Recombinant VHL protein (His tag)

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This recombinant protein product features a stable and soluble fragment (residues 58-213) of the human von Hippel-Lindau disease tumor suppressor (pVHL), optimized for structural and biochemical studies. It enables researchers to investigate the critical functions of VHL in ubiquitin-mediated degradation pathways and cellular oxygen sensing.

The full-length von Hippel-Lindau disease tumor suppressor (VHL) is a key component of the E3 ubiquitin ligase complex, primarily responsible for the oxygen-dependent ubiquitination and proteasomal degradation of hypoxia-inducible factors (HIFs) under normoxic conditions. It functions as a target recruitment subunit, binding hydroxylated HIFs to regulate cellular responses to oxygen availability. Additionally, VHL participates in transcriptional repression through interactions with HIF1A, HIF1AN, and histone deacetylases, and ubiquitinates substrates such as ADRB2 and RPTOR, the latter acting as a negative regulator of mTORC1 signaling. Subcellularly, VHL localizes to the cytoplasm, nucleus, endoplasmic reticulum, and cell membrane, with isoform-specific distributions—isoform 1 is found predominantly in the cytoplasm with some nuclear or membrane association, while isoform 3 is equally distributed between the nucleus and cytoplasm. These roles underscore VHL's importance in tumor suppression, cellular metabolism, and hypoxia adaptation.