Product Overview

The sequence is derived from Streptococcus pyogenes, recombinantly expressed in E. coli without any purification tag. It specifically cleaves the β(1-4) glycosidic bond between the first and second N-acetylglucosamine residues adjacent to Asp in the N-glycan chain of IgG.

One unit of activity is defined as the amount of enzyme required to remove 95% of the glycans from 5 μg of monoclonal antibody in a 10 μl reaction system within 1 hour at 37°C.

Key Features

Recombinant Expression in E. coli

Derived from Streptococcus pyogenes and recombinantly expressed in E. coli without any purification tag, minimizing interference from tag-related components in downstream applications.

High Substrate Specificity

Specifically cleaves the β (1-4) glycosidic bond between the first and second N-acetylglucosamine residues adjacent to the asparagine-linked glycan core of IgG.

High Purity

Purity is typically >95% as determined by SDS-PAGE and SEC-HPLC analysis.

Good Enzymatic Activity and Stability

Demonstrates consistent activity under recommended reaction conditions, with stable storage performance for up to 2 years.

Defined Specific Activity

Enzyme specific activity is >100 kU/mg under standard assay conditions.

Applications

Antibody Glycan Remodeling

Used for enzymatic modification of IgG Fc glycans, supporting antibody structure-function studies and glycoengineering workflows.

Antibody Conjugation and Labeling

Applicable in site-specific antibody modification strategies, including conjugation, labeling, and functionalization based on glycan remodeling.

Protein Modification and Immobilization

Suitable for controlled modification of glycoproteins, including applications involving cross-linking and immobilization in biochemical assays.

Performance Data

SDS-PAGE Purity Identification (>95%)

Product Specifications

FAQ

1. What is Endo S2 and its function in ADC development?

Endo S2 is a recombinant endoglycosidase derived from Streptococcus pyogenes, which specifically cleaves N-linked glycans at the N297 site of the antibody Fc region. It has two core applications in ADC development:

• Deglycosylation: It can specifically cleave the β(1-4) glycosidic bonds between the first and second N-acetylglucosamine residues near the Asp on the N-glycan chain of IgG, including complex-type, heterozygous and high-mannose types, etc.

• Glycan-based site-specific conjugation: Directly conjugates toxins to glycosylation sites to construct homogeneous ADCs.

Single enzyme enables both glycan cleavage and transglycosylation. However, wild-type Endo S2 is restricted by patents. Our independently developed mutant EndoS2 pro via AI design breaks patent limitations and is available for licensing to clients.

2. Recognizable glycan substrates of Endo S2

Endo S2 features broad substrate compatibility and catalyzes transglycosylation on various disaccharide structures:

The LacNAc substrate is the mainstream choice for glycan-based site-specific ADCs due to its simple synthesis and strong resistance to hydrolysis by Endo S2.