Proteasomes are protein complexes inside all eukaryotes and archaea, and in some bacteria which main function is to degrade unneeded or damaged proteins by proteolysis. The 26S proteasome is a eukaryotic ATP-dependent protease (EC 3.4.-) that is known to collaborate with the ubiquitin system,  the system that tags proteins with polyubiquitin chains as a marker for protein degradation in eukaryotic cells that degrades ubiquitin conjugates[1]. It consists of no less than 31 principal subunits arranged into two subcomplexes, the 20S core protease (CP) and the 19S regulatory particle (RP). The CP is a broad spectrum ATP- and ubiquitin-independent protease. It is a cylindrical stack created by the assembly of four heptameric rings. The two peripheral rings are composed of seven related α-subunits and the two central rings are composed of seven related β-subunits. The subunits have active sites with various hydrolase cleavage capacities, enabling the 26S proteasome to cleave most, if not all, peptide bonds[2]. Bortezomib (Axon 1810) is a specific inhibitor of 26S proteasome activity with approved application for use in multiple myeloma[3].