Research area: Cancer

The von-Hippel Lindau tumor suppressor (VHL) complex is a multi-subunit ubiquitin ligase composed of VHL, Elongin B, Elongin C, Cul2 and Rbx1. The VHL protein serves as the substrate recognition component and is linked by Elongin C to a heterodimeric Cul2/Rbx1 module that functions as a potent activator of the ubiquitination of target proteins by an E2 conjugating enzyme. Elongin B interacts with the complex through Elongin C and appears to stabilize the binding of Elongin C to VHL.

Ubiquitination Cascade Comoponent: E3

The primary function of the von-Hippel Lindau tumor suppressor (VHL) complex is to regulate HIF (hypoxia inducible factor) activity by targeting the hydroxylated HIF-1α subunit for ubiquitination and rapid proteasomal degradation during normoxia under normoxic conditions. It therefore plays an important role in the regulation of hypoxia-inducible genes such as the vascular endothelial growth factor (VEGF) and glucose transport-1 (Glut-1). Mutations in VHL are associated with the inherited von Hippel-Lindau (VHL) cancer syndrome and numerous forms of renal cell carcinoma.

Purified using glutathione sepharose.

For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.

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