Von Hippel-Lindau, or VHL, is an E3 Ligase that mediates ubiquitination and proteasomal degradation of target proteins. VHL is indicated to play a large role in tumor suppression, particularly due to its interactions with HIF (hypoxia inducible factor). The VHL is typically used as the required E3 ligase in PROTAC (Proteolysis Targeting Chimera) drug design, protein degradation studies and selectivity profiling. VHL complex is a multi-subunit ubiquitin ligase constituted with VHL, Elongin B, Elongin C, Cullin-2 and Rbx1. Elongin B (ELOB) and Elongin C (ELOC) as a heterodimer binds to the BC-box motif present in SOCS- & VHL-box protein families. VHL is the substrate recognition component that brings target specificity. VHL is linked to scaffolding proteins Cullin-2/Rbx1 of the complex via adaptor protein Elongin C with Elongin B stabilizing the complex.
This VHL/CUL2/ELOB/ELOC/RBX1 complex is an active VHL-box E3 ubiquitin ligase.
This complex is demonstrated to be active as E3 ligase in enzymatic ubiquitination assays, for evaluating substrate ubiquitination and PROTAC mediated ubiquitination. Most importantly, this complex is ideal for studying PROTAC interaction with biophysical and HTRF assays for monitoring ternary complex. This complex has Flag tagged proteins suitable for pulldown assays.
|Tag||Various, see Datasheet|
|Molecular Weight||VHL: 25 kDa, CUL2: 88 kDa, ELOB: 14 kDa, ELOC: 13 kDa, Rbx1: 13 kDa|
|Quantity||10 µg, 50 µg|
|Formulation||40 mM Tris-HCL, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 20% glycerol, 3 mM DTT|
|Storage||-80°C, avoid freeze/thaw cycles|
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