CD BioGlyco has a professional Glycoengineering Platform with multiple world-leading technologies to help customers comprehensively promote the digestion of flexible linkers.
Designing fusion proteins composed of multiple protein domains is a very popular way of designing new protein functions. The linker not only separates the two protein domains, but its properties directly affect the functional properties of the fusion protein. The most commonly used linkers for linking protein or peptide domains are flexible linkers.
The most commonly used flexible linkers have sequences consisting primarily of stretches of glycine (Gly) and serine (Ser) residues ("GS" linker). Currently, the most widely used flexible linkers have the sequence (Gly-Gly-Gly-Gly-Ser)n. In addition to GS linkers, many other flexible linkers have emerged for recombinant fusion proteins. These flexible linkers, including KESGSVSSEQLAQFRSLD and EGKSSGSGSESKST, have been used to construct biologically active single-chain variable fragments (scFvs). The Gly and Ser residues in the linker were designed to provide flexibility, whereas glutamic acid (Glu) and lysine (Lys) were added to improve the solubility.
Flexible linkers with good flexibility and solubility are often rich in small or polar amino acids, such as Gly and Ser. Flexible linkers with this property are very useful when the fusion protein domains require certain movements or interactions (e.g. scFv).
Fig.1 Cyan-linker-yellow proteins for studying the behavior of flexible linkers. (Van, et al., 2017)
Intermediate analytical strategies provide a means to rapidly improve mass spectrometry quality. However, the new model brings new analytical challenges.
CD BioGlyco provides specific enzymes to digest flexible glycine-rich fusion protein linkers including GS and polyglycine (G) linkers. This enzyme enables the isolation of different domains of multifunctional fusion proteins to facilitate characterization and increase protein understanding. This facilitates intermediate-level analysis of fusion proteins that can both reduce overall sample complexity and enable domain-specific recognition and monitoring of post-translational modifications. Fusion proteins and various monoclonal antibody fragments containing glycine-rich linkers can be characterized in detail by intermediate methods.
CD BioGlyco provides one-stop Antibody Digestion Services and ensures the continuity and transparency of the experimental process. We will continue to improve our standards to meet customers' glycobiology research needs with high quality. If you are interested in our services, please contact us for more details without any hesitation.
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