EPAS1 Recombinant Monoclonal Antibody

Code CSB-RA904931A0HU
Size US$210
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  • Immunofluorescence staining of Hela Cells with CSB-RA904931A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeated by 0.2% TritonX-100, and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4℃. Nuclear DNA was labeled in blue with DAPI. The secondary antibody was FITC-conjugated AffiniPure Goat Anti-Rabbit IgG (H+L).
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Product Details

Uniprot No.
Target Names
Alternative Names
Endothelial PAS domain-containing protein 1 (EPAS-1) (Basic-helix-loop-helix-PAS protein MOP2) (Class E basic helix-loop-helix protein 73) (bHLHe73) (HIF-1-alpha-like factor) (HLF) (Hypoxia-inducible factor 2-alpha) (HIF-2-alpha) (HIF2-alpha) (Member of PAS protein 2) (PAS domain-containing protein 2), EPAS1, BHLHE73 HIF2A MOP2 PASD2
Species Reactivity
A synthesized peptide derived from human HIF-2 alpha
Immunogen Species
Homo sapiens (Human)
Rabbit IgG
Clone No.
Purification Method
It differs from different batches. Please contact us to confirm it.
Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Tested Applications
Recommended Dilution
Application Recommended Dilution
IF 1:20-1:200
Troubleshooting and FAQs
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

B cells isolated from the animal that was immunized with a synthesized peptide derived from human EPAS1 were fused with myeloma cells to form hybridomas. The cDNA for the variable light (VL) and variable heavy (VH) domains of the EPAS1 antibody-producing hybridomas was sequenced and used as a model for vector construction in the recombinant generation. The vector containing the EPAS1 monoclonal antibody gene was then transfected into cells for culture. The EPAS1 recombinant monoclonal antibody was purified from the cell culture supernatant using affinity chromatography, and its specificity was tested in ELISA and IF applications, with the antibody proving to detect only human EPAS1 protein.

The EPAS1 (also known as HIF-2 alpha) protein plays a critical role in cellular adaptation to hypoxic environments. In normal oxygen levels, EPAS1 is rapidly degraded by hydroxylation, which targets the protein for degradation by the proteasome. However, in hypoxic environments, the hydroxylation process is inhibited, allowing EPAS1 to accumulate and activate the expression of genes involved in angiogenesis, erythropoiesis, and metabolism. EPAS1 also plays a role in the development and function of certain organs, such as the lungs and kidneys. Mutations in EPAS1 have been associated with various diseases, including cancer, pulmonary hypertension, and erythrocytosis.

