The 26S proteasome is a crucial component of the ubiquitin-proteasome system (UPS), which is responsible for the degradation of most intracellular proteins. This system plays a vital role in maintaining cellular homeostasis by removing misfolded, damaged, or unneeded proteins. The 26S proteasome itself is a large, multi-subunit complex composed of a 20S core particle and two 19S regulatory particles.
The 20S core particle is a cylindrical structure composed of four stacked rings, each containing seven subunits. The two outer rings consist of alpha subunits, while the two inner rings are made up of beta subunits. The 19S regulatory particles, which cap each end of the 20S core, are responsible for recognizing ubiquitinated proteins, unfolding them, and translocating them into the core for degradation.
The 19S regulatory particle is further divided into a base and a lid. The base contains six ATPase subunits and two non-ATPase subunits, while the lid contains up to ten non-ATPase subunits. One of these non-ATPase subunits is the 26S proteasome non-ATPase regulatory subunit 11 (PSMD11), also known as Rpn6 or S9 .
PSMD11 is a critical component of the 19S regulatory particle’s lid. It plays a significant role in the assembly and stability of the 26S proteasome complex. PSMD11 is involved in the recognition and binding of ubiquitinated substrates, facilitating their translocation into the 20S core for degradation. This subunit is also phosphorylated by AMP-activated protein kinase, which may regulate its function .
The clone PAT2C7AT is a monoclonal antibody produced in mice that specifically targets the human PSMD11 protein. Monoclonal antibodies are highly specific and are produced by identical immune cells that are clones of a unique parent cell. These antibodies are widely used in research and diagnostic applications due to their specificity and consistency.
The PAT2C7AT antibody is used in various research applications to study the function and regulation of the 26S proteasome. It can be used in techniques such as Western blotting, immunoprecipitation, and immunofluorescence to detect and quantify PSMD11 in different biological samples. By using this antibody, researchers can gain insights into the role of PSMD11 in protein degradation and its implications in various diseases, including cancer and neurodegenerative disorders .