Recombinant Human EGLN1/PHD2 GST (N-Term) Protein

Recombinant Human EGLN1/PHD2 GST (N-Term) Protein [H00054583-P01] - Analysis by 12.5% SDS-PAGE. Gel stained with Coomassie Blue.

• Reactivity: Hu
• Applications: WB, ELISA, Func, MA, AP, Enzyme Activity

Recombinant Human EGLN1/PHD2 GST (N-Term) Protein Summary

• Description: A recombinant protein with GST tag at N-terminal corresponding to the amino acids 1-128 of Human EGLN1.
  

  Source: Wheat Germ (in vitro)

  Amino Acid Sequence: MVACYPGNGTGYVRHVDNPNGDGRCVTCIYYLNKDWDAKVSGGILRIFPEGKAQFADIEPKFDRLLFFWSDRRNPHEVQPAYATRYAITVWYFDADERARAKVKYLTGEKGVRVELNKPSDSVGKDVF

• Preparation Method: In vitro wheat germ expression system
• Details of Functionality: This protein was produced in an in vitro wheat germ expression system that should preserve correct conformational folding that is necessary for biological function. While it is possible that this protein could display some level of activity, the functionality of this protein has not been explicitly measured or validated.
• Source: Wheat germ
• Protein/Peptide Type: Recombinant Protein
• Gene: EGLN1
• Purity: >80% by SDS-PAGE and Coomassie blue staining

Applications/Dilutions

• Dilutions:
  • ELISA
  • Enzyme Activity
  • Immunoaffinity Purification
  • In vitro assay
  • Protein Array
  • Western Blot
• Theoretical MW: 41 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at -80C. Avoid freeze-thaw cycles.
• Buffer: Elution buffer: 50 mM Tris-HCl, 10 mM reduced Glutathione, pH 8.0
• Preservative: No Preservative
• Purity: >80% by SDS-PAGE and Coomassie blue staining

Notes

This product is produced by and distributed for Abnova, a company based in Taiwan.

Alternate Names for Recombinant Human EGLN1/PHD2 GST (N-Term) Protein

• C1orf12
• EC 1.14.11.29
• EC:1.14.11.291
• ECYT3
• egl nine homolog 1
• egl nine-like protein 1
• EGLN1
• HALAH
• 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

Background

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.

References

1. Amorim-Pires, D., Peixoto, J., & Lima, J. (2016). Hypoxia Pathway Mutations in Pheochromocytomas and Paragangliomas. Cytogenetic and genome research. https://doi.org/10.1159/000457479

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.). https://doi.org/10.2147/HP.S54455

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. https://doi.org/10.1016/j.biochi.2015.07.009

4. Semenza G. L. (2007). Hypoxia-inducible factor 1 (HIF-1) pathway. Science's STKE : signal transduction knowledge environment. https://doi.org/10.1126/stke.4072007cm8

5. Chan, D. A., & Giaccia, A. J. (2010). PHD2 in tumour angiogenesis. British journal of cancer. https://doi.org/10.1038/sj.bjc.6605682

6. Meneses, A. M., & Wielockx, B. (2016). PHD2: from hypoxia regulation to disease progression. Hypoxia (Auckland, N.Z.). https://doi.org/10.2147/HP.S53576

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Publications for EGLN1/PHD2 Full Length Recombinant Protein (H00054583-P01)(2)

Publications using H00054583-P01

• Li Z, Zhou W, Zhang Y et al. ERK regulates HIF-1 alpha-mediated platinum resistance by directly targeting PHD2 in ovarian cancer Clin. Cancer Res. 2019-07-08 [PMID: 31285371] (In vitro, Human)
• Vidimar V, Licona C, Ceron-Camacho R et al. A redox ruthenium compound directly targets PHD2 and inhibits the HIF1 pathway to reduce tumor angiogenesis independently of p53. Cancer Lett. [PMID: 30339780] (EnzAct, Human)

Bioinformatics

• Gene Symbol: EGLN1