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Human Polyclonal HIF1AN Primary Antibody for EM, ICC - ABIN151887
Birle, Hedley: Suppression of the hypoxia-inducible factor-1 response in cervical carcinoma xenografts by proteasome inhibitors. in Cancer research 2007
Show all 22 Pubmed References
Human Monoclonal HIF1AN Primary Antibody for ICC, IF - ABIN440718
Cockman, Lancaster, Stolze, Hewitson, McDonough, Coleman, Coles, Yu, Hay, Ley, Pugh, Oldham, Masson, Schofield, Ratcliffe: Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH). in Proceedings of the National Academy of Sciences of the United States of America 2006
Show all 8 Pubmed References
Polyclonal HIF1AN Primary Antibody for IHC (fro), IP - ABIN540709
Ferguson, Muir: MMP-2 and MMP-9 increase the neurite-promoting potential of schwann cell basal laminae and are upregulated in degenerated nerve. in Molecular and cellular neurosciences 2000
Show all 4 Pubmed References
Low FIH expression is associated with lung cancer.
ANKDD1A directly interacts with FIH1 and inhibits the transcriptional activity of HIF1alpha by upregulating FIH1. ANKDD1A decreases the half-life of HIF1alpha by upregulating FIH1, decreases glucose uptake and lactate production, inhibits glioblastoma multiforme (GBM) autophagy, and induces apoptosis in GBM cells under hypoxia
High FIH expression is associated with Ovarian Cancer metastasis.
FIH-1 plasmid transfection decreased the cell proliferation of OS-RC-2 renal carcinoma cells,but did not show inhibition on 786-0 cell proliferation
Since the FIH-1 dependent hydroxylation of NAA10 occurs oxygen-dependently, NAA10 acetylates HIF-1alpha under normoxia but does not under hypoxia.
Authors identified KANK3 as a new substrate for the oxygen sensor hypoxia-inducible factor 1-alpha inhibitor (HIF1AN), which hydroxylates HIF-1/2alpha and other ankyrin repeat domain-containing proteins at asparagine residues.
MiR-31-5p plays an important role in HS formation by inhibiting FIH and regulating the HIF-1alpha pathway.
Low FIH1 expression is associated with chemotherapy resistance in breast cancer.
data support a model in which the facial triad carboxylate Asp(201) provides both steric and polar contacts to favor O2 access to the Fe(II) only after substrate binds, leading to coupled turnover in FIH and other alphaKG oxygenases.
None of the clinicopathological parameters were associated with the expressions of FIH-1 and SOCS3 at mRNA level.
This study provides novel clues indicating that miR-21, miR-31, and miR-184 co-target FIH tumor suppressor during pathogenesis in the vast majority of head and neck squamous cell carcinoma.
Results suggest that NECAB3, a novel Mint3-binding protein, activates HIF-1 to promote normoxic glycolysis and tumorigenicity by forming a ternary complex with Mint3 and FIH-1.
the levels of both miR-182 and HIF1alpha were elevated, while the expression PHD2 and FIH1 was downregulated in a mouse model of prostate cancer.
OTUB1 is a target for functional hydroxylation by FIH.
demonstrates that miR-135b regulates ERalpha, AR and HIF1AN protein levels through interaction with their 3'UTR regions, and proliferation in ERalpha-positive BCa and AR-positive PCa cells
Hypoxia, FIH inhibitors and mutation of asparagine 242 all potentiated TRPV3-mediated current, without altering TRPV3 protein levels, indicating that oxygen-dependent hydroxylation inhibits TRPV3 activity.
the nuclear entry of FIH-1 depends on HIF-1alpha
The kinetic properties of PHD2 and FIH with respect to oxygen reflect their cellular hypoxia-sensing ability.
data support the concept that FIH-1 may interact with Notch2 and repress its activity, thereby playing a critical role in controlling the survival of vascular endothelial cells
miR-31/FIH1 pathway associates with liver fibrosis, perhaps by participation in the TGF-beta/Smad3 signalling of hepatic stellate cells.
FIH-1 has a role in disrupting the LRRK1/EGFR complex to positively regulate keratinocyte migration
gankyrin binds to and sequester factor inhibiting hypoxia-inducible factor-1 (FIH-1), which results in decreased interaction between FIH-1 and hypoxia-inducible factor-1alpha (HIF-1alpha) and increased activity of HIF-1 to promote VEGF production.
Our results define a previously unknown mechanism for keratinocyte fate decisions where Notch signaling potential is, in part, controlled through a miR-31/FIH-1 nexus.
Overexpression of factor inhibiting HIF-1 enhances vessel maturation and tumor growth via platelet-derived growth factor-C in osteosarcoma.
FIH recognizes distinct molecular features within HIF-alpha1 versus ankyrin repeat containing substrates Notch1/4 and Gankyrin.
Quantitative mass spectrometry reveals dynamics of factor-inhibiting hypoxia-inducible factor-catalyzed hydroxylation.
FIH1 appears to be a suppressor of oxygen-dependent genes in the kidney, operating through HIF-dependent and -independent mechanisms.
Lackin of hypoxia-inducible factor 1 alpha subunit inhibitor exhibit reduced body weight, elevated metabolic rate, hyperventilation, and improved glucose and lipid homeostasis and are resistant to high-fat-diet-induced weight gain and hepatic steatosis.
This gene encodes the alpha subunit of transcription factor hypoxia-inducible factor-1 (HIF-1), which is a heterodimer composed of an alpha and a beta subunit. HIF-1 functions as a master regulator of cellular and systemic homeostatic response to hypoxia by activating transcription of many genes, including those involved in energy metabolism, angiogenesis, apoptosis, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1 thus plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene.
, factor inhibiting HIF-1
, factor inhibiting HIF1
, hypoxia-inducible factor 1-alpha inhibitor
, hypoxia-inducible factor asparagine hydroxylase
, peptide-aspartate beta-dioxygenase
, hypoxia-inducible factor 1, alpha subunit inhibitor
, LOW QUALITY PROTEIN: hypoxia-inducible factor 1-alpha inhibitor