Greater than 90.0% as determined by SDS-PAGE.
Ubiquitin-conjugating enzyme E2H (UBE2H) is a crucial component of the ubiquitin-proteasome system (UPS), which is responsible for the regulated degradation of proteins within eukaryotic cells. This enzyme plays a pivotal role in various cellular processes, including protein turnover, signal transduction, and cell cycle regulation.
The ubiquitination process involves three main types of enzymes: E1 (ubiquitin-activating enzymes), E2 (ubiquitin-conjugating enzymes), and E3 (ubiquitin ligases). UBE2H belongs to the E2 family and acts as an intermediary that transfers ubiquitin from the E1 enzyme to the substrate protein, which is recognized by the E3 ligase .
UBE2H is a protein-coding gene that encodes a protein involved in the ubiquitination pathway. It has ligase activity and binds to ubiquitin protein ligases . The enzyme is essential for the conjugation of ubiquitin to target proteins, marking them for degradation by the proteasome. This process is vital for maintaining cellular homeostasis and regulating various biological processes.
Recent studies have explored the potential of UBE2H in targeted protein degradation. For instance, researchers have developed chimeric human E2 ubiquitin-conjugating enzymes that can induce the degradation of specific intracellular proteins . This approach, known as targeted protein degradation (TPD), offers a promising avenue for therapeutic interventions in various diseases.