Recombinant Human Egl nine homolog 1 (EGLN1), partial

Code CSB-EP863932HU1
Size $306
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Greater than 90% as determined by SDS-PAGE.
Target Names
Uniprot No.
Research Area
Alternative Names
(Hypoxia-inducible factor prolyl hydroxylase 2)(HIF-PH2)(HIF-prolyl hydroxylase 2)(HPH-2)(Prolyl hydroxylase domain-containing protein 2)(PHD2)(SM-20)
Homo sapiens (Human)
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
31.9 kDa
Protein Length
Tag Info
N-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
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Target Background

Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized 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 that inhibits ferroptosis PMID: 28900510
  2. In vitro studies showed 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 the regulation of HIF1alpha stability. Accumulation of HIF1alpha, resulting from GPT2-alpha-ketoglutarate-PHD2 axis, constitutively activates sonic hedgehog (Shh) signaling pathway. PMID: 28839461
  4. Studied the association between SNPs around the EGLN1 genomic region, possibly 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 results indicate that more studies about the functions of MSCs from CKD patients are required before they can be applied in the clinical setting 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 neither present in our ARDS patients of Caucasian heritage nor in healthy Caucasian blood donors. PMID: 28613249
  7. 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
  8. PHD2 is a direct binding partner of EGFR and show that PHD2 regulates EGFR stability as well as its subsequent signaling in breast carcinoma cells. PMID: 28038470
  9. A mechanism of PHD2 regulation that involves the mTOR and PP2A pathways. PMID: 28199842
  10. These data unravel 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, which is at least in part mediated by targeting of PHD2 and subsequently up-regulating 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 an important 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. Results identified a critical role of PHD2 for a 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 and thus possibly contributes to delayed wound healing in SM-injured patients, which could be treated with PHD-2 inhibitors. PMID: 26082309
  19. The HIFalpha subunit is usually prolyl-hydroxylated by EglN family members under normoxic conditions, causing its rapid degradation. 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. The present study demonstrated that the antiapoptotic effect of TMP in CoCl2-induced HUVECs was, at least in part, via the regulation of the PHD2/HIF-1alpha signaling pathway. PMID: 26676934
  22. 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. PMID: 26205124
  23. findings show hypoxia and loss of PHD2 revert 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. a genetic link between EGLN1 and VWF in a constitution specific manner which could modulate thrombosis/bleeding susceptibility and outcomes of hypoxia, is reported. PMID: 26047609
  26. Data show 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. 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 detected in patients with pheochromocytoma/paraganglioma-polycythemia PMID: 25263965
  30. The association between EGLN1 and HIF-1AN single nucleotide polymorphisms and acute mountain sickness in a Han Chinese population, was examined. 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. higher expression 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 to the biology of sarcomas, and loss of PHD2 function has an additional adverse effect in the prognosis of sarcomas in tumors expressing HIF-1a. PMID: 20026900
  35. Data indicate 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. results demonstrate that HIF-1alpha transcription and protein synthesis are controlled by TGF-beta1/Smad3 signaling, whereas 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. a unique mechanism for the regulation of HIF-1alpha stability that involves ERbeta-mediated transcriptional regulation of PHD2 and they highlight an unexpected role for PHD2 in maintaining epithelial differentiation. PMID: 23487784
  48. The 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 the intracellular cAMP levels in cardiomyocytes. PMID: 22975349
  50. prevalence of the 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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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
Database Links

HGNC: 1232

OMIM: 606425

KEGG: hsa:54583

STRING: 9606.ENSP00000355601

UniGene: Hs.444450

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