PSMB9/LMP2 (E7J1L) Rabbit mAb #87667

The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. It consists of four stacked rings, each with seven distinct subunits. The two outer layers are identical rings composed of α subunits (called PSMAs), and the two inner layers are identical rings composed of β subunits. While the catalytic sites are located on the β rings (1-3), the α subunits are important for assembly and as binding sites for regulatory proteins (4). Seven different α and ten different β proteasome genes have been identified in mammals (5). PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. PA700 binds polyubiquitin with high affinity and associates with the 20S proteasome to form the 26S proteasome, which preferentially degrades polyubiquitinated proteins (1-3). The proteasome has a broad substrate spectrum that includes cell cycle regulators, signaling molecules, tumor suppressors, and transcription factors. By controlling the degradation of these intracellular proteins, the proteasome functions in cell cycle regulation, cancer development, immune responses, protein folding, and disease progression (6-9).~Proteasome subunit β type-9 (PSMB9, LMP2) is expressed as a proenzyme that is autocleaved to form a mature immunoproteasome core particle subunit (10). Like other immunoproteasome subunits, PSMB9/LMP2 expression is induced by IFN-γ and subsequent replacement of constitutively expressed PSMB6/Y within the 20S proteasome proteolytic core particle facilitates processing and presentation of MHC class I-restricted peptide antigens on the cell surface (11-13). Research studies have shown that immunoproteasome subunits, including PSMB9/LMP2, are overexpressed in some types of human cancers and expression levels correlate with survival and improved response to immune-checkpoint blockade (14).