-glycopeptides while retaining glycan structure information.
Combining multiple digestions for O-glycan site mapping with glycan structure analysis for complete characterization of heavily O-glycosylated proteins.
GlySERIAS Immobilized delivers a more complete digestion of linkers for precise characterization of fusion protein quality attributes.
High efficiency and peptide coverage maintained in strong denaturants, supporting analysis of highly structured and aggregation-prone proteins.
Site-specific IgM digestion under physiological conditions, producing homogeneous fragments for precise middle-level LC-MS characterization.
Site-specific digestion of human IgA2m1, generating homogeneous Fab and Fc fragments for high-resolution middle-level LC-MS characterization.
Site-specific digestion of human IgA1, generating homogeneous Fab and Fc fragments for high-resolution middle-level LC-MS characterization.
