Date published: 2026-1-9

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LYZL Substrates

Santa Cruz Biotechnology now offers a broad range of LYZL Substrates for use in various applications. LYZL, or lysozyme-like proteins, are enzymes known for their ability to break down bacterial cell walls, playing a crucial role in innate immunity and microbial defense. LYZL Substrates are vital tools in scientific research for studying the enzymatic activity and functional roles of lysozyme-like proteins in various biological contexts. These substrates allow researchers to investigate the mechanisms through which LYZL enzymes contribute to cell wall degradation and how they are regulated within cells. By utilizing LYZL Substrates in enzyme activity assays, scientists can measure the kinetics of LYZL action and explore the structural and functional properties of these proteins. This research is important for understanding the broader implications of LYZL activity in immune response, microbial interactions, and cellular homeostasis. Furthermore, LYZL Substrates are employed in high-throughput screening assays to identify new modulators of lysozyme-like activity, aiding in the discovery of novel pathways and regulatory mechanisms. This research enhances our understanding of microbial defense strategies and their integration into cellular physiology. View detailed information on our available LYZL Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

4-Nitrophenyl β-D-N,N′,N′′-triacetylchitotriose

7699-38-9sc-220973
sc-220973A
1 mg
5 mg
$203.00
$676.00
1
(0)

4-Nitrophenyl β-D-N,N',N''-triacetylchitotriose exhibits unique molecular interactions that enhance its role as a LYZL. Its structure facilitates specific hydrogen bonding and hydrophobic interactions, promoting selective binding to target substrates. The compound's distinct steric configuration influences enzymatic reaction pathways, resulting in altered kinetics and enhanced substrate specificity. This behavior underscores its potential in modulating biochemical processes through intricate molecular dynamics.