The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S 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 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 3. Alternatively spliced transcript variants encoding
Western Blot analysis of various cells using PSMD12 Polyclonal Antibody
Western Blot analysis of HepG2 cells using PSMD12 Polyclonal Antibody
Western blot analysis of lysates from HepG2 cells, using PSMD12 Antibody. The lane on the right is blocked with the synthesized peptide.
Western blot analysis of the lysates from HT-29 cells using PSMD12 antibody.