23-044-M
VHL Protein Complex, Active, 10 µg
Active complex of five (5) recombinant human enzymes: VHL amino acids 54-end, full length Elongin C, full length Elongin B, full length Cul2, & full length Rbx1. For use in Enzyme Assays. Functions as an E3 ligase in ubiquitination assays.
Synonym(s):
VCB-Cul2 complex, ECV complex, CBC VHL
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About This Item
UNSPSC Code:
12352202
eCl@ss:
32160405
NACRES:
NA.41
Recommended Products
biological source
human
Quality Level
recombinant
expressed in Sf21 cells
form
liquid
manufacturer/tradename
Upstate®
technique(s)
activity assay: suitable
solubility
water: soluble
NCBI accession no.
Gene Information
human ... Cul2(8453) , Rbx1(9978) , VHL(7428)
General description
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.
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.
Application
Ubiquitination Cascade Comoponent: E3
Biochem/physiol Actions
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.
Physical form
Purified using glutathione sepharose.
Other Notes
For Specific Activity data, refer to the Certificate of Analysis for individual lots of this enzyme.
Legal Information
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Volker H Haase
Current pharmaceutical design, 15(33), 3895-3903 (2009-08-13)
Hypoxia-Inducible Factors (HIFs) are heterodimeric oxygen-sensitive basic helix-loop-helix transcription factors that play central roles in cellular adaptation to low oxygen environments. The von-Hippel Lindau tumor suppressor (pVHL) is the substrate recognition component of an E3 ubiquitin ligase and functions as
Sang Bae Lee et al.
Molecular cell, 79(3), 376-389 (2020-07-09)
Activation of dual-specificity tyrosine-phosphorylation-regulated kinases 1A and 1B (DYRK1A and DYRK1B) requires prolyl hydroxylation by PHD1 prolyl hydroxylase. Prolyl hydroxylation of DYRK1 initiates a cascade of events leading to the release of molecular constraints on von Hippel-Lindau (VHL) ubiquitin ligase
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