The 26S proteasome is an essential component of the ubiquitin-proteolytic pathway in eukaryotic cells and is responsible for the degradation of most cellular proteins. It is composed of a 20S proteasome as a catalytic core and regulatory particles at either end. The subunits of the 20S proteasome can be classified into two families, α and β. In eukaryotes, the 20S proteasome contains seven α-type subunits and seven β-type subunits. The fourteen subunits are arranged in four rings of seven and form an α7β7β7α7 structure. This antibody recognizes α2 subunit of the 20S proteasome from all organisms tested, yeast to human. The advance of this antibody is application for immuno-electron microscopy.
Figure 1. Immunoblotting of the purified 26S proteasomes
26S proteasomes were electrophoresed under denaturing conditions (12.0% gel) and stained with Coomassie Brilliant Blue (CBBR), or immunostained with antibodies (α-20S, anti-Xenopus 20S proteasome polyclonal antibody; GC3α; GC4/5; GC3β; or 1-4D5) after electroblotting. Lanes I and M indicate 26S proteasomes from immature and mature oocytes, respectively. Protein bands that cross-reacted with GC4/5 (p25), GC3β (p30 and p31) and 1-4D5 (p62) are indicated. Molecular masses of standard proteins are indicated on the left. Reference : Eur J Biochem. 2000 Jan;267(1)97-103
Figure 2. Immunoelectronmicroscopic localization of proteasome α2 subunit
Anti 20S proteasome (GC4/5)
To be used for research only. DO NOT use for human gene therapy or clinical diagnosis.