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clasto-Lactacystin β-lactone, a synthetic derivative of lactahydrin, is a cell permeable, irreversible and specific inhibitor of the 20S proteasome involved in the ubiquitin-proteasome degradation pathway. Kinetic studies indicate that clasto-Lactacystin β-lactone interacts with the proteasome at its catalytic site threonines, which opens the β-lactone ring and allows the proteasome‘s catalytic hydroxyl group to become acylated. clasto-Lactacystin β-lactone has been reported to rapidly enter cells in mammalian cell culture media and to additionally inactivate the proteasome in Jurkat cells in a dose-dependent manner. In addition, clasto-Lactacystin β-lactone is reported to inhibit cathepsin A, lead to adipogenesis and induce neurite growth in rat PC12 cells.


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