Recombinant Human UBE2H protein

UBE2H, a member of the ubiquitin-conjugating enzyme (E2) family, plays a critical role in the ubiquitin-proteasome system (UPS), a primary pathway for targeted protein degradation in eukaryotic cells. As an E2 enzyme, UBE2H facilitates the transfer of ubiquitin from E1-activating enzymes to substrate proteins, often in coordination with E3 ubiquitin ligases. This post-translational modification regulates diverse cellular processes, including cell cycle progression, DNA repair, signal transduction, and immune responses. Dysregulation of UBE2H has been implicated in neurodegenerative diseases, cancers, and developmental disorders, highlighting its biological and clinical significance.

Recombinant UBE2H protein is engineered through molecular cloning and heterologous expression systems (e.g., E. coli or mammalian cells) to study its structure, enzymatic activity, and interaction networks. Unlike endogenous UBE2H, the recombinant form is typically produced with affinity tags (e.g., His-tag, GST-tag) for simplified purification and detection. Structural studies reveal that UBE2H adopts a conserved ubiquitin-conjugating fold, with a catalytic cysteine residue essential for thioester bond formation during ubiquitin transfer. Researchers utilize recombinant UBE2H in vitro to reconstitute ubiquitination cascades, screen E3 ligase partners, and investigate substrate specificity. Its applications extend to drug discovery, particularly in developing small-molecule modulators targeting UPS components. However, challenges remain in understanding context-dependent regulation, tissue-specific isoforms, and post-translational modifications affecting UBE2H functionality. Ongoing research aims to elucidate its role in disease mechanisms and exploit recombinant UBE2H as a tool for therapeutic innovation.