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anti-Human VHL Antibodies:
anti-Mouse (Murine) VHL Antibodies:
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Human Monoclonal VHL Primary Antibody for IHC (f), ICS - ABIN2689963
Baba, Hirai, Kawakami, Kishida, Sakai, Kaneko, Yao, Shuin, Kubota, Hosaka, Ohno: Tumor suppressor protein VHL is induced at high cell density and mediates contact inhibition of cell growth. in Oncogene 2001
Show all 6 Pubmed References
Human Polyclonal VHL Primary Antibody for IP, WB - ABIN151930
Esteban, Tran, Harten, Hill, Castellanos, Chandra, Raval, Obrien, Maxwell: Regulation of E-cadherin expression by VHL and hypoxia-inducible factor. in Cancer research 2006
Show all 4 Pubmed References
Human Polyclonal VHL Primary Antibody for FACS, IHC (p) - ABIN390463
Li, Qu, Jin, Guo, Wang, Qi, Yang, Zhang, Li: Protective effect of salidroside against bone loss via hypoxia-inducible factor-1α pathway-induced angiogenesis. in Scientific reports 2018
Show all 2 Pubmed References
Human Polyclonal VHL Primary Antibody for IHC (p), IP - ABIN250564
Xi, Gao, Han, Li, Feng, Zhang, Ji, Xiao, Zhang, Wei: Hypoxia inducible factor-1α suppresses Peroxiredoxin 3 expression to promote proliferation of CCRCC cells. in FEBS letters 2014
Show all 2 Pubmed References
Human Polyclonal VHL Primary Antibody for ELISA, WB - ABIN188556
Kong, Lin, Liang, Fath, Sang, Caro: Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha. in Molecular and cellular biology 2006
aldehyde dehydrogenase 2 (ALDH2) is found to be transcriptionally regulated by VHL and contributes to enhanced anthracyclines cytotoxicity in clear cell renal cell carcinoma cells.
Data show that von Hippel-Lindau-binding protein 1 (VBP1 (show PFDN3 Antibodies)) enhances the stability of von Hippel-Lindau tumor suppressor protein (show TP53 Antibodies) (pVHL) and facilitates pVHL-mediated ubiquitination of hypoxia-inducible factor 1 (show HIF1A Antibodies), alpha subunit (show POLG Antibodies) (HIF-1alpha (show HIF1A Antibodies)).
Study suggests that reduced expression of PBRM1 (show PBRM1 Antibodies) and VHL in clear cell renal cell carcinoma (show MOK Antibodies) is correlated with an increased tumor aggressiveness. Low VHL expression identified as a risk factor for worse patient overall survival.
The results of the present study also demonstrated a mutation in VHL associated with the VHL syndrome phenotype, which may be of future therapeutic benefit for the diagnosis of VHL syndrome.
Overexpression of VHL was more successful at inhibiting fibrosis compared with silencing HIF-1a plus HIF-2a. Normoxia-active HIF-1a or HIF-2a prevented the inhibitory effect of VHL on liver fibrosis, indicating that attenuating fibrosis via VHL is HIF-1a- and HIF-2a-dependent to some extent.
The inverse correlation between the VHL gene expression profile and alisertib sensitivity was further confirmed in human cancer xenografts models. Taken together, these results suggested that VHL loss could potentially serve as a biomarker for predicting the efficacy of AURKA (show AURKA Antibodies) inhibitors.
JMJD6 (show JMJD6 Antibodies) regulates VHL gene expression in the human placenta. VHL downregulation in preeclampsia is dependent on decreased JMJD6 (show JMJD6 Antibodies) demethylase (show MBD2 Antibodies) activity due to hypoxia and reduced Fe2+ bioavailability.
Low VHL expression is associated with papillary thyroid carcinoma.
that the reduced expression of LimD1 (show LIMD1 Antibodies) and VHL might have synergistic effect on induction of HIF1alpha (show HIF1A Antibodies) resulting increased cellular proliferation and progression of the disease.
A two-hit loss involving VHL predicted for clear-cell renal cell carcinoma (show MOK Antibodies)(ccRCC ) and a better prognosis, whereas mutations in PTEN, TP53 (show TP53 Antibodies), or RELN (show RELN Antibodies) predicted for Sarcomatoid clear-cell renal cell carcinoma (show MOK Antibodies) and worse prognosis.
Interaction between Nm23 (show NME1 Antibodies) and the tumor suppressor VHL
Transgenic pVHL can fully maintain normal dVHL-HIF1-alpha (show HIF1A Antibodies) downstream pathways in flies.
Codepletion of Vhl with Mgr (show GRHL1 Antibodies) gives partial rescue of tubulin (show TUBB Antibodies) instability, monopolar spindle formation, and loss of centrosomes.
The results establish a developmental function of the VHL gene that is relevant to its tumor-suppressor activity.
findings reveal a second type of tracheal hypoxic response in which Sima activation conflicts with developmental tracheogenesis, and identify the dVHL and ago ubiquitin ligases as key determinants of hypoxia sensitivity in tracheal cells
the vhl(-/-) zebrafish kidney is characterized by an increased tubule diameter, disorganized cilia, the dramatic formation of cytoplasmic lipid vesicles, glycogen (show GYS2 Antibodies) accumulation, aberrant cell proliferation and abnormal apoptosis.
In this review, we have tried to bring together knowledge on the HIF/hypoxic signaling pathway in zebrafish, including what is known on VHL functions.
by modulating hypoxia-inducible factor activity via up-regulation of VHL, FOXO3a (show FOXO3 Antibodies) (foxo3b) plays an important role in survival in response to hypoxic stress.
Zebrafish embryos lacking endogenous vhl lead to defective phenotypes in the renal system that were characterized by the curved and cystic pronephric tubule or/and a cystic and malformed glomerulus.
Inhibiting PHD (show PDC Antibodies) or knocking down VHL rescues Methyl tert (show TERT Antibodies)-butyl ether induced vascular lesions.
Zebrafish vhl mutants display a marked increase in blood vessel formation throughout the embryo, and the most severe neovascularization is observed in distinct areas that overlap with high vegfa (show VEGFA Antibodies) mRNA expression, including the vhl mutant brain and eye.
Vhl mutants develop polycythemia with increased epo (show EPO Antibodies)/epor (show EPOR Antibodies) mRNA & erythropoietin (show EPO Antibodies) signaling. VHL regulates hematopoiesis & erythroid differentiation. Zebrafish vhl mutants are the 1st congenital embryonic viable systemic vertebrate animal model for VHL.
Data show that 100% of von Hippel-Lindau tumor suppressor protein (show TP53 Antibodies) (Vhl) / polybromo 1 protein (Pbrm1 (show PBRM1 Antibodies)) knockout mice developed renal cancers by 20 months of age.
VHL-HIF-glycolysis axis is essential for the late-stage maturation and function of ILC2s via targeting IL-33-ST2 pathway.
Oxidative stress upregulates pVHL expression to induce PLN (show PLN Antibodies) degradation in failing hearts.
Loss of VHL could be driving tumour cell dissemination through stabilization of HIF-1alpha (show HIF1A Antibodies) in a murine renal-cell carcinoma (show MOK Antibodies) model. Overexpression of HIF-1alpha (show HIF1A Antibodies)-regulated genes that are upregulated in our VHL knockout cells signifies an aggressive form of clear-cell renal-cell carcinoma (show MOK Antibodies).
We conditionally targeted Bap1 (show BAP1 Antibodies) and Pbrm1 (show PBRM1 Antibodies) (with Vhl) in the mouse using several Cre drivers.Sglt2 and Villin proximal convoluted tubule drivers failed to cause tumorigenesis, challenging the conventional notion of Clear cell renal cell carcinoma (show MOK Antibodies) (ccRCC)origins
dual inactivation of Vhl with either Bap1 (show BAP1 Antibodies) or Pbrm1 (show PBRM1 Antibodies) results in faithful genetically engineered murine models of clear cell renal cell carcinoma (show MOK Antibodies) (ccRCC).
HIF-1alpha (show HIF1A Antibodies)-dependent, HIF-2alpha (show EPAS1 Antibodies)-independent angiogenesis and constitutive diuresis is caused by Vhl deletion in renal epithelia
HIF-1alpha (show HIF1A Antibodies)/miR (show MLXIP Antibodies)-210 pathway is strongly activated in VHL mutated paragangliomas, weakly activated in SDHx mutated PGLs (show PGLS Antibodies), and not activated in VHLdel- and SDHxwt/VHLwt-PGLs (show PGLS Antibodies).
kidney-specific deletion of Vhl and Pbrm1 (show PBRM1 Antibodies), but not either gene alone, results in bilateral, multifocal, transplantable clear cell kidney cancers.
Codeletion of VHL together with HIF2A (show EPAS1 Antibodies) but not with HIF1A (show HIF1A Antibodies) led to apparently normal kidneys, and the animals reached normal age but were anemic because of low erythropoietin (show EPO Antibodies) levels. Stromal deletion of HIF2A (show EPAS1 Antibodies) or HIF1A (show HIF1A Antibodies) alone did not affect kidney development.
Von Hippel-Lindau syndrome (VHL) is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign tumors. A germline mutation of this gene is the basis of familial inheritance of VHL syndrome. The protein encoded by this gene is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible-factor (HIF), which is a transcription factor that plays a central role in the regulation of gene expression by oxygen. RNA polymerase II subunit POLR2G/RPB7 is also reported to be a target of this protein. Alternatively spliced transcript variants encoding distinct isoforms have been observed.
elongin binding protein
, protein G7
, von Hippel-Lindau disease tumor suppressor
, von hippel lindau
, von hippel lindau protein
, von Hippel-Lindau tumor suppressor
, von Hippel-Lindau syndrome homolog
, von Hippel-Lindau syndrome protein homolog
, Von Hippel-Lindau disease tumor suppressor