N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin was used in proteasome chymotrypsin-like activity assay in Jurkat cell lysate6 and crude cell lysate of rice.7
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In the presence of chymotrypsin-like enzyme activity, the fluorophore, 7-amido-4-methylcoumarin is released from N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin. The fluorescence obtained is a measure of the enzyme activity.6
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Bottomless glass bottle. Contents are inside inserted fused cone.
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Fluorogenic substrate for chymotrypsin-like enzymes, such as cathepsin B and calpain which have been implicated in programmed cell death.
The Biochemical journal, 335 ( Pt 3), 637-642 (1998-10-31)
Oxidatively modified ferritin is selectively recognized and degraded by the 20S proteasome. Concentrations of hydrogen peroxide (H2O2) higher than 10 micromol/mg of protein are able to prevent proteolytic degradation. Exposure of the protease to high amounts of oxidants (H2O2, peroxynitrite
Proteasomes are multisubunit proteases that exist universally among eukaryotes. They have multiple proteolytic activities and are believed to have important roles in regulating cell cycle, selective intracellular proteolysis, and antigen presentation. Here we have partially purified Leishmania chagasi proteasome. The
Proteasomes are multi-subunit proteases involved in several mechanisms and thought to contribute to the regulation of cellular homeostasis. Here, we report for the first time biochemical evidence for the existence of a ubiquitin-proteasome proteolytic pathway in this parasite. Proteasomes from
The effect of the newly developed, nonpeptide, calpain inhibitor, PD 150606, on hypoxia and ionomycin-induced increases in calpain activity in rat proximal tubules (PT) was determined. PD150606 inhibited both hypoxia and ionomycin-induced calpain activity as determined by the fluorescent substrate
DISCOVER Bioactive Small Molecules for Nitric Oxide & Cell Stress Research
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