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Validated All-in-One™ qPCR Primer for EGLN1(NM_022051.2) Search again
Product ID:
HQP054538
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
C1orf12, ECYT3, HALAH, HIF-PH2, HIFPH2, HPH-2, HPH2, PHD2, SM20, ZMYND6
Gene Description:
egl-9 family hypoxia inducible factor 1
Target Gene Accession:
NM_022051.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Gene References into function
- PHD2 is the critical oxygen sensor setting the low steady-state levels of HIF-1alpha in normoxia. It is upregulated by oxygen.
- we demonstrate that PHD2 is not affected by overexpression or downregulation of HIF-2alpha
- PHD1, PHD2, and PHD3 have roles in the regulation of hypoxia-inducible factor
- The phd2 gene is transcribed exclusively from the downstream promoter that contains a functional hypoxia-responsive, cis-regulatory element.
- the N-terminal region of PHD2 contains a Myeloid translocation protein 8, Nervy, and DEAF1 (MYND)-type zinc finger domain, whereas the catalytic domain is located in its C-terminal region; the MYND domain inhibits the catalytic activity of PHD2
- Accumulated EGLN1 in hypