His₆-Tagged Endoglycosidase H for N-linked Glycan Removal

A Reliable Tool for Structural Biology & Protein Engineering

MinneBio Endoglycosidase H (Endo H) is a highly active recombinant glycosidase designed for precise removal of high-mannose/hybrid N-linked glycans from glycoproteins. By specifically cleaving the chitobiose core of susceptible N-glycans while leaving a single GlcNAc residue attached to the protein, Endo H enables detailed analysis of glycosylation patterns, protein maturation, and glycoprotein quality. Ideal for structural biology, biopharmaceutical research, and protein characterization workflows, MinneBio Endo H provides reliable and consistent performance for both analytical and preparative applications.

1. Upper Left Image: Purified MinneBio His₆-Tagged Endoglycosidase H (Endo H)

SDS-PAGE analysis demonstrates the high purity and consistent quality of recombinant MinneBio His₆-Tagged Endoglycosidase H (Endo H), supporting reliable performance for precise glycoprotein processing applications.

2. Upper Right Image: Efficient Cleavage of High-Mannose/Hybrid N-Linked Glycans by MinneBio His₆-Tagged Endoglycosidase H (Endo H)

Following incubation with MinneBio His₆-Tagged Endoglycosidase H for 1 hour at 37°C, RNase B was efficiently converted to RNase A, demonstrating the enzyme’s high specificity and activity under optimized cleavage conditions. This result confirms efficient removal of high-mannose/hybrid N-linked glycans while maintaining the integrity of the target protein.

3. Lower Image: Specific Recognition and Cleavage Mechanism

MinneBio His₆-Tagged Endoglycosidase H specifically recognizes and cleaves Endo H-sensitive N-linked glycans, enabling efficient deglycosylation and generation of native-like recombinant proteins for structural and functional studies.