20S proteasome:
High integrity, high purity 20S proteasome complex purified from human erythrocytes. Characterised by SDS-PAGE and fluorogenic peptide substrate activity assay to determine 20S proteasome purity and chymotrypsin-like, trypsin-like and caspase-like activities. Degrades peptide substrates but not polyubiquitinated proteins (ubiquitin independent activity).
Background:
Proteasomes are non-lysosomal proteolytic complexes localised primarily in the cytoplasm and in the nucleus of eukaryotic cells. The 26S proteasome structure is composed of a 20S proteasome catalytic core complex and one or two 19S (PA700) regulatory subcomplexes (26S and 30S complexes respectively). The 20S core comprises two copies of 14 subunits (7 alpha subunits and 7 beta subunits) arranged in a
