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anti-Human VHL Anticorps:
anti-Mouse (Murine) VHL Anticorps:
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Human Monoclonal VHL Primary Antibody pour 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. dans Oncogene 2001
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Human Polyclonal VHL Primary Antibody pour IP, WB - ABIN151930
Esteban, Tran, Harten, Hill, Castellanos, Chandra, Raval, Obrien, Maxwell: Regulation of E-cadherin expression by VHL and hypoxia-inducible factor. dans Cancer research 2006
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Human Polyclonal VHL Primary Antibody pour IHC, WB - ABIN6672194
Du, Zhang, Zhang, Ouyang, Wang, Liu, Li, Ji, Liu, Xiao: pVHL Negatively Regulates Antiviral Signaling by Targeting MAVS for Proteasomal Degradation. dans Journal of immunology (Baltimore, Md. : 1950) 2015
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Mouse (Murine) Polyclonal VHL Primary Antibody pour IHC, WB - ABIN3020968
Liu, Cai, Hu, Mei, Zhang, Ouyang, Wang, Zhang, Xiao: Forkhead Transcription Factor 3a (FOXO3a) Modulates Hypoxia Signaling via Up-regulation of the von Hippel-Lindau Gene (VHL). dans The Journal of biological chemistry 2017
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Human Polyclonal VHL Primary Antibody pour 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. dans FEBS letters 2014
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Dog (Canine) Polyclonal VHL Primary Antibody pour ELISA, WB - ABIN547719
Kong, Lin, Liang, Fath, Sang, Caro: Histone deacetylase inhibitors induce VHL and ubiquitin-independent proteasomal degradation of hypoxia-inducible factor 1alpha. dans Molecular and cellular biology 2006
Human Monoclonal VHL Primary Antibody pour ELISA, WB - ABIN532934
Stebbins, Kaelin, Pavletich: Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. dans Science (New York, N.Y.) 1999
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We found the tumors of African American patients to have a significantly lower frequency of VHL mutation (32% vs 49%; p = 0.03) and lower HIF-2a expression (16% vs 41% in the third tertile; ptrend < 0.0001) than those of white patients.
Study in a human renal carcinoma cell line Caki-1 with inactivated VHL gene showed that even without hypoxia, VHL inactivation leads to hypermethylation of the genome. Hypermethylated cytosines were evenly distributed throughout the genome with a slight preference for AP-1 binding sites and tended to be enriched within the binding sites of transcription factors that showed increased gene expression after VHL inactivation.
Most RCC-subtype-discriminative CT features were associated with the key RCC-driven gene-the VHL gene mutation.
These findings showed that VHL regulates NEK1 via both HIF-2alpha pathway and ubiquitin-proteasome pathway in renal cancer cells.
VHL Loss affects Global DNA Methylome and is associated with clear-cell renal cell carcinoma.
Genotype-phenotype correlation in patients with germline mutation in VHL and pancreatic neuroendocrine tumors.
Data show the interactions between von Hippel-Lindau tumor suppressor (VHL) and the cyclin-dependent kinase inhibitor family CDKN1 (p21, p27 and p57).
VHL exon and complex splicing alterations are associated with familial erythrocytosis or von Hippel-Lindau disease.
A novel mutation was found in exon 2 of the VHL gene; the alpha-structure of pVHL is completely absent. The novel c.426delT(p.V142fs) mutation probably underlies von Hippel-Lindau syndrome in this pedigree.
VHL-TGFBI signaling is involved in the synergy between DAC and PTX against RCC cells.
A novel W117R was detected in the VHL gene that caused retinal hemangioblastomas in affected members of a Chinese family.
VHL DNA methylation at the E2F4 transcription factor-binding site is altered in preeclamptic placenta.
Thus after VHL inactivation, HIF induces ISGF3, which is reversed by the loss of secondary tumor suppressors, suggesting that this is a key negative feedback loop in clear cell renal cell carcinoma.
Mutations in the promoter of VHL gene were identified in two cases of Von Hippel-Lindau disease.
In this study, which examined a large cohort of Chinese patients with Von Hippel-Lindau (VHL)disease, we describe a modified genotype-phenotype correlation according to alterations of the HIF-a binding site in VHL protein (pVHL)
VHL tumoral mutations improve NKs effectiveness in RCC patients and need to be considered in the evaluation of immune response.
these results demonstrate that dsVHL-821, a novel saRNA for VHL, induces the expression of the VHL gene by epigenetic changes, leading to inhibition of cell growth and induction of apoptosis, and suggest that targeted activation of VHL by dsVHL-821 may be explored as a novel treatment of renal cell carcinoma.
Inactivation of VHL gene direct angiogenesis in vascular endothelial cells, not vasculogenesis via Twist1 accumulation, was associated with hemangioblastoma neovascularization.
The sporadic hemangioblastoma can occur rarely without a somatic biallelic VHL mutation. The VHL protein was earlier found to be associated with the deposition of matrix fibronectin (FN) protein in the renal extracellular matrix.
In both models, L- as well as D-arginine enhanced the ability of wild-type pVHL and certain misfolded mutant versions of pVHL to bind ODD, the HIF-derived target peptide, reflecting restoration of pVHL function. Moreover, continuous feeding of Drosophila expressing misfolded versions of pVHL either L- or D-arginine rich diet rescued their lethal phenotype.
Interaction between Nm23 and the tumor suppressor VHL
Transgenic pVHL can fully maintain normal dVHL-HIF1-alpha downstream pathways in flies.
Codepletion of Vhl with Mgr gives partial rescue of tubulin 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
vhl is required to maintain pronephric tubule and glomerulus integrity during zebrafish development, and suggests a role for VHL in endocytic vesicle trafficking
the vhl(-/-) zebrafish kidney is characterized by an increased tubule diameter, disorganized cilia, the dramatic formation of cytoplasmic lipid vesicles, glycogen 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 (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 or knocking down VHL rescues Methyl tert-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 mRNA expression, including the vhl mutant brain and eye.
Vhl mutants develop polycythemia with increased epo/epor mRNA & erythropoietin signaling. VHL regulates hematopoiesis & erythroid differentiation. Zebrafish vhl mutants are the 1st congenital embryonic viable systemic vertebrate animal model for VHL.
Study results in transgenic mice demonstrate that the type 2B (murine G518A representing human R167Q) VHL mutation may influence vascular changes and hemangioblastoma formation by accelerating the maturation of larger-caliber arteries in addition to maintaining and expanding capillary density, which could, in turn, worsen pathological progression via blood perfusion defects.
VHL is required for optimal alveolar macrophage terminal differentiation, self-renewal, and function.
results indicate that VHL acts as a crucial regulatory factor in lung inflammation and fibrosis by regulating alveolar macrophages.
Osteocytic Vhl deletion caused high bone mass phenotype, but Hif1a was dispensable in osteocytes.
constitutive or postnatally induced deletion of the hypoxia signaling pathway component von Hippel-Lindau (VHL) in skeletal osteolineage cells of mice led to high bone mass as well as hypoglycemia and increased glucose tolerance, not accounted for by osteocalcin or insulin
Heterozygous mutation in Vhl cooperated with Snf5 deletion to produce hemorrhagic ovarian cysts.
Deletion of the von Hippel-Lindau Gene is associated with Hemangioblastoma-like Lesions in Retina.
VHL role in the clear cell renal cell carcinoma
Data show that 100% of von Hippel-Lindau tumor suppressor protein (Vhl) / polybromo 1 protein (Pbrm1) 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 degradation in failing hearts.
Loss of VHL could be driving tumour cell dissemination through stabilization of HIF-1alpha in a murine renal-cell carcinoma model. Overexpression of HIF-1alpha-regulated genes that are upregulated in our VHL knockout cells signifies an aggressive form of clear-cell renal-cell carcinoma.
We conditionally targeted Bap1 and Pbrm1 (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 (ccRCC)origins
dual inactivation of Vhl with either Bap1 or Pbrm1 results in faithful genetically engineered murine models of clear cell renal cell carcinoma (ccRCC).
HIF-1alpha-dependent, HIF-2alpha-independent angiogenesis and constitutive diuresis is caused by Vhl deletion in renal epithelia
HIF-1alpha/miR-210 pathway is strongly activated in VHL mutated paragangliomas, weakly activated in SDHx mutated PGLs, and not activated in VHLdel- and SDHxwt/VHLwt-PGLs.
kidney-specific deletion of Vhl and Pbrm1, but not either gene alone, results in bilateral, multifocal, transplantable clear cell kidney cancers.
Codeletion of VHL together with HIF2A but not with HIF1A led to apparently normal kidneys, and the animals reached normal age but were anemic because of low erythropoietin levels. Stromal deletion of HIF2A or HIF1A alone did not affect kidney development.
High VHL expression is associated with liver fibrosis.
Study demonstrated that mice with a loss of one allele of the VHL gene exhibited normal phenotypes without evidence of predisposition to the development of CNS-hemangioblastomas. Heterozygous VHL +/- mice exhibited the neuroprotective response to acute cerebral ischemia/reperfusion injury due to enhanced angiogenesis by HIF-dependent regulation and HIF-independent Twist 1 signaling.
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