Recombinant Human von Hippel-Lindau Protein Complex

The von Hippel–Lindau (VHL) E3 ubiquitin ligase complex is one of the most extensively studied E3 ligase systems in targeted protein degradation and a major component utilized in PROTAC (proteolysis-targeting chimera) technology. Under normoxic conditions, the VHL complex selectively recognizes hydroxylated hypoxia-inducible factor alpha (HIF-α) through the VHL substrate recognition protein, leading to ubiquitination and subsequent proteasomal degradation of HIF-α. By exploiting this natural ubiquitination pathway, VHL-binding ligands have become one of the most widely used E3 ligase recruiting elements in PROTAC design for targeted degradation of disease-associated proteins.

Elongin B (ELOB) and Elongin C (ELOC) form a stable heterodimer that functions as an essential adaptor module within the VHL E3 ubiquitin ligase complex. The ELOB/ELOC heterodimer interacts with the BC-box motif of VHL and connects the substrate recognition component to the Cullin-2/RBX1 ubiquitin ligase machinery, enabling assembly and activation of the functional E3 ligase complex. Because of its critical role in VHL complex formation and activity, the ELOB/ELOC complex is an important research reagent for studying VHL-mediated ubiquitination mechanisms and developing next-generation PROTAC degraders. The recombinant human von Hippel–Lindau (VHL) protein complex is a heterotrimeric protein complex composed of three components: VHL (residues 54–213), Elongin B (ELOB; residues 1–118), and Elongin C (ELOC; residues 17–112). This recombinant complex represents the functional substrate recognition module of the VHL E3 ubiquitin ligase system and is widely used for studying VHL-mediated ubiquitination and PROTAC-based targeted protein degradation.