Date published: 2026-5-27

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POP Substrates

Santa Cruz Biotechnology now offers a broad range of POP Substrates for use in various applications. POP Substrates, or Proteolytic Oligopeptidase Substrates, are critical in the study of protease activity, enzyme kinetics, and biochemical pathways. These substrates are small peptides that are specifically designed to be cleaved by proteases, allowing researchers to measure enzymatic activity through the release of detectable fragments. The specificity of POP Substrates makes them invaluable in research settings, particularly in the study of post-translational modifications, signal transduction, and protein degradation processes. They are frequently utilized in assays to investigate the activity of serine proteases, metalloendopeptidases, and other proteolytic enzymes. This ability to monitor protease function is essential for understanding complex biological systems and mechanisms, including protein turnover, regulatory pathways, and cellular responses to environmental changes. Moreover, POP Substrates play a crucial role in the development of biochemical assays and analytical techniques, contributing to advancements in fields such as molecular biology, biochemistry, and biotechnology. These substrates are available in various forms, including fluorogenic, chromogenic, and luminescent versions, each offering distinct advantages for sensitivity and detection in diverse experimental setups. By enabling precise and reliable measurement of protease activity, POP Substrates support a wide range of research initiatives, from fundamental studies to applied science projects. View detailed information on our available POP Substrates by clicking on the product name.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

GP-AMC, Fluorogenic Substrate

115035-46-6sc-201157
5 mg
$133.00
(0)

GP-AMC, a fluorogenic substrate, exhibits remarkable specificity in its interactions with proteases, leading to enhanced fluorescence upon cleavage. This substrate undergoes rapid hydrolysis, resulting in a significant increase in signal intensity, which is directly proportional to enzyme activity. Its unique structural features facilitate selective binding, allowing for precise monitoring of proteolytic activity in various biological contexts. The compound's stability and reactivity make it an effective tool for studying enzyme kinetics and dynamics.