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Human PSME2 / PA28b Protein (His Tag)

PA28B,PA28beta,REGbeta

Catalog Number P14640-H07E
Organism Species Human
Host E. coli
Synonyms PA28B,PA28beta,REGbeta
Molecular Weight 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.
predicted N His
SDS-PAGE
Purity > 90 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the human PSME2 (Met1-Tyr239) was expressed with a polyhistidine tag at the N-terminus.
Bio-activity
Research Area Epigenetics |Cell cycle |other in cell cycle |Ubiquitin-Proteasome Pathway |Proteasome
Formulation Lyophilized from sterile 50mM Tris, 100mM NaCl, 10% Glycerol, 1mM DTT, pH 8.0.
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background 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.
Reference
  • Ahn K. et al., 1996, J Biol Chem. 271 (30): 18237-42.
  • Rual Jean-François. et al., 2005, Nature. 437 (7062): 1173-8.
  • Ahn JY. et al., 1995, FEBS Lett. 366 (1): 37-42.