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VHL Complex, Active, Recombinant, Human (VCB-Cul2 complex, ECV complex, CBCVHL)

VHL Complex, Active, Recombinant, Human (VCB-Cul2 complex, ECV complex, CBCVHL)

Cat no: 029641

Supplier: United States Biological
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The 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. The primary function of the VHL complex is to regulate HIF (hypoxia inducible factor) activity by targeting the hydroxylated HIF-1a subunit for ubiquitination and rapid proteasomal degradation 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. Source: Recombinant corresponding to aa54-end from human VHL, fused to GST-tag at N-terminus, human Elongin C, GST-tag at N-terminus, human Elongin B, human Cul2, fused to 6His tagged at N-terminal, and human Rbx1, co-expressed by baculovirus in Sf21 insect cells. Molecular Weight: VHL: ~45kD, Elongin C: ~40kD, Elongin B: ~13kD, Cul2: ~91kD, Rbx1: ~12kD Storage and Stability: Aliquot to avoid repeated freezing and thawing and store at -70 degrees C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Catalogue number: 029641
Size: 10ug
Form: Supplied as a liquid in 50mM Tris/HCl pH7.5, 150mM sodium chloride, 0.1mM EGTA, 0.03% Brij-35, 270mM sucrose, 1mM benzamidine, 0.2mM PMSF, 0.1% 2- mercaptoethanol.
Purity: ~86% (SDS-PAGE, Coomassie blue staining)
References: 1. Tanimoto K. et al., Mechanism of Regulation of the Hypoxia-Inducible Factor-1 alpha by the von Hippel-Lindau Tumor Suppressor Protein. EMBO J. 19: 4298-4309, 2000. 2. Stebbins C. E. et al., Structure of the VHL-ElonginC-ElonginB Complex: Implications for VHL Tumor Suppressor Function. Science, 284: 455-461, 1999. 3. Tyers M. and Rottapel R. VHL: A Very Hip Ligase. PNAS, 96: 12230

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