Date published: 2026-5-25

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KLK1 Substrates

Santa Cruz Biotechnology now offers a broad range of KLK1 Substrates for use in various applications. Kallikrein-1 (KLK1) is a member of the kallikrein family of serine proteases, known for its role in the kinin-kallikrein system, where it is responsible for the cleavage of kininogens to release kinins, such as bradykinin. These peptides play a crucial role in processes like vasodilation, blood pressure regulation, inflammation, and pain signaling. KLK1 Substrates are essential tools in scientific research, allowing researchers to study the enzymatic activity of KLK1 and its involvement in various physiological and pathological processes. By utilizing these substrates, scientists can explore how KLK1 activity influences the generation of bioactive peptides, contributing to our understanding of cardiovascular function, inflammatory responses, and tissue remodeling. These substrates are widely used in biochemical assays to quantify KLK1 activity, as well as in studies investigating the role of KLK1 in conditions such as hypertension, chronic inflammation, and certain cancers. Additionally, KLK1 Substrates are valuable in the development of inhibitors and modulators of KLK1, which are of interest for applications aimed at regulating kinin release and its effects. The availability of these substrates has significantly advanced research in fields such as cardiovascular biology, oncology, and inflammation, providing critical insights into the complex mechanisms mediated by KLK1. View detailed information on our available KLK1 Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

H-D-Val-Leu-Arg-AFC

sc-391026
sc-391026A
1 mg
5 mg
$177.00
$640.00
1
(0)

H-D-Val-Leu-Arg-AFC serves as a substrate for the enzyme klk1, showcasing its specificity through unique peptide interactions. The compound's structure facilitates enzyme recognition, leading to efficient cleavage and fluorescence emission upon hydrolysis. This reaction kinetics highlights its role in monitoring proteolytic activity, as the release of AFC generates a measurable signal. Its distinct amino acid sequence enhances selectivity, making it a valuable tool for studying protease dynamics.