CST, 53324P, VHL (E3X9K) Rabbit Monoclonal Antibody (Biotinylated)

Monoclonal Antibody for studying VHL. Validated for Peptide ELISA (DELFIA). Highly specific and rigorously validated in-house, VHL (E3X9K) Rabbit Monoclonal Antibody (Biotinylated) (CST #53324) is ready to ship. Product Usage Information Biotinylated antibodies are ideal for immunoassay technologies and high-throughput ELISA platforms that require antibody pairs where both antibodies are from the same host. Platforms utilizing biotinylated antibodies include, but are not limited to, MSD, xMAP, Quanterix Simoa, AlphaLISA, AlphaScreen, HTRF, LANCE, and TR-FRET. Optimal dilutions/working concentrations should be determined by the end user. Please contact us if you require the antibody clone biotinylated at a different concentration, a carrier-free formulation, or a more customized packaging solution. Storage Supplied in 140 mM NaCl, 3 mM KCl, 10 mM sodium phosphate (pH 7.4) dibasic, 2 mM potassium phosphate monobasic, 2 mg/mL BSA, and 50% glycerol. Store at -20°C. Do not aliquot the antibody. Specificity / Sensitivity VHL (E3X9K) Rabbit Monoclonal Antibody (Biotinylated) 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. Alternate Names elongin binding protein; HRCA1; Protein G7; pVHL; RCA1; VHL; VHL1; von Hippel-Lindau disease tumor suppressor; von Hippel-Lindau tumor suppressor; von Hippel-Lindau tumor suppressor, E3 ubiquitin protein ligase Specification REACTIVITY: H M SENSITIVITY: Endogenous Source/Isotype: Rabbit IgG