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Proteasome

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.

Cat. No.

A77319

CAS No.

1334608-28-4

Biotin-epoxomicin

Biotin-epoxomicin is a proteasome subunit binder that serves as an affinity reagent for the identification and purification of proteasomal catalytic subunits. This compound enables the affinity purification of active subunits, facilitating their subsequent analysis via liquid chromatography-mass spectrometry (LC-MS). Biotin-epoxomicin is particularly useful in research applications focused on solid tumors, such as those derived from B16 melanoma, providing insights into proteasome function in cancer biology.

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1 mg

$50.00

5 mg

$125.00

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Proteasome

Biotin-epoxomicin