Glycosylation modification plays an important role in the immunogenicity, safety and effectiveness of antibody drugs. In order to greatly shorten the preparation time of N-glycan samples and improve the detection efficiency, Creative Diagnostics have developed a kit for the rapid release and labeling of N-glycan chains in biopharmaceuticals. This kit has been validated for use with monoclonal antibodies (IgG), and a variety of N-linked glycoproteins.
Therapeutic proteins have unique advantages over small-molecule drugs in the treatment of various diseases, such as higher target specificity, stronger pharmacological efficacy and relatively low side effects. As one of the most important post-translational modifications, glycosylation has been shown to exert positive effects on many properties of proteins, including molecular stability, and pharmacodynamic and pharmacokinetic characteristics. Glycoengineering, which involves changing the glycosylation patterns of proteins, is therefore expected to be an effective means of overcoming the problems of therapeutic proteins. There are two main types of protein glycosylation: N-linked glycosylation (N-glycosylation) and O-linked glycosylation (O-glycosylation). In N-glycosylation, the glycans are covalently attached to the side-chain nitrogen (N) atoms of the Asn residues in the N-X-S/T sequons, where X is any amino acid except proline.
It is generally believed that the diverse N-glycan structures could confer different biological effects to therapeutic antibodies. These effects may be beneficial for the treatment of diseases by improving the therapeutic properties, or may adversely affect the biological functions.
This protocol was validated using monoclonal antibodies and has been tested for a variety of other N-linked glycoproteins. We recommend that users confirm the enzyme release for their specific samples.
| Cat. No. | Product Name | Price |
| DCQA-2308-1 | N-Glycan Analysis Kit | Inquiry |