Low molecular mass protein 2 ; Macropain chain 7 ; Multicatalytic endopeptidase complex chain 7 ; Proteasome chain 7 ; Proteasome subunit beta-1i ; Really interesting new gene 12 protein ; LMP2 ; PSMB6i ; RING12
Categories
Elisa
Function
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB6 by PSMB9 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues.
Specificity
Natural and recombinant Human Proteasome subunit beta type-9
The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. This subunit is part of the immunoproteasome where it displaces the equivalent houskeeping subunit PSMB6. Interacts with HIV-1 TAT protein.