Search by product name, CAS, target or catalog number. Press Down Arrow to reach product suggestions, Tab to move between links, and Escape to close suggestions.
Proteasome inhibitors block the 26S proteasome, the protease complex that degrades ubiquitin-tagged proteins. Its 20S core carries caspase-like, trypsin-like and chymotrypsin-like active sites on β subunits with an N-terminal threonine. In 1994, peptide aldehydes including MG-132 were shown to block degradation of most cell proteins. The same inhibitors prevented generation of peptides for major histocompatibility complex (MHC) class I molecules. Lactacystin, a Streptomyces metabolite, modifies the catalytic threonine of specific subunits. Later chemotypes include the boronates bortezomib and ixazomib and the epoxyketones carfilzomib and epoxomicin, which bind irreversibly. ONX-0914 prefers low molecular mass polypeptide 7 (LMP7), a subunit of the immunoproteasome.
TCH-165 is a small molecule proteasome assembly modulator that enhances the levels of the 20S proteasome. This compound facilitates 20S-mediated protein degradation, making it a valuable tool for studying protein turnover and homeostasis. TCH-165 is applicable in research involving cancer biology, neurodegenerative diseases, and cellular stress responses.
20S Proteasome Activator 1 is a potent activator of the 20S proteasome, demonstrating effective EC200 values of 0.3 μM, 0.7 μM, and 1.8 μM for trypsin-like, chymotrypsin-like, and caspase-like activities, respectively. This compound functions effectively within cellular environments, mitigating the accumulation of the pathogenic A53T mutant of α-synuclein. It is particularly useful for research in the context of neurodegenerative diseases, facilitating studies on proteostasis and related therapeutic approaches.
Immunoproteasome Activator 1 is a selective activator of the immunoproteasome that enhances the presentation of MHC-I-bound peptides by over 100-fold. This compound functions by binding to the proteasome structural subunit PSMA1, facilitating the association of the proteasome activator PA28α/β (PSME1/PSME2) with immunoproteasomes. Its significant biological activity makes it valuable for research focused on immune response modulation and antigen processing.
