Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human HIF1A Protein expressed in Wheat germ - ABIN1306618
Vadivel, Alphonse, Etches, van Haaften, Collins, OReilly, Eaton, Thébaud: Hypoxia-inducible factors promote alveolar development and regeneration. in American journal of respiratory cell and molecular biology 2014
Show all 3 Pubmed References
Data indicate that the HIF-1alpha/VEGF-A (show VEGFA Proteins) axis is an essential aspect of tumor immunity.
PROX1 overexpression in DAB2IP-deficient prostate cancer cells could enhance the accumulation of HIF1alpha protein by inhibiting ubiquitin pathway and then consequently induce an epithelial-mesenchymal transition response.
findings suggest that hypoxia, through HIF1A, contributes to the development and progression of pulmonary fibrosis through its regulation of ADORA2B (show ADORA2B Proteins) expression on alternatively activated macrophages, cell differentiation, and production of profibrotic mediators
Death receptor5 pathway and mitochondrial pathway, which are likely mediated by HIF-1alpha, contribute to hypoxia-induced spermatocyte apoptosis.
Mechanical low shear stress activates HIF1alpha at atheroprone regions of arteries via nuclear factor-kappaB and Cezanne (show OTUD7B Proteins). HIF1alpha promotes atherosclerosis initiation at these sites by inducing excessive endothelial cell proliferation and inflammation via the induction of glycolysis enzymes.
CRP (show CRP Proteins) can upregulate vascular endothelial growth factor-A (VEGF-A (show VEGFA Proteins)) expression by activating hypoxia inducible factor-1alpha (HIF-1alpha) in ADSCs.
induction of HIF-1alpha mediated transcriptional up-regulation of pro-apoptotic/inflammatory signaling contributes to astrocyte cell death during thiamine deficiency.
Smad3 (show SMAD3 Proteins) binding to the -335 hypoxia-responsive element of the COL1A2 (show COL1A2 Proteins) promoter required HIF-1alpha both in vitro and in kidney lysate from the disease model, suggesting formation of an HIF-1alpha-Smad3 (show SMAD3 Proteins) transcriptional complex. Thus, HIF-1alpha-Smad3 (show SMAD3 Proteins) has a novel interaction in glomerulosclerosis.
These results suggest that cyclosporine A (CsA (show HSPA9 Proteins)) exhibits antifibrotic effects by degrading HIF-1alpha and that the CsA (show HSPA9 Proteins)-HIF-1alpha axis provides new insights into therapeutic options for the treatment of pulmonary fibrosis.
HIF-1alpha protein levels in the ipsilateral hemisphere were higher in the WT mice than Par-1 (show MARK2 Proteins) KO mice after glioma cell implantation.
Results show that HIF-1a expression is positively regulated by LINC00152 through its binding to miR (show MLXIP Proteins)-138.
These results indicate that the immunohistochemistry analysis of the protein expression of PDK1 (show PDK1 Proteins), PHD3 (show EGLN3 Proteins), and HIF-1alpha defines the hypoxic status of Neuroblastoma (show ARHGEF16 Proteins) tumors.
This phosphorylation increases its ability to degrade HIF1alpha.
MiR (show MLXIP Proteins)-31-5p plays an important role in HS formation by inhibiting FIH (show CASR Proteins) and regulating the HIF-1alpha pathway.
ASK1 (show MAP3K5 Proteins) phosphorylated and stabilized TLX (show CD46 Proteins), which led induction of HIF-1alpha, and its downstream VEGF-A (show VEGFA Proteins) in an Akt (show AKT1 Proteins) dependent manner.
The BAFF (show TNFSF13B Proteins) promoter increased in response to TNF-alpha (show TNF Proteins) treatment or overexpression of HIF-1alpha. However, TNF-alpha (show TNF Proteins)-induced BAFF (show TNFSF13B Proteins) expression and promoter activity decreased after treatment with the ERK (show EPHB2 Proteins) inhibitor PD98059.
This study demonstrated that HIF-1alpha is a key regulator of glucose metabolism in skeletal muscle by directly controlling the transcription of RAB20 (show RAB20 Proteins) and TXNIP (show TXNIP Proteins).
we report that genetic removal of CSL (show CSHL1 Proteins) in breast tumor cells caused accelerated growth of xenografted tumors. Loss of CSL (show CSHL1 Proteins) unleashed a hypoxic response during normoxic conditions, manifested by stabilization of the HIF1alpha protein and acquisition of a polyploid giant-cell, cancer stem cell-like, phenotype.
NAP peptide prevents outer blood retinal barrier breakdown by reducing HIF1alpha/HIF2alpha (show EPAS1 Proteins), VEGF (show VEGFA Proteins)/VEGFRs, and increasing HIF3alpha expression Moreover it is able to reduce the percentage of apoptotic cells by modulating the expression of two death related genes, BAX (show BAX Proteins) and Bcl2 (show BCL2 Proteins).
a high expression of hypoxia induced factor-1a (HIF-1a) and heat shock protein 70 (HSP70 (show HSP70 Proteins)) was noted
Induction of ischemic osteonecrosis results in IL-6 (show IL6 Proteins) production in the articular cartilage through an HIF-1-dependent pathway.
Upregulation of VEGF (show VEGFA Proteins) during hypoxia in chondrocyte is mediated partially through HIF-1alpha.
