Rabbit anti-Human PSMD12 Polyclonal Antibody

Uniprot Id

O00232

Target Species

Human

Target Name

PSMD12

Target Full Name

26S proteasome non-ATPase regulatory subunit 12

Target Function

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.

Target Involvement

Stankiewicz-Isidor syndrome (STISS)

Target Protein Families

Proteasome subunit p55 family

Target Synonyms

26S proteasome non-ATPase regulatory subunit 12; 26S proteasome regulatory subunit p55; 26S proteasome regulatory subunit RPN5; MGC75406; p55; proteasome (prosome, macropain) 26S subunit, non ATPase12; Proteasome 26S non ATPase subunit 12 isoform 2; PSD12_HUMAN; PSMD12; Rpn5

Target Background

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 different isoforms have been found for this gene.