EGLN1 Antibody

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Product Specs

Buffer
PBS with 0.02% Sodium Azide, 50% Glycerol, pH 7.3. Store at -20°C. Avoid freeze / thaw cycles.
Lead Time
Typically, we can ship the products within 1-3 business days after receiving your order. Delivery times may vary depending on the purchasing method or location. Please contact your local distributors for specific delivery times.
Synonyms
C1ORF12 antibody; Chromosome 1 Open Reading Frame 12 antibody; DKFZp761F179 antibody; ECYT 3 antibody; ECYT3 antibody; Egl 9 family hypoxia inducible factor 1 antibody; EGL 9 homolog of C. elegans 1 antibody; EGL nine (C.elegans) homolog 1 antibody; Egl nine homolog 1 (C. elegans) antibody; Egl nine homolog 1 antibody; Egl nine like protein 1 antibody; EGLN 1 antibody; Egln1 antibody; EGLN1_HUMAN antibody; HIF PH2 antibody; HIF Prolyl Hydroxylase 2 antibody; HIF-PH2 antibody; HIF-prolyl hydroxylase 2 antibody; HIFP4H 2 antibody; HIFPH2 antibody; HPH 2 antibody; HPH-2 antibody; HPH2 antibody; Hypoxia inducible factor prolyl hydroxylase 2 antibody; Hypoxia-inducible factor prolyl hydroxylase 2 antibody; ORF13 antibody; P4H2 antibody; PHD 2 antibody; PhD2 antibody; PNAS 118 antibody; PNAS 137 antibody; Prolyl Hydroxylase Domain Containing Protein 2 antibody; Prolyl hydroxylase domain-containing protein 2 antibody; Rat Homolog of SM20 antibody; SM 20 antibody; SM-20 antibody; SM20 antibody; Zinc finger MYND domain containing protein 6 antibody; ZMYND6 antibody
Target Names
Uniprot No.

