Enzyme for Hydrolyzing Terminal Sialic Acids on Glycans

Sialic acids are terminal monosaccharides that are predominantly located at the ends of glycans in biological systems and play important roles in determining the physicochemical properties of glycans as well as mediating cell–cell interactions. Through their involvement in molecular recognition and the masking of cell surface molecules, sialic acids are known to participate in a wide range of physiological and pathological processes. Sialidase (neuraminidase) is an exoglycosidic enzyme that specifically hydrolyzes and removes sialic acids from the termini of glycans. The removal of sialic acids alters glycan structure and function, which can in turn affect cellular recognition, molecular interactions, and even disease progression. Accordingly, sialidase is widely used in various research fields, including glycan biology, cancer research, and studies on viral infection mechanisms.¹⁾

1 is a sialidase with broad specificity toward α2-3, α2-6, and α2-8 linked sialic acids and acts on a wide variety of glycan structures regardless of linkage type. It is therefore suitable for evaluating glycan modifications, analyzing disease-associated glycoforms, and investigating cell surface glycan functions across diverse experimental systems.^2,3) In addition, 1 is supplied as a frozen solution and is ready for immediate use after thawing.

References

• 1) Biological function of sialic acid and sialylation in human health and disease
  • W. Zhu, Y. Zhou, L. Guo, Cell Death Discov. 2024, 10, 103.
• 2) Enzymatic Properties of Neuraminidases from Arthrobacter ureafaciens
  • Y. Uchida, Y. Tsukada, T. Sugimori, J. Biochem. 1979, 86, 1573.
• 3) Susceptibility of ganglioside GM1 to a new bacterial neuraminidase
  • K. Sugano, M. Saito, Y. Nagai, FEBS Lett. 1978, 89, 321.

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