Proteasome 20S α1,2,3,5,6,& 7 subunits, mAb (MCP231)

Based on sequence similarity, all fourteen 20S proteasomal subunit sequences may be classified into two groups, α and β, each group having distinct structural and functional roles. The α-subunits comprise the outer rings and the β-subunits the inner rings of the 20S proteasome. Observations of the eukaryotic proteasome and analysis of subunit sequences indicate that each ring contains seven different subunits (α7β7β7α7) with a member of each sub-family represented in each particle. Each subunit is located in a unique position within the α- or β-rings. 120S Proteasomes degrade only unfolded proteins in an energy-independent manner, whereas 26S proteasomes degrade native and ubiquitinylated proteins in an ATP-dependent manner. The native protein substrates are recognised by subunits, some with ATP binding sites, of the outer 19S caps of the 26S proteasome.

The hybridoma secreting the antibody to subunits HC2, HC3, HC8, HC9, Iota and Zeta was generated by fusion of spenocytes from Balb/c mice which had recieved repeated immunisation with dinitrophenylated proteasomes.