Target Background

Function
EGLN1 (Egl Nine homolog 1), also known as PHD2 (Prolyl Hydroxylase Domain 2), is a cellular oxygen sensor that plays a critical role in regulating the stability of hypoxia-inducible factors (HIFs). Under normoxic conditions, EGLN1 catalyzes the post-translational hydroxylation of specific proline residues within the oxygen-dependent degradation (ODD) domains of HIFα proteins, such as HIF1A and HIF2A. This hydroxylation event targets HIFα proteins for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Conversely, under hypoxic conditions, EGLN1 activity is attenuated, allowing HIFα proteins to escape degradation and translocate to the nucleus, where they heterodimerize with HIF1B and promote the expression of hypoxia-inducible genes. EGLN1 is the most prominent isozyme responsible for HIF1 stability under normoxic conditions, and it is involved in various hypoxia-influenced processes, including angiogenesis in retinal and cardiac function. EGLN1 preferentially recognizes target proteins via a LXXLAP motif.
Gene References Into Functions
  1. This study elucidates the molecular basis of the c-Myc/EGLN1-mediated induction of LSH expression, which inhibits ferroptosis. PMID: 28900510
  2. In vitro studies demonstrated that a complement C1q-A chain peptide is not a substrate for PHD2 but is a substrate for CP4H1. PMID: 28506759
  3. GPT2 reduced alpha-ketoglutarate level in cells, leading to the inhibition of proline hydroxylase 2 (PHD2) activity involved in regulating HIF1alpha stability. Accumulation of HIF1alpha, resulting from the GPT2-alpha-ketoglutarate-PHD2 axis, constitutively activates the sonic hedgehog (Shh) signaling pathway. PMID: 28839461
  4. This study examined the association between SNPs around the EGLN1 genomic region, potentially involved in high-altitude adaptation, and physiological changes to hypobaric hypoxia exposure in a cohort of Japanese lowlanders. PMID: 29625625
  5. The expression of prolyl hydroxylase domain 2 (PHD2) is selectively increased in CKD-AT-MSCs, and its inhibition can restore the expression of HIF-1alpha and the wound healing function of CKD-AT-MSCs. These findings suggest that further research into the functions of MSCs from CKD patients is necessary before their clinical application. PMID: 28537846
  6. 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 not observed in our ARDS patients of Caucasian heritage or in healthy Caucasian blood donors. PMID: 28613249
  7. This study 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
  8. PHD2 is a direct binding partner of EGFR and regulates EGFR stability and subsequent signaling in breast carcinoma cells. PMID: 28038470
  9. This study describes a mechanism of PHD2 regulation involving the mTOR and PP2A pathways. PMID: 28199842
  10. These data identify B55alpha as a PHD2 substrate and highlight a role for PHD2-B55alpha in the response to nutrient deprivation. PMID: 28329677
  11. miR-21 contributes to the protection of delayed ischemic preconditioning against renal ischemia reperfusion injury in mice, at least partially through targeting of PHD2 and subsequent up-regulation of the HIF-1alpha/VEGF pathway. PMID: 27030384
  12. Phd2 is the dominant HIF-hydroxylase in neutrophils under normoxic conditions; intrinsic regulation of glycolysis and glycogen stores is linked to the resolution of neutrophil-mediated inflammatory responses. PMID: 28805660
  13. Prolyl hydroxylase 2 plays a significant tumor suppressive role in liver cancer. PMID: 27307407
  14. Genetic variants in HIF-1alpha and PHD2 genes exist in Caucasians but do not appear to alter 30-day mortality in sepsis. PMID: 27515179
  15. This study identified a critical role of PHD2 for reversible glycolytic reprogramming in macrophages, with a direct impact on their function. PMID: 27795296
  16. Tuning the Transcriptional Response to Hypoxia by Inhibiting Hypoxia-inducible Factor (HIF) Prolyl and Asparaginyl Hydroxylases. PMID: 27502280
  17. The role of PHD-2 in breast cancer [review]. PMID: 26951539
  18. Sulfur mustard negatively affects hypoxia-stimulated HIF-1alpha signaling in keratinocytes and fibroblasts, potentially contributing to delayed wound healing in SM-injured patients, which could be treated with PHD-2 inhibitors. PMID: 26082309
  19. This study confirmed that triple-negative breast cancer cells secrete glutamate, which is both necessary and sufficient for the paracrine induction of HIF1alpha in such cells under normoxic conditions. PMID: 27368101
  20. Disulfide bond-mediated PHD2 dimerization and inactivation result in the activation of HIF-1alpha and aerobic glycolysis in response to oxidative stress. PMID: 26740011
  21. This study demonstrated that the antiapoptotic effect of TMP in CoCl2-induced HUVECs was, at least partially, through regulation of the PHD2/HIF-1alpha signaling pathway. PMID: 26676934
  22. The levels of both miR-182 and HIF1alpha were elevated, while the expression of PHD2 and FIH1 was downregulated in a mouse model of prostate cancer. PMID: 26205124
  23. These findings show that hypoxia and loss of PHD2 reverse cancer-associated fibroblast (CAF) activation. PMID: 26323721
  24. In this article, UTMD/PEI mediated gene transfection was investigated, and the US parameters were optimized. Furthermore, the biological effects of PHD2 shRNA were investigated in H9C2 cells. PMID: 26267649
  25. This study reports a genetic link between EGLN1 and VWF in a constitution-specific manner, which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia. PMID: 26047609
  26. This study demonstrated that dimethyl-2-ketoglutarate (DKG) inhibits hypoxia-inducible factor 1alpha (HIF-1alpha) proline hydroxylation and degradation mediated by prolyl-4-hydroxylase PHD2. PMID: 25420025
  27. This study revealed a striking enrichment of high-altitude ancestry in the Tibetan genome, indicating that migrants from low altitude acquired adaptive alleles from the highlanders. PMID: 24513612
  28. The kinetic properties of PHD2 and FIH with respect to oxygen reflect their cellular hypoxia-sensing ability. PMID: 26112411
  29. Germ-line PHD1 and PHD2 mutations were detected in patients with pheochromocytoma/paraganglioma-polycythemia. PMID: 25263965
  30. This study examined the association between EGLN1 and HIF-1AN single nucleotide polymorphisms and acute mountain sickness in a Han Chinese population. PMID: 25431923
  31. Compared to those with high PHD2 expressions, patients with low PHD2 expression had significantly longer DFS and OS periods. PMID: 25546659
  32. PHD2 inhibits the adaptation of glioblastoma cells to hypoxia by regulating the expression of HIF-alpha subunits. PMID: 25010988
  33. PHD2 is expressed at higher levels in normal skin compared to seborrheic keratosis, Bowen's disease, and cutaneous squamous cell carcinoma. PMID: 24354513
  34. Regulation and expression of both PHD2 and HIF-1a are important for the biology of sarcomas, and loss of PHD2 function has an additional adverse effect on the prognosis of sarcomas in tumors expressing HIF-1a. PMID: 20026900
  35. This study revealed that the Tibetan prolyl hydroxylase domain protein 2 (PHD2) haplotype (D4E/C127S) strikingly diminishes the interaction of PHD2 with heat shock protein 90 co-chaperone protein p23 (prostaglandin E synthase). PMID: 24711448
  36. The diminished expression of PHD1 and PHD2 and elevated level of FIH protein in cancerous tissue compared to histopathologically unchanged colonic mucosa was not associated with DNA methylation within the CpG islands of the PHD1, PHD2, and FIH genes. PMID: 24195777
  37. This study demonstrates that HIF-1alpha transcription and protein synthesis are controlled by TGF-beta1/Smad3 signaling, while HIF-1alpha protein stability is controlled by PHD2, which is regulated by TGF-beta1/Smad3 signaling. PMID: 23088526
  38. EGLN1 contributes to the adaptively low hemoglobin level of Tibetans compared with acclimatized lowlanders at high altitude. PMID: 23666208
  39. PHD2 regulates and hydroxylates HIF-1alpha by binding to its C-terminal domain. PMID: 23787140
  40. These studies formally prove that a missense mutation in PHD2 is the cause of the erythrocytosis, show that this occurs through haploinsufficiency, and point to multifactorial control of red cell mass by PHD2. PMID: 24121508
  41. The N-terminal region of C16 is predicted to have a PHD2-like structural fold but lacks the catalytic active site residues of PHDs. PMID: 23836663
  42. PHD2 silencing promotes adipose-derived stem cell survival in infarcted myocardia. PMID: 23694817
  43. HIF-specific hydroxylase PHD-2 may represent a relevant target for cartilage repair. PMID: 23334958
  44. Knockdown of prolyl-4-hydroxylase domain 2 inhibits tumor growth of human breast cancer MDA-MB-231 cells by affecting TGF-beta1 processing. PMID: 23225569
  45. PHD2-mediated hydroxylation of HIF-1alpha predominantly occurs in the cell nucleus and is dependent on very dynamic subcellular trafficking of PHD2. PMID: 22946054
  46. p23 recruits PHD2 to the HSP90 machinery to facilitate HIF-1alpha hydroxylation. PMID: 23413029
  47. This study unveils a unique mechanism for the regulation of HIF-1alpha stability involving ERbeta-mediated transcriptional regulation of PHD2, highlighting an unexpected role for PHD2 in maintaining epithelial differentiation. PMID: 23487784
  48. This study scrutinizes the unfolding pathways of the PHD2 catalytic domain's possible species and demonstrates the properties of their unfolding states by computational approaches. PMID: 23077544
  49. PHD2 may directly interact with PDE4D to function as a novel regulator of intracellular cAMP levels in cardiomyocytes. PMID: 22975349
  50. The prevalence of risk alleles in high altitude pulmonary edema and the protective alleles in healthy Lakakhi highland natives have provided us with allelic variants at the same locus that are involved in disease and adaptation. PMID: 23130672

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Database Links

HGNC: 1232

OMIM: 606425

KEGG: hsa:54583

STRING: 9606.ENSP00000355601

UniGene: Hs.444450

Involvement In Disease
Erythrocytosis, familial, 3 (ECYT3)
Subcellular Location
Cytoplasm. Nucleus.
Tissue Specificity
According to PubMed:11056053, widely expressed with highest levels in skeletal muscle and heart, moderate levels in pancreas, brain (dopaminergic neurons of adult and fetal substantia nigra) and kidney, and lower levels in lung and liver. According to Pub

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