The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure 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. 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 member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. Proteolytic processing is required to generate a mature subunit. Expression of this gene is induced by gamma interferon, and this gene product replaces catalytic subunit 2 (proteasome beta 7 subunit) in the immunoproteasome.

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Western blotting analysis using PSMB10 antibody . Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with PSMB10 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

Western blotting analysis using PSMB10 antibody . PSMB10 expression in wild type (WT) and PSMB10 shRNA knockdown (KD) HeLa cells with 20 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with PSMB10 antibody and HRP-conjugated goat anti-rabbit secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

Flow cytometric analysis of PSMB10 expression in C2C12 cells using PSMB10 antibody . Green, isotype control; red, PSMB10.

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