New Product Release: Endo S2
Endo-S2 is an endo-β-N-acetylglucosaminidase derived from Streptococcus pyogenes, which cleaves the glycosidic bond between the two innermost N-acetylglucosamine residues of N-linked glycans on glycoproteins.
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Endo-S2 is an endo-β-N-acetylglucosaminidase derived from Streptococcus pyogenes that cleaves the glycosidic bond between the two innermost N-acetylglucosamine (GlcNAc) residues in the N-linked glycans of glycoproteins. It is applicable to IgG from humans, as well as IgG antibodies from mice, rats, monkeys, goats, sheep, cows, and horses. Endo-S2 exhibits broad substrate specificity, effectively acting on the three major types of N-glycans: high-mannose, hybrid, and complex. Additionally, research has shown that Endo-S2 demonstrates significant activity in transglycosylation reactions.

Figure 1. Schematic Illustration of Endo-S2 Hydrolysis of Rituximab and Transglycosylation
Endo-S2 can recognize both core-fucosylated and non-fucosylated GlcNAc molecules in the Fc domain, utilizing them as acceptors for transglycosylation. Studies have demonstrated that Endo-S2 can efficiently remodel the glycosylation of rituximab and trastuzumab (Herceptin), producing homogeneous glycoforms without side reactions (Figure 2). As a result, it is widely applicable for structural and functional studies of antibodies with uniform glycoforms, as well as for the development of more effective antibody-based therapies.

Figure 2. Specificity of Endo-S2 Toward Monoclonal Antibodies with Different Glycans
Product Information
Purity: >95%
Activity: 200 U/μl
Tag: His-Tag
Storage Conditions: -25 to -15 °C for 24 months

Figure 3. Results of Endo-S2 Treatment on Human IgG
M marker
Lan1 human IgG 5μg
Lan2 human IgG 5μg+20 U Endo S2
Lan3 human IgG 5μg+10 U Endo S2
Lan4 human IgG 5μg+5 U Endo S2
Lan5 human IgG 5μg+2.5 U Endo S2
Lan6 human IgG 5μg+1 U Endo S2
Lan7 human IgG 5μg+0.5 U Endo S2
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1. Li T, Tong X, Yang Q, Giddens JP, Wang LX. Glycosynthase Mutants of Endoglycosidase S2 Show Potent Transglycosylation Activity and Remarkably Relaxed Substrate Specificity for Antibody Glycosylation Remodeling. J Biol Chem. 2016 Aug 5;291(32):16508-18.












