EGLN1/PHD2 Antibody [DyLight 488]


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Product Details

Reactivity Hu, Mu, RtSpecies Glossary
Applications WB, ICC/IF, IHC, IP, KD, KO
DyLight 488

Order Details

EGLN1/PHD2 Antibody [DyLight 488] Summary

This EGLN1/PHD2 antibody was developed against a synthetic peptide made to an internal portion of mouse PHD2/HIF Prolyl Hydroxylase 2 (between residues 300-400). [Uniprot: Q91YE3]
Immunogen affinity purified
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  • Immunocytochemistry/ Immunofluorescence
  • Immunohistochemistry
  • Immunohistochemistry-Paraffin
  • Immunoprecipitation
  • Knockdown Validated
  • Knockout Validated
  • Western Blot
Application Notes
Optimal dilution of this antibody should be experimentally determined.

Packaging, Storage & Formulations

Store at 4C in the dark.
50mM Sodium Borate
0.05% Sodium Azide
Immunogen affinity purified


DyLight (R) is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.

Alternate Names for EGLN1/PHD2 Antibody [DyLight 488]

  • C1orf12
  • EC
  • EC:
  • ECYT3
  • egl nine homolog 1
  • egl nine-like protein 1
  • EGLN1
  • HIF prolyl hydroxylase 2
  • HIFPH2
  • HIF-PH2
  • HIF-prolyl hydroxylase 2
  • HPH2
  • HPH-2
  • Hypoxia-inducible factor prolyl hydroxylase 2
  • PHD2
  • PNAS-118
  • PNAS-137
  • Prolyl hydroxylase domain-containing protein 2
  • SM20
  • SM-20
  • zinc finger MYND domain-containing protein 6
  • ZMYND6


PHD2 (Prolyl Hydroxylase Domain-containing protein 2) belongs to the Prolyl-4-hydroxylase domain (PHD) family of proteins and is encoded by the Egl-9 Family Hypoxia Inducible Factor 1 (EGLN1) gene (1). Human EGLN1/PHD2 is a ubiquitously expressed enzyme that is 426 amino acids (aa) long with a theoretical molecular weight of ~46 kDa. Structurally PHD2 contains a nuclear export signal (NES, aa 6-20), an N-terminal MYND zinc finger domain (aa 21-58), and a C-terminal catalytic domain (aa 291-392) (2, 3). Functionally, PHD2 serves as an oxygen sensor and is responsible for post-translational modification of Hypoxia-inducible factor alpha (HIF-1alpha), a component of a transcriptional complex involved in oxygen homeostasis (1-3). During normoxia, PHD2 is responsible for oxygen-dependent hydroxylation of HIF-1alpha proline residue 402, 564, or both (3). The hydroxylation event promotes the binding of von Hippel-Lindau protein (VHL) and targets HIF1-alpha for ubiquitination and degradation (4, 5).

EGLN1/PHD2 has been implicated in several critical processes including erythropoiesis, angiogenesis, and metabolism as well as various pathologies such as cancer (2, 5, 6). Studies in mice have found that somatic deletion of PHD2 resulted in higher vascular endothelial growth factor A (VEGF-A) levels, increased blood vessel formation, and more erythropoietin (EPO), leading to severe polycythemia or erythrocytosis (high red blood cell (RBC) volume) (6). Another study revealed that specific point mutations in EGLN1/PHD2 led to elevated EPO and RBC mass associated with hemorrhages and strokes (6). Accordingly, given the known role of PHD2 in inhibition of EPO production, PHD2 inhibitors are being studied as a potential therapeutic for anemia (6). Additionally, dysregulation in EGLN1, and specifically the PHD2-VHL-HIF-1alpha pathway, has been associated with the development of pheochromocytomas (PCC) and sympathetic paragangliomas (PGL), which are rare neuroendocrine tumors (2). Besides pathological features, EGLN1/PHD2 may also be important for high altitude adaptation as two coding sequence variants in PHD2 are prevalent in the Tibetan population but is very rare in people at lower altitudes (2).

Alternate names for EGLN1/PHD2 include HIF Prolyl Hydroxylase 2, PH2, Prolyl hydroxylase domain containing protein 2, HIF2PH2, HIF-Prolyl hydroxylase 2, egl nine homolog 1, and C1orf12.


1. Amorim-Pires, D., Peixoto, J., & Lima, J. (2016). Hypoxia Pathway Mutations in Pheochromocytomas and Paragangliomas. Cytogenetic and genome research.

2. Gardie, B., Percy, M. J., Hoogewijs, D., Chowdhury, R., Bento, C., Arsenault, P. R., Richard, S., Almeida, H., Ewing, J., Lambert, F., McMullin, M. F., Schofield, C. J., & Lee, F. S. (2014). The role of PHD2 mutations in the pathogenesis of erythrocytosis. Hypoxia (Auckland, N.Z.).

3. Minervini, G., Quaglia, F., & Tosatto, S. C. (2015). Insights into the proline hydroxylase (PHD) family, molecular evolution and its impact on human health. Biochimie.

4. Semenza G. L. (2007). Hypoxia-inducible factor 1 (HIF-1) pathway. Science's STKE : signal transduction knowledge environment.

5. Chan, D. A., & Giaccia, A. J. (2010). PHD2 in tumour angiogenesis. British journal of cancer.

6. Meneses, A. M., & Wielockx, B. (2016). PHD2: from hypoxia regulation to disease progression. Hypoxia (Auckland, N.Z.).


This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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Gene Symbol EGLN1