HIF-1alpha activates Sox9 (show SOX9 Proteins) expression and enhances Sox9 (show SOX9 Proteins)-mediated transcriptional activity.
Intramyocardial delivery of mesenchymal stem cells seems to trigger the release of angiogenic HIF-1alpha more effectively than does intracoronary delivery.
immunostaining for HIF-1alpha and HIF-2alpha (show EPAS1 Proteins) was observed during endochondral ossification, whereas only HIF-2alpha (show EPAS1 Proteins) was present at sites of intramembranous ossification
Downregulation of miR (show MYLIP Proteins)-199a derepresses hypoxia-inducible factor-1alpha and Sirtuin 1 (show SIRT1 Proteins) and recapitulates hypoxia preconditioning in cardiac myocytes.
Viable chondrocytes in the superficial layer of the epiphyseal cartilage showed HIF-1alpha activation and VEGF upregulation with subsequent revascularization occurring in the cartilage.
inverse expression and localization pattern of HIF1A and vasohibins during different stages of ovarian function in cow
Hypoxia increased the amounts of HIF1A protein, VEGF mRNA and VEGF protein in cultured bovine luteal cells.
hypoxia-induced changes in vascular cell growth are altered by hyperglycemia via inhibition of HIF-1alpha expression and activity
VEGF has an effect on the expression of its own transcription factor, HIF-1, and on VEGF itself
Identify sphingosine-1-phosphate as a novel and potent nonhypoxic activator of HIF-1.
Suggest supplemental oxygen inhibits HIF-1alpha/VEGF signaling to reduce smooth muscle proliferation in rabbit arteriovenous fistula model.
HIF-1alpha-induced HSP70 (show HSP70 Proteins) overexpression increased the expression levels of ECM (show MMRN1 Proteins) genes and cell viability, and protected chondrocytes from apoptosis. HIF-1alpha may regulate anabolic effects of chondrocytes under hypoxic conditions by regulating HSP70 (show HSP70 Proteins) expression
Transcatheter arterial embolization of liver tumors increases the expression of HIF-1alpha at protein level in the residual viable tumor.
Upregulation of HIF-1 protects cardiac myocyte function after ischemia/reperfusion by maintaining calcium release.
HIF-1alpha expression in early atherosclerosis can promote the formation of neovascularization.
Xells respond to hypoxia through a transcription factor, hypoxia-inducible factor 1
Upregulation of HIF-1 could protect isolated cardiac myocytes against nitrate tolerance through a cyclic GMP protein kinase-independent mechanism and through a kinase-dependent mechanism in myocardial stunning.
rhEPO can down-regulate HIF-1alpha expression in the retina of rabbits with acute high intraocular pressure.
Increased HIF-1 alpha protects the functional effects of cyclic GMP thorough maintenance of cyclic GMP protein kinase activity after ischemic-reperfusion
blocking HIF-1 activity may promote survival in cells with compromised mitochondrial function.
HIF-1-mediated activation of 5-HT (show DDC Proteins) signalling promotes axon regeneration by activating both the RhoA (show RHOA Proteins) and cAMP pathways.
this study reports that neuronal stabilization of HIF-1 mediates these effects in Caenorhabditis elegans through a cell nonautonomous signal to the intestine, which results in activation of the xenobiotic detoxification enzyme flavin-containing monooxygenase-2 (FMO-2 (show FMO2 Proteins)).
AMPK (show PRKAA1 Proteins) and HIF-1 may control immunity and longevity tightly by acting as feedback regulators of ROS (show ROS1 Proteins)
Growth in hypoxia increases longevity in wild-type worms but not in animals lacking HIF-1 or DAF-16. Conversely, hypoxia shortens life span in combination with overexpression of the antioxidant stress response protein SKN-1.
Increased levels of hydrogen peroxide induce a HIF-1-dependent modification of lipid metabolism in AMPK (show PRKAA1 Proteins) compromised C. elegans dauer larvae.
These data show that HIF-1 regulates intestinal iron homeostasis during iron deficiency by activating and inhibiting genes involved in iron uptake and storage.
Data indicate that genes sqrd-1, ethe-1 (show ETHE1 Proteins), cysl-1, cysl-2 and HIF-1 are involved in survival to hydrogen sulfide (show SQRDL Proteins) and hydrogen cyanide.
Data show that stabilization of HIF-1 increases life span robustly under all conditions tested; however, deletion of hif-1 increases life span in a temperature-dependent manner.
Data show that that reactive oxygen species (ROS (show ROS1 Proteins)) are increased in respiration mutants and that mild increases in ROS (show ROS1 Proteins) can stimulate HIF-1 to activate gene expression and promote longevity.
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.
, HIF1 alpha
, Hypoxia-inducible factor 1 alpha
, hypoxia-inducible factor 1-alpha
, ARNT-interacting protein
, ARNT interacting protein
, PAS domain-containing protein 8
, basic-helix-loop-helix-PAS protein MOP1
, class E basic helix-loop-helix protein 78
, hypoxia-inducible factor 1 alpha isoform I.3
, hypoxia-inducible factor 1, alpha subunit (basic helix-loop-helix transcription factor)
, hypoxia-inducible factor1alpha
, member of PAS protein 1
, member of PAS superfamily 1
, hypoxia-inducible factor 1 alpha
, hypoxia inducible factor 1 alpha subunit
, hypoxia inducible factor 1, alpha subunit