Date published: 2026-5-15

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uPA Substrates

Santa Cruz Biotechnology now offers a broad range of uPA Substrates for use in various applications. uPA Substrates are pivotal in biochemical research, particularly in the study of proteolytic enzymes such as urokinase-type plasminogen activator (uPA). These substrates are specifically designed to be cleaved by uPA, a serine protease involved in the degradation of the extracellular matrix and the regulation of various cellular processes. In research settings, uPA Substrates are invaluable for investigating enzyme kinetics, substrate specificity, and the mechanisms of enzyme inhibition. They are also used in assays to quantify uPA activity, which is critical for understanding processes such as cell migration, tissue remodeling, and signal transduction. The specificity and sensitivity of uPA Substrates make them ideal tools for explaining the role of uPA in physiological and pathological conditions. Researchers use these substrates to develop and validate experimental models, enhance our understanding of enzymatic pathways, and explore the regulatory mechanisms of protease activity. The versatility of uPA Substrates extends to various fields, including biochemistry, cell biology, and molecular biology, where they contribute to the advancement of scientific knowledge and the development of new technologies. View detailed information on our available uPA Substrates by clicking on the product name.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

N-CBZ-Glycyl-glycyl-L-arginine 7-amido-4-methylcoumarin hydrochloride

102601-58-1sc-208012
sc-208012C
sc-208012A
sc-208012D
sc-208012B
2 mg
5 mg
10 mg
25 mg
50 mg
$131.00
$214.00
$339.00
$682.00
$1151.00
(0)

N-CBZ-Glycyl-glycyl-L-arginine 7-amido-4-methylcoumarin hydrochloride functions as a uPA inhibitor through its ability to form hydrogen bonds and hydrophobic interactions with the enzyme's active site. This compound's unique coumarin moiety enhances fluorescence, allowing for real-time monitoring of enzyme activity. Its structural flexibility contributes to varied binding affinities, influencing reaction kinetics and modulating proteolytic processes in distinct biochemical environments.