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 one of the non-ATPase subunits of the 19S regulator lid. Pseudogenes have been identified on chromosomes 10 and 21.

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Western blotting analysis using PSMD4 antibody . Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with PSMD4 antibody and HRP-conjugated goat anti rabbit secondary antibody respectively. Image was developed using NaQ™ ECL Substrate Kit .

Western blotting analysis using PSMD4 antibody . PSMD4 expression in wild type (WT) and PSMD4 knockdown (KD) HSHC cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with PSMD4 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

Flow cytometric analysis of PSMD4 expression in HepG2 cells using PSMD4 antibody . Green, isotype control; red, PSMD4.

Immunocytochemical staining of HepG2 cells with PSMD4 antibody . Nuclei were stained blue with DAPI; PSMD4 was stained magenta with Alexa Fluor® 647. Images were taken using Leica stellaris 5. Protein abundance based on laser Intensity and smart gain: Medium. Scale bar, 20 μm.

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