PSMD8 Rabbit Polyclonal Antibody (HA500408)

UNIPROT #

P48556

PROTEIN NAME

PSMD8

SYNONYMS

26S proteasome non ATPase regulatory subunit 8 antibody;26S proteasome non-ATPase regulatory subunit 8 antibody;26S proteasome regulatory subunit p31 antibody;26S proteasome regulatory subunit RPN12 antibody;26S proteasome regulatory subunit S14 antibody;AAV38494 antibody;HIP6 antibody;HYPF antibody;MGC1660 antibody;Nin1p antibody;P31 antibody;Proteasome (prosome macropain) 26S subunit non ATPase 8 antibody;PSMD8 antibody;PSMD8_HUMAN antibody;Rpn12 antibody;S14 antibody

SUBCELLULAR LOCATION

Cytosol. Nucleus.

FUNCTION

26S proteasome non-ATPase regulatory subunit 8 is an enzyme that in humans is encoded by the PSMD8 gene. 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 1. The proteasome and its subunits are of clinical significance for at least two reasons: (1) a compromised complex assembly or a dysfunctional proteasome can be associated with the underlying pathophysiology of specific diseases, and (2) they can be exploited as drug targets for therapeutic interventions. More recently, more effort has been made to consider the proteasome for the development of novel diagnostic markers and strategies. An improved and comprehensive understanding of the pathophysiology of the proteasome should lead to clinical applications in the future.