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Target Background

Transcription factor involved in the induction of oxygen regulated genes. Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters. Regulates the vascular endothelial growth factor (VEGF) expression and seems to be implicated in the development of blood vessels and the tubular system of lung. May also play a role in the formation of the endothelium that gives rise to the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase expression. Activation requires recruitment of transcriptional coactivators such as CREBBP and probably EP300. Interaction with redox regulatory protein APEX1 seems to activate CTAD.
Gene References into Functions
  1. CPT1A is repressed by HIF1 and HIF2, reducing fatty acid transport into the mitochondria, and forcing fatty acids to lipid droplets for storage. PMID: 29176561
  2. PD-L1 tumor cell expression is strongly associated with increased HIF-2alpha expression and presence of dense lymphocytic infiltration in clear cell renal cell carcinoma. PMID: 30144808
  3. Hypoxia-induced angiogenesis is a complex process that involves distinct but also overlapping functions of HIF-1alpha and HIF- 2alpha in regard to angiogenesis, bioenergetic adaption and the redundant transcriptional induction of MIF. PMID: 28993199
  4. High HIF2A expression is associated with high Collagen I Fibers in Triple Negative Breast Cancer. PMID: 29247885
  5. The studies indicate that HIF2-alpha induces myocardial AREG expression in cardiac myocytes, which increases myocardial ischemia tolerance. PMID: 29483579
  6. High HIF2A expression is associated with Cervical Cancer. PMID: 29321085
  7. Data found that overexpression of HIF-2alpha up-regulate the level of NEAT1 and promote EMT and metastasis in hepatoma cell under hypoxia, and inhibition of HIF-2alpha reverse the results. These indicated that HIF-2alpha can promote EMT and metastasis in hepatocellular carcinoma under hypoxia. PMID: 29091312
  8. Studies have shown that both HIF1alpha and HIF2alpha may contribute to the regulation of cellular adaptation to hypoxia and resistance to cancer therapies with their potential to exert significant effects on the maintenance and evolution of cancer stem cells. Also, HIF1alpha and HIF2alpha seemed to have significant prognostic and predictive value. [review] PMID: 29845228
  9. HIF-2alpha expression may be associated with the carcinogenesis of colorectal cancer (CRC), which is higher in males than in females, negatively linked to tumor differentiation, and correlated with a worse disease-free survival of CRC - Systematic Analysis PMID: 30021192
  10. 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. PMID: 28112200
  11. HDX negatively regulates EPAS1 expression through a release-of-inhibition mechanism. PMID: 29577908
  12. sing imputed data, we found that this SNP remained significant in the entire TRICL-ILCCO consortium (p=.03). Additional functional studies are warranted to better understand interrelationships among genetic polymorphisms, DNA methylation status, and EPAS1 expression. PMID: 29859855
  13. Results suggest an interplay of the production and action of hydrogen sulfide during hypoxia with subsequent erythropoietin production regulated by HIF-1alpha and HIF-2alpha. PMID: 26880412
  14. This suggests that higher aerobic capacities are caused by the presence of at least one minor A-Allele of the EPAS1 gene in the genome of an athlete PMID: 29446909
  15. we report a rare case of renal-cell carcinoma and hereditary polycythemia. Genotyping revealed that the patient carried both a germline HIF2A mutation and a somatic VHL mutation. Both mutations result in overactivation of HIF2A and its downstream target genes PMID: 29172931
  16. Identification of gain-of-function somatic mutations of EPAS1, which encodes for HIF-2alpha, in pheochromocytomas and paragangliomas in patients who presented with cyanotic congenital heart disease. PMID: 29601261
  17. HIF-2a regulates non-canonical glutamine metabolism via activation of PI3K/mTORC2 pathway and GOT1 expression in human pancreatic ductal adenocarcinoma. PMID: 28544376
  18. We studied the hypoxic activation of the transcription factors HIF-1alpha and HIF-2alpha in endothelial cells within a spatial linear gradient of oxygen. Quantification of the nuclear to cytosolic ratio of HIF immunofluorescent staining demonstrated that the threshold for HIF-1alpha activation was below 2.5% O2 while HIF-2alpha was activated throughout the entire linear gradient. PMID: 28840922
  19. miRNA-101 level is decreased in RCC tissues/cells, which could be responsible for DNA-PKcs overexpression and DNA-PKcs mediated oncogenic actions; DNA-PKcs over-expression regulates mTORC2-AKT activation, HIF-2alpha expression and RCC cell proliferation PMID: 27412013
  20. report shows that somatic gain-of-function HIF2A mutations are present in 20% of gangliocytic paragangliomas (GPGLs) in the present series; the mutations appear to be located in the hot spot of the oxygen-sensing domain of HIF-2alpha, resulting in increased HIF-2alpha stabilization and impaired ubiquitination and degradation PMID: 27130043
  21. these findings establish a new link between HIF-2alpha and MAPK-signaling that mediates the adaptive regulation of mitochondrial gene expression under low oxygen tension. PMID: 28709643
  22. HIF-2alpha and VM were overexpressed in pancreatic cancer tissues and were associated with poor pathological characteristics. HIF-2alpha contributes to VM formation by regulating the expression of VE-cadherin through the binding of the transcription factor Twist1 to the promoter of VE-cadherin in pancreatic cancer both in vitro and in vivo. PMID: 28599281
  23. HIF-2alpha facilitated the preservation of Human placenta-derived mesenchymal stem cell stemness and promoted their proliferation by regulating CCND1 and MYC through the MAPK/ERK signaling pathway. PMID: 27765951
  24. Results showed that HIF-1alpha and HIF-2alpha were highly expressed in vascular malformation (GIVM) and suggest that they induced angiogenesis in GIVM. PMID: 27249651
  25. The present study demonstrates that hypoxia-induced downregulation of Dicer serves as key mechanism in the maintenance of the hypoxic response in HCC and that prevention of hypoxic suppression of Dicer not only alleviates hypoxia-induced upregulation of HIF1alpha and HIF2alpha and other key hypoxia-responsive/HIF target genes, but also inhibits hypoxia-induced metastatic phenotypes such as EMT and increased cell motility. PMID: 28167508
  26. HIF-2alpha dictates the resistance of human pancreatic cancer cells to TRAIL under normoxic and hypoxic conditions and transcriptionally regulates survivin expression. PMID: 28476028
  27. SOD3 reduced HIF prolyl hydroxylase domain protein activity, which increased hypoxia-inducible factor-2alpha (HIF-2alpha) stability and enhanced its binding to a specific vascular endothelial cadherin promoter region. PMID: 29422508
  28. Functionally active PHD2 SNP rs516651 [18], located in the key pathway for the hypoxic-inflammatory response, is associated with increased 30-day mortality in Acute Respiratory Distress Syndrome (ARDS) patients. In contrast, the PHD2 SNP rs480902 is not. Furthermore, the HIF-2alpha SNP [ch2: 46441523(hg18)] GG-genotype was neither present in our ARDS patients of Caucasian heritage nor in healthy Caucasian blood donors. PMID: 28613249
  29. We genotyped 347 Tibetan individuals from varying altitudes for both the Tibetan-specific EGLN1 haplotype and 10 candidate SNPs in the EPAS1 haplotype and correlated their association with hemoglobin levels. PMID: 28233034
  30. HIF-2alpha plays an important role in regulating the expression of c-Myc in chronic hypoxia, and consequently controls the sensitivity of colon cancer cells to 5-FU treatment in this environment. PMID: 27793037
  31. The present study identifies novel HIF-2alpha-target genes that may regulate endothelial sprouting during prolonged hypoxia. PMID: 27699500
  32. Exogenous acetate augments Acss2/HIF-2 dependent cancer growth and metastasis in cell culture and mouse models PMID: 29281714
  33. the structural model of the HIF2a-pVHL complex presented in this study enhances understanding of how HIF2a is captured by pVHL. Moreover, the important contact amino acids that we identified may be useful in the development of drugs to treat HIF2a-related diseases. PMID: 27902963
  34. Thus, we provide evidence here that HIF-2a is a critical regulator of PD-L1 at both mRNA and protein levels and that HIF-2a regulates the expression of PD-L1 by binding directly to the HRE-4 in the PD-L1 proximal promoter. PMID: 26707870
  35. HIF2alpha has a role and is an independent marker of the metastatic potential of bone metastatic clear cell renal cell cancer; however, unlike HIF1alpha, increased HIF2alpha expression is a favorable prognostic factor PMID: 27244898
  36. Knockdown of either HIF-1 or CREB or both in hypoxia reduced the expression of hypoxia-response elements- and CRE-mediated gene expression, diminished cell proliferation and increased caspase-3 activity. We did not detect any significant effect of the efficiently knocked down HIF-2 on any of the functions tested in vitro. PMID: 27934882
  37. miR-558 facilitates the expression of HIF-2alpha through binding to its 5'-UTR, thus promoting the tumorigenesis and aggressiveness of neuroblastoma PMID: 27276678
  38. Over-expression of HIF-2alpha induced apoptosis in HCC cells and increased the levels of pro-apoptotic proteins, Bak, ZBP-89 and PDCD4, whereas the inhibition of HIF-2alpha expression achieved opposite results. HIF-2alpha was decreased and played an anti-tumorigenic role in hepatocellular carcinoma. PMID: 27119229
  39. Probiotic Bifidobacterium bifidum MIMBb75 may help attenuating EPAS1 overexpression associated with intestinal inflammation. PMID: 27883285
  40. Data suggest that HIF2alpha mediates hypoxia-induced cancer growth/metastasis and that EFEMP1 is a downstream effector of hypoxia-induced HIF2alpha during breast tumorigenesis. PMID: 27270657
  41. intestine HIF-2alpha regulates ceramide metabolism mainly from the salvage pathway, by positively regulating the expression of Neu3, the gene encoding neuraminidase 3. These results suggest that intestinal HIF-2alpha could be a viable target for hepatic steatosis therapy PMID: 29035368
  42. demonstrated that MM cells are resistant to hypoxia-mediated apoptosis in vivo and in vitro, and that constitutive expression of HIF2alpha contributed to this resistance PMID: 29206844
  43. HIF1A and EPAS1 potentiate hypoxia-induced upregulation of INHA expression in human term cytotrophoblasts in vitro. PMID: 28115494
  44. Data show there was a significant negative correlation between PHGDH copy-number alteration and EPAS1 (HIF2A) expression. PMID: 28951458
  45. NAP peptide prevents outer blood retinal barrier breakdown by reducing HIF1alpha/HIF2alpha, VEGF/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 and Bcl2. PMID: 28436035
  46. Data identify a previously unrecognized cellular process associated with hypoxia, and suggests that in vivo tumour hypoxia determines copper isotope fractionation in hepatocellular carcinoma and demonstrate that this effect of hypoxia is pH, HIF-1 and -2 independent. PMID: 27500357
  47. findings suggest the HIF-2alpha pathway predominates over HIF-1alpha signalling in neuronal-like cells following acute hypoxia PMID: 28968430
  48. these findings demonstrated that HIF-2alpha in vselMSCs cooperated with Oct4 in survival and function. The identification of the cooperation between HIF-2alpha and Oct4 will lead to deeper characterization of the downstream targets of this interaction in vselMSCs and will have novel pathophysiological implications for the repair of infarcted myocardium. PMID: 28079892
  49. findings indicate that HIF-2alpha increases cancer cell growth by up-regulating YAP1 activity PMID: 28848049
  50. Findings show that hypoxia inducible factor 1 alpha subunit (HIF-1alpha) is phylogenetically conserved among most metazoans, whereas HIF-2alpha protein appeared later. PMID: 28614393

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Involvement in disease
Erythrocytosis, familial, 4 (ECYT4)
Subcellular Location
Nucleus. Nucleus speckle.
Tissue Specificity
Expressed in most tissues, with highest levels in placenta, lung and heart. Selectively expressed in endothelial cells.
Database Links

HGNC: 3374

OMIM: 603349

KEGG: hsa:2034

STRING: 9606.ENSP00000263734

UniGene: Hs.468410

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