EPAS1 Antibodies

Structure of EPAS1

The molecular weight of the EPAS1 protein (the α subunit of hypoxia-inducible factor) is approximately 100 kDa. The number of amino acid residues varies among different species, resulting in a slight fluctuation in molecular weight.

This protein is composed of approximately 870 amino acid residues and exhibits a modular structure. Its N-terminal region contains a helix-loop-helix (HLH) and two tandem PAS (Per-ARNT-Sim) domains, which are responsible for dimerization with the ARNT protein and recognition of hypoxia response elements on DNA; the oxygen-dependent degradation domain (ODD) at the C-terminal is ubiquitinated and degraded by proline hydroxylase under normoxic conditions. The protein's internal hydrophobic core encapsulates the interface that binds to cofactors (such as HRE sequences), and key sites such as specific residues within the PAS-B domain (for example, the common D3E variation among Zang people) can alter protein stability or transcriptional activity, thereby affecting the organism's ability to adapt to low-oxygen environments. Its activity is directly regulated by cellular oxygen concentration and constitutes the core of oxygen homeostasis regulation.

Fig. 1 The structure of EPAS1.¹

Key structural properties of EPAS1:

• Modular protein domains (including helix-ring-helix and PAS functional domains)
• Stability regulation mediated by the oxygen-sensitive degradation domain (ODD)
• Key amino acid sites (such as Tibetan-specific variant sites) affect the efficiency of hypoxia response

Functions of EPAS1

The core function of the EPAS1 gene (also known as HIF-2α) is to act as the primary regulatory factor in hypoxic conditions, coordinating the body's adaptation and response to oxygen deprivation. Its main physiological functions are as follows:

Its expression and activity are precisely regulated by oxygen concentration, prolyl hydroxylase, and the ubiquitination degradation pathway.

Applications of EPAS1 and EPAS1 Antibody in Literature

1. Pirri, Daniela, et al. "EPAS1 attenuates atherosclerosis initiation at disturbed flow sites through endothelial fatty acid uptake." Circulation research 135.8 (2024): 822-837. https://doi.org/10.1161/CIRCRESAHA.123.324054

Research has revealed the protective effect of the transcription factor EPAS1 in atherosclerosis: the expression of EPAS1 increases in areas with blood flow disorders, and obesity inhibits its expression through the triglyceride-PHD2 pathway, leading to a decline in the proliferation and repair ability of endothelial cells, thereby accelerating plaque formation. Targeting this pathway may provide a new strategy for obesity-related vascular lesions.

2. Kyriakopoulou, Eirini, et al. "EPAS1 induction drives myocardial degeneration in desmoplakin-cardiomyopathy." Iscience 28.3 (2025). https://doi.org/10.1016/j.isci.2025.111895

Research has revealed that EPAS1 is a key regulatory factor driving mitochondrial dysfunction, hypoxia stress and myocardial degeneration in cardiomyocytes in arrhythmic cardiomyopathy (ACM). This discovery provides new molecular mechanisms and potential therapeutic targets for ACM related to gene mutations such as DSP.

3. Wang, Na, et al. "Updated perspective of EPAS1 and the role in pulmonary hypertension." Frontiers in cell and developmental biology 11 (2023): 1125723. https://doi.org/10.3389/fcell.2023.1125723

Research reveals that the core pathology of pulmonary arterial hypertension (PH) is hypoxia-driven vascular remodeling. This article reviews the molecular structure and function of EPAS1 (HIF-2α) and its regulatory network in cardiovascular diseases such as PH, providing a theoretical basis for the development of new targets for vascular remodeling.

4. Li, Qinyu, et al. "Atractylenolide I inhibits angiogenesis and reverses sunitinib resistance in clear cell renal cell carcinoma through ATP6V0D2-mediated autophagic degradation of EPAS1/HIF2α."Autophagy21.3 (2025): 619-638. https://doi.org/10.1080/15548627.2024.2421699

Studies have revealed that Atletalide I (ATL-I) inhibits angiogenesis and tumor growth in clear cell renal cell carcinoma (ccRCC) by upregulating ATP6V0D2, promoting autophagic degradation of EPAS1 (HIF-2α), and suppressing VEGFA production, and can reverse sunitinib resistance.

5. Liu, Lili, et al. "EPAS1 amplifies asthma pathogenesis through JAK2/STAT3-mediated ferroptosis and inflammation." Biomolecules and Biomedicine 25.9 (2025): 2092. https://doi.org/10.17305/bb.2025.11334

Research has found that in asthma, the JAK2/STAT3 signaling axis drives ferroptosis and inflammatory responses by up-regulating EPAS1 expression. EPAS1 has been identified as a key hub gene related to immune cell infiltration and can serve as a potential therapeutic target and novel biomarker for asthma.

Creative Biolabs: EPAS1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality EPAS1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom EPAS1 Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our EPAS1 antibodies, custom preparations, or technical support, contact us at email.