Render Target: STATIC
Render Timestamp: 2024-11-25T11:44:03.955Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-04-05 20:37:44.672
Product last modified at: 2024-11-16T00:30:09.211Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

VHL Antibody #68547

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 18-22
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Simple Western™ 1:10 - 1:50

    Storage

    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.

    Protocol

    Specificity / Sensitivity

    VHL Antibody recognizes endogenous levels of total VHL protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of 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.
    For Research Use Only. Not For Use In Diagnostic Procedures.
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