Fresh savings just popped up! 25% off 3 or more products. | Start Saving >>
VHL Antibody

VHL Antibody #2738

This product is discontinued

We recommend the following alternatives

  • WB

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

This antibody detects endogenous levels of total VHL protein (isoforms 1, 2 and 3).

Species predicted to react based on 100% sequence homology:


Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino acids from the human VHL protein. Antibodies are purified by protein A and peptide affinity chromatography.

The Von Hippel-Lindau (VHL) protein is a substrate recognition component of an E3 ubiquitin ligase complex containing elongin BC (TCEB1 and TCEB2), cullin 1 (CUL1), and RING-box protein 1 (RBX1) (1,2,3). VHL protein has been shown to exist as three distinct isoforms resulting from alternatively spliced transcript variants (4). Loss of VHL protein function results in a dominantly inherited familial cancer syndrome that manifests as angiomas of the retina, hemangioblastomas of the central nervous system, renal clear-cell carcinomas, and pheochromocytomas (4). Under normoxic conditions, VHL directs the ubiquitylation and subsequent proteosomal degradation of the hypoxia inducible factor 1α (HIF-1α), maintaining very low levels of HIF-1α in the cell. Cellular exposure to hypoxic conditions, or loss of VHL protein function, results in increased HIF-1α protein levels and increased expression of HIF-induced gene products, many of which are angiogenesis factors such as vascular endothelial growth factor (VEGF). Thus, loss of VHL protein function is believed to contribute to the formation of highly vascular neoplasias (4). In addition to HIF-1α, VHL is known to regulate the ubiquitylation of several other proteins, including tat-binding protein 1 (TBP-1), the atypical protein kinase C lambda (aPKC), and two subunits of the multiprotein RNA Polymerase II complex (RPB1 and RPB7) (5,6,7,8). Interactions with elongin BC, RPB1, RPB7 and the pVHL-associated KRAB-A domain containing protein (VHLaK) suggest that VHL may also play a more direct role in transcriptional repression.

  1. Kibel, A. et al. (1995) Science 269, 1444-6.
  2. Pause, A. et al. (1997) Proc Natl Acad Sci U S A 94, 2156-61.
  3. Kamura, T. et al. (2000) Proc Natl Acad Sci U S A 97, 10430-5.
  4. Czyzyk-Krzeska, M.F. and Meller, J. (2004) Trends Mol Med 10, 146-9.
  5. Corn, P.G. et al. (2003) Nat Genet 35, 229-37.
  6. Na, X. et al. (2003) EMBO J 22, 4249-59.
  7. Kuznetsova, A.V. et al. (2003) Proc Natl Acad Sci U S A 100, 2706-11.
  8. Li, Z. et al. (2003) EMBO J 22, 1857-67.
Entrez-Gene Id
Swiss-Prot Acc.
For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

Upstream / Downstream


Explore pathways related to this product.