Recombinant UB2V1 protein (His tag)

• DataSheet
• Material Safety Data Sheets (MSDS)

Recombinant Human Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) fragment (amino acids 2-147) is a high-purity protein designed for studying Lys-63-linked polyubiquitination and its critical roles in NF-kappa-B activation, DNA repair, and immune signaling pathways. This fragment fully encompasses the UBC core domains, making it an ideal reagent for functional assays and mechanistic investigations.

Ubiquitin-conjugating enzyme E2 variant 1 (UEV-1), encoded by the UBE2V1 gene, lacks intrinsic ubiquitin ligase activity but forms a heterodimer with UBE2N to catalyze Lys-63-linked polyubiquitination—a key regulatory mechanism that activates IKK and NF-kappa-B without targeting proteins for proteasomal degradation. It mediates cellular responses to cytokines (e.g., IL1B, TNF), supports error-free DNA repair, and promotes antiviral signaling through RIG-I activation and TRIM5-mediated restriction. UEV-1 also contributes to cell cycle progression and differentiation. The protein is primarily localized in the nucleus, though excluded from the nucleolus, underscoring its involvement in nuclear signaling and transcriptional regulation.