Recombinant Human UBE2K protein

UBE2K, also known as ubiquitin-conjugating enzyme E2K, is a member of the E2 enzyme family involved in the ubiquitin-proteasome system (UPS), a critical pathway for targeted protein degradation in eukaryotic cells. It plays a role in transferring ubiquitin molecules to specific substrate proteins, marking them for proteasomal destruction. UBE2K functions in conjunction with E3 ubiquitin ligases, which provide substrate specificity, and is particularly associated with the ubiquitination of misfolded or damaged proteins in endoplasmic reticulum-associated degradation (ERAD) and stress response pathways. Dysregulation of UBE2K activity has been implicated in neurodegenerative diseases, cancer, and other disorders linked to protein homeostasis.

Recombinant UBE2K protein is produced using biotechnological methods, typically by expressing the cloned *UBE2K* gene in bacterial (e.g., *E. coli*) or mammalian cell systems. The recombinant form retains the enzyme’s catalytic core structure, including the conserved cysteine residue required for ubiquitin-thioester intermediate formation. Purification often involves affinity tags (e.g., His-tag) for ease of isolation. Researchers use recombinant UBE2K to study ubiquitination mechanisms, screen modulators of UPS activity, or investigate its interactions with E3 ligases and substrates in vitro. Its applications extend to drug discovery, particularly in targeting diseases caused by aberrant protein aggregation. Structural and functional studies of recombinant UBE2K have also clarified its role in mediating Lys48-linked polyubiquitin chains, which signal proteasomal degradation. However, challenges remain in maintaining its stability and activity during experimental workflows, necessitating optimized buffer conditions. Overall, recombinant UBE2K serves as a vital tool for decoding UPS-related cellular processes and developing therapeutic strategies.