Catalog number: SBB-PP0005, 50 μg
Highly active protein complex that has been purified from human red blood cells (RBC). The Human 20S proteasome is able to proteolytically degrade substrates in an ATP-independent manner. The 20S core can be activated chemically with SDS (0.035%) or by the addition of PA28. Initial experiments should be carried out at 20S proteasome concentrations between 2-5 nM.
20S Proteasome, human RBC
The ubiquitin-proteasome pathway is the major proteolytic system in eukaryotic cells, where it catalyzes the selective degradation of short-lived regulatory proteins or the rapid turnover of misfolded proteins. One of the most important proteases in this pathway is the 26S proteasome, an ATP-dependent proteolytic complex, which is formed by the association of the barrel-shaped 20S proteasome (700-kDa) and two 19S (700-kDa) regulatory complexes. The 20S catalytic core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 20S catalytic core is able to degrade a variety of peptide substrates and poly-ubiquitinated proteins involved with apoptosis, DNA repair, endocytosis, and cell cycle control. The 20S proteasome can be activated chemically by the addition of the detergent SDS at a concentration not exceeding 0.035% or by the proteinaceous activator PA28.