Human PSME2 / PA28b (His Tag) recombinant protein

Human PSME2 / PA28b (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

PSME2, also known as PA28b, is a subunit of proteasome. The 26S proteasome multicatalytic proteinase complex has 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. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. PSME2 gene encodes the beta subunit of the 11S regulator, one of the two 11S subunits that is induced by gamma-interferon. Three beta and three alpha subunits combine to form a heterohexameric ring.

AI788882; 11S REGULATOR COMPLEX SUBUNIT BETA; PROTEASOME ACTIVATOR HPA28 SUBUNIT BETA; PA28B; MCP ACTIVATOR; MACROPAIN) ACTIVATOR SUBUNIT 2 (PA28 BETA); PA28BETA; PROTEASOME (PROSOME; ACTIVATOR OF MULTICATALYTIC PROTEASE SUBUNIT 2; PSME2; REG-BETA; PROTEASOME ACTIVATOR 28-BETA; AA589371; CELL MIGRATION-INDUCING PROTEIN 22; PROTEASOME ACTIVATOR COMPLEX SUBUNIT 2; REGBETA; PROTEASOME ACTIVATOR 28 SUBUNIT BETA; 31-KD SUBUNIT; 11S REGULATOR COMPLEX BETA SUBUNIT

E. coli

A DNA sequence encoding the human PSME2 (Met1-Tyr239) was expressed with a polyhistidine tag at the N-terminus.

Human

The recombinant human PSME2 consists of 254 amino acids and predicts a molecular mass of 29.2 KDa. It migrates as an approximately 29 KDa band in SDS-PAGE under reducing conditions.

> 90 % as determined by SDS-PAGE