Date published: 2025-11-20

1-800-457-3801

SCBT Portrait Logo
Seach Input

Neuraminidase Substrates

Santa Cruz Biotechnology now offers a broad range of Neuraminidase Substrates for use in various applications. Neuraminidase enzymes play a crucial role in the removal of sialic acids from glycoproteins and glycolipids, a process that is essential in various biological and pathological contexts, including viral replication and bacterial pathogenesis. Neuraminidase Substrates are vital tools in scientific research, enabling the detailed study of enzyme activity and its implications in cellular processes. These substrates are designed to be cleaved by neuraminidases, making them indispensable for assays that measure enzyme activity, specificity, and kinetics. By utilizing Neuraminidase Substrates, researchers can explore how these enzymes contribute to the spread of viruses, such as influenza, by facilitating the release of newly formed viral particles from infected cells. Additionally, these substrates are used to study bacterial neuraminidases, which play a role in the colonization and invasion of host tissues. Beyond infectious diseases, Neuraminidase Substrates are also employed in research investigating cell signaling pathways, immune responses, and the role of sialic acid modifications in various physiological processes. The availability of these substrates has significantly advanced research in virology, microbiology, and biochemistry, providing essential insights into the enzymatic mechanisms that underlie a wide range of biological functions and their broader impact on health and disease. View detailed information on our available Neuraminidase Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

5-Bromo-4-chloro-3-indolyl α-D-N-acetylneuraminic acid sodium salt

160369-85-7sc-217158
sc-217158A
10 mg
50 mg
$256.00
$549.00
1
(1)

5-Bromo-4-chloro-3-indolyl α-D-N-acetylneuraminic acid sodium salt acts as a neuraminidase through its ability to mimic sialic acid, facilitating competitive inhibition. Its unique indole structure allows for π-π stacking interactions with aromatic residues in the enzyme, enhancing binding affinity. The presence of halogen substituents contributes to its electronic properties, influencing the transition state stabilization and altering the reaction kinetics, ultimately affecting the enzyme's catalytic profile.