Recombinant Human RPN13 protein

**Background of RPN13 Recombinant Protein**

RPN13 (Regulatory Particle Non-ATPase 13), also known as ADRM1 (Adhesion-Regulating Molecule 1), is a key component of the 26S proteasome, a large multi-subunit complex responsible for ubiquitin-dependent protein degradation in eukaryotic cells. As part of the 19S regulatory particle, RPN13 functions as a ubiquitin receptor, recognizing polyubiquitinated substrates and facilitating their translocation into the proteasome’s catalytic core (20S) for proteolysis. This process is critical for maintaining cellular homeostasis, regulating processes such as cell cycle progression, stress responses, and antigen presentation.

Structurally, RPN13 contains an N-terminal pleckstrin-like receptor for ubiquitin (Pru) domain, which binds ubiquitin chains, and a C-terminal KEKE motif-rich region that interacts with proteasome components like UCHL5 (a deubiquitinating enzyme). Its dual role in substrate recognition and deubiquitination highlights its regulatory importance. Dysregulation of RPN13 has been linked to cancers, neurodegenerative diseases, and immune disorders, making it a potential therapeutic target.

Recombinant RPN13 protein is engineered using expression systems (e.g., *E. coli*, mammalian cells) to produce purified, functional protein for research. It enables mechanistic studies of proteasome function, ubiquitin signaling, and inhibitor screening. Recent studies also explore RPN13’s role in cancer progression, as its overexpression in tumors correlates with poor prognosis and chemoresistance. Inhibitors targeting RPN13-ubiquitin interactions are under investigation for anticancer therapies.

Overall, RPN13 recombinant protein serves as a vital tool for dissecting proteasome biology and developing strategies to modulate proteostasis in disease contexts.