Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.
UBE2N produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-152a.a.) and having a molecular mass of 19.3kDa.
UBE2N is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Ubiquitin-conjugating enzyme E2 N, Bendless-like ubiquitin-conjugating enzyme, Ubc13, Ubiquitin carrier protein N, Ubiquitin-protein ligase N, UBE2N, BLU, MGC8489, UbcH-ben, MGC131857.
Ubiquitin Conjugating Enzyme E2N (UBE2N), also known as UBC13, is a crucial component of the ubiquitination pathway, which is a post-translational modification process that regulates protein degradation and various cellular functions. UBE2N is a member of the E2 ubiquitin-conjugating enzyme family and plays a significant role in the synthesis of non-canonical ‘Lys-63’-linked polyubiquitin chains .
UBE2N, in conjunction with its co-factors UBE2V1 and UBE2V2, catalyzes the formation of ‘Lys-63’-linked polyubiquitin chains. Unlike the more common ‘Lys-48’-linked chains that target proteins for degradation by the proteasome, ‘Lys-63’-linked chains are involved in various cellular processes, including DNA repair, signal transduction, and immune response . This type of polyubiquitination does not lead to protein degradation but rather mediates transcriptional activation of target genes and plays a role in cell cycle control and differentiation .
UBE2N is essential for the error-free DNA repair pathway and contributes to cell survival following DNA damage. It is involved in the Toll-Like Receptor (TLR) signaling pathway and the homologous recombination repair (HRR) or single-strand annealing (SSA) pathways . The enzyme’s activity is crucial for maintaining genomic stability and proper cellular function.
Human recombinant UBE2N is typically produced using recombinant DNA technology. The gene encoding UBE2N is cloned into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or yeast. The host cells are cultured under conditions that promote the expression of the UBE2N protein. After expression, the protein is purified using various chromatographic techniques to obtain a highly pure and functional enzyme.
UBE2N participates in the ubiquitination process by transferring activated ubiquitin from the E1 ubiquitin-activating enzyme to the substrate protein, with the help of an E3 ubiquitin ligase. The enzyme’s activity can be analyzed using in vitro ubiquitination assays, where the formation of polyubiquitin chains is monitored. Additionally, mass spectrometry and Western blotting are commonly used to study the enzyme’s function and interaction with other proteins.
Mutations or dysregulation of UBE2N have been associated with various diseases, including certain types of cancer and neurodegenerative disorders. Understanding the enzyme’s function and regulation can provide insights into potential therapeutic targets for these conditions.