VHL (E3X9K) Rabbit mAb #81292

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Supporting Data

REACTIVITY	H M
SENSITIVITY	Endogenous
MW (kDa)
Source/Isotype	Rabbit IgG

Application Key:

WB-Western Blotting
IHC-Immunohistochemistry

Species Cross-Reactivity Key:

H-Human
M-Mouse

Product Information

Product Usage Information

Application	Dilution
Simple Western™	1:10 - 1:50
IHC Leica Bond	1:100 - 1:400
Immunohistochemistry (Paraffin)	1:100 - 1:400

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

For a carrier free (BSA and azide free) version of this product see product #82127.

Protocol

Specificity / Sensitivity

VHL (E3X9K) Rabbit mAb recognizes endogenous levels of total VHL protein. Non-specific staining of skeletal and cardiac muscle has been observed by immunohistochemistry. This antibody is not approved for traditional western blot analysis.

Species Reactivity:

Human, Mouse

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to human VHL protein.

Background

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) (1-3). 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 proteasomal 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 (aPKC) lambda, and two subunits of the multiprotein RNA polymerase II complex (RPB1 and RPB7) (5-8). 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.

Database Links

UniProt ID: P40337

Entrez-Gene Id: 7428

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For Research Use Only. Not For Use In Diagnostic Procedures.

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