Date published: 2026-5-10

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Angiotensinase C Substrates

Santa Cruz Biotechnology now offers a broad range of Angiotensinase C Substrates for use in various applications. Angiotensinase C substrates are essential tools in the field of enzymology and cardiovascular research, particularly for studying the intricate processes involved in the renin-angiotensin system (RAS), a crucial regulator of blood pressure, fluid balance, and vascular function. Angiotensinase C is an enzyme responsible for the hydrolysis of angiotensin peptides, playing a key role in modulating the activity of angiotensin II and other related peptides. By providing well-characterized substrates for angiotensinase C, researchers can precisely monitor the enzyme's activity, explore its kinetic properties, and investigate its role in the broader context of RAS regulation. These substrates are indispensable in experiments aimed at understanding how angiotensinase C influences the degradation and inactivation of angiotensin peptides, thereby affecting the downstream signaling pathways that control cardiovascular homeostasis. In addition to their utility in basic research, angiotensinase C substrates are also used in high-throughput screening assays to identify potential modulators of enzyme activity, contributing to the discovery of new regulatory mechanisms within the RAS. The detailed study of angiotensinase C activity using these substrates provides critical insights into the complex interactions between enzymes and substrates in the RAS, helping to unravel the molecular basis of blood pressure regulation and vascular function. Furthermore, these substrates are valuable in structural biology studies aimed at explaining the enzyme-substrate interactions at the molecular level. View detailed information on our available Angiotensinase C Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

GP-pNA, Chromogenic Substrate

103213-34-9sc-201156
25 mg
$198.00
(1)

GP-pNA, a chromogenic substrate for Angiotensinase C, exhibits distinctive reactivity through its aromatic structure, which allows for specific interactions with the enzyme's active site. This substrate undergoes hydrolysis, resulting in a colorimetric change that can be quantitatively measured. Its unique electronic properties enhance the sensitivity of detection, while the substrate's kinetic profile reveals a rapid turnover rate, making it an effective tool for studying enzymatic activity and substrate specificity.