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anti-Human PSMD5 Antibodies:
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Study in HT-29 cells and mouse colorectal tumor models revealed that levels of the proteasome assembly inhibitor PSMD5/S5B are significantly decreased in tumors, and re-expression of PSMD5 blocks 26S proteasome assembly. These results suggest that intestinal cancer cells escape proteotoxic stress by reducing PSMD5 to stimulate 26S proteasome assembly.
the critical role of S5b/PSMD5 in negative regulation of proteasome by TNF-alpha/NFkappaB and provide insights into proteasome inhibition in human disease.
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. This gene encodes a non-ATPase subunit of the 19S regulator base that functions as a chaperone protein during 26S proteasome assembly.
26S protease subunit S5 basic
, 26S proteasome non-ATPase regulatory subunit 5
, 26S proteasome subunit S5B