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Anti-VHL Antibody
  • Anti-VHL Antibody
Antibodies.com

Anti-VHL Antibody

Price on request

SKUPriceQuantity
A28690-100

Price on request

Description

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The Von Hippel-Lindau (VHL) tumor suppressor is the substrate-recognition subunit of an E3 ubiquitin ligase complex (with Elongin B/C, Cullin 2, and Rbx1) that targets hydroxylated hypoxia-inducible factors HIF-1α and HIF-2α for proteasomal degradation under normoxic conditions. Loss of functional pVHL is the defining molecular event in clear cell renal cell carcinoma and underlies the autosomal dominant VHL syndrome, which predisposes affected families to hemangioblastomas, pheochromocytomas, and pancreatic neuroendocrine tumors. This unconjugated rabbit polyclonal primary antibody from Antibodies.com was raised against VHL and is intended for western blot, immunohistochemistry, and immunofluorescence workflows on human, mouse, and rat samples.

The reagent ships as 100 µl of a 1 mg/ml stock formulated in PBS with 0.1% sodium azide as a preservative and 50% glycerol as a cryoprotectant, allowing convenient handling and storage at -20 °C. Because the antibody is polyclonal, the reagent recognizes multiple epitopes across the VHL protein, which can be advantageous when probing for short isoforms, N-terminal or C-terminal truncations, or partially folded variants that a single monoclonal epitope might miss. Validated reactivity across three mammalian species supports cross-species experimental designs, including paired human tumor xenograft and syngeneic mouse tissue comparisons, as well as rat model studies of renal or neural VHL pathology.

Typical uses include confirming VHL status in renal carcinoma cell lines, mapping pVHL expression patterns in fixed tissue sections, and tracking pVHL subcellular localization by immunofluorescence. Researchers can also deploy the antibody in co-immunoprecipitation experiments to pull down HIF pathway components or other pVHL-interacting partners. For best results, aliquot the stock into single-use working volumes upon first thaw to limit repeated freeze-thaw cycles and preserve binding activity across extended studies.