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Mouse Anti-EGLN1 (AA 1-24) Recombinant Antibody (366G/76/3) (CBMAB-E0124-FY)

This product is mouse antibody that recognizes EGLN1. The antibody 366G/76/3 can be used for immunoassay techniques such as: IHC, WB.
See all EGLN1 antibodies
Published Data
Fig.1 Immunoblots demonstrating PHD proteins in different cell lines.
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Fig.2 Immunoblot demonstrating specificity of siRNA-based suppression of PHDs.
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Fig.3 Immunostaining of a follicular lymphoma with PHD-2 demonstrates predominantly cytoplasmic staining of tumour cells, which is strongest with FIH and PHD-2.
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Summary

Host Animal
Mouse
Specificity
Human
Clone
366G/76/3
Antibody Isotype
IgG1
Application
IHC, WB

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, pH 7.4
Preservative
0.01% Thiomersal
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1-24

Target

Full Name
Egl-9 Family Hypoxia Inducible Factor 1
Introduction
The protein encoded by this gene catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. HIF is a transcriptional complex that plays a central role in mammalian oxygen homeostasis. This protein functions as a cellular oxygen sensor, and under normal oxygen concentration, modification by prolyl hydroxylation is a key regulatory event that targets HIF subunits for proteasomal destruction via the von Hippel-Lindau ubiquitylation complex. Mutations in this gene are associated with erythrocytosis familial type 3 (ECYT3).
Entrez Gene ID
54583
UniProt ID
Q9GZT9
Alternative Names
Egl-9 Family Hypoxia Inducible Factor 1; Prolyl Hydroxylase Domain-Containing Protein 2; Hypoxia-Inducible Factor Prolyl Hydroxylase 2; HIF-Prolyl Hydroxylase 2; C1orf12; HIF-PH2; HPH-2; PHD2; Zinc Finger MYND Domain-Containing Protein 6; Egl-9 Family Hypoxia-Inducible Factor 1; Egl Nine Homolog 1 (C. Elegans); EGL Nine (C.Elegans) Homolog 1; HIF Prolyl Hydroxylase 2
Research Area
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.
Biological Process
Cellular response to hypoxia Source: GO_Central
Negative regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
Negative regulation of DNA-binding transcription factor activity Source: HGNC-UCL
Oxygen homeostasis Source: HGNC-UCL
Peptidyl-proline hydroxylation to 4-hydroxy-L-proline Source: FlyBase
Regulation of angiogenesis Source: UniProtKB
Response to hypoxia Source: HGNC-UCL
Response to nitric oxide Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm. Mainly cytoplasmic. Shuttles between the nucleus and cytoplasm (PubMed:19631610). Nuclear export requires functional XPO1.
Involvement in disease
Erythrocytosis, familial, 3 (ECYT3):
An autosomal dominant disorder characterized by elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.
PTM
S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe2+ has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-323 or Cys-326.

Tang, J., Deng, H., Wang, Z., Zha, H., Liao, Q., Zhu, C., ... & Xiao, W. (2022). EGLN1 prolyl hydroxylation of hypoxia-induced transcription factor HIF1α is repressed by SET7-catalyzed lysine methylation. Journal of Biological Chemistry, 298(6).

Gangat, N., Oliveira, J. L., Porter, T. R., Hoyer, J. D., Al-Kali, A., Patnaik, M. M., ... & Tefferi, A. (2022). Erythrocytosis associated with EPAS1 (HIF2A), EGLN1 (PHD2), VHL, EPOR or BPGM mutations: the Mayo Clinic experience. Haematologica, 107(5), 1201.

Reggiani, F., Sauta, E., Torricelli, F., Zanetti, E., Tagliavini, E., Santandrea, G., ... & Sancisi, V. (2021). An integrative functional genomics approach reveals EGLN1 as a novel therapeutic target in KRAS mutated lung adenocarcinoma. Molecular Cancer, 20(1), 1-6.

Bonnin, A., Gardie, B., Girodon, F., Airaud, F., Garrec, C., Bézieau, S., ... & Lellouche, F. (2020). A new case of rare erythrocytosis due to EGLN1 mutation with review of the literature. La Revue de Medecine Interne, 41(3), 196-199.

Moore, J. A., Hubbi, M. E., Wang, C., Wang, Y., Luo, W., Hofmann, S., & Rambally, S. (2020). Isolated Erythrocytosis Associated With 3 Novel Missense Mutations in the EGLN1 Gene. Journal of Investigative Medicine High Impact Case Reports, 8, 2324709620947256.

Liu, G., Zhao, W., Zhang, H., Wang, T., Han, Z., & Ji, X. (2020). rs1769793 variant reduces EGLN1 expression in skeletal muscle and hippocampus and contributes to high aerobic capacity in hypoxia. Proceedings of the National Academy of Sciences, 117(47), 29283-29285.

Yasukochi, Y., Nishimura, T., Ugarte, J., Ohnishi, M., Nishihara, M., Alvarez, G., ... & Aoyagi, K. (2020). Effect of EGLN1 genetic polymorphisms on hemoglobin concentration in Andean highlanders. BioMed research international, 2020.

Price, C., Gill, S., Ho, Z. V., Davidson, S. M., Merkel, E., McFarland, J. M., ... & Hahn, W. C. (2019). Genome-wide interrogation of human cancers identifies EGLN1 dependency in clear cell ovarian cancers. Cancer research, 79(10), 2564-2579.

Heinrich, E. C., Wu, L., Lawrence, E. S., Cole, A. M., Anza‐Ramirez, C., Villafuerte, F. C., & Simonson, T. S. (2019). Genetic variants at the EGLN1 locus associated with high‐altitude adaptation in Tibetans are absent or found at low frequency in highland Andeans. Annals of human genetics, 83(3), 171-176.

Graham, A. M., & McCracken, K. G. (2019). Convergent evolution on the hypoxia-inducible factor (HIF) pathway genes EGLN1 and EPAS1 in high-altitude ducks. Heredity, 122(6), 819-832.

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For research use only. Not intended for any clinical use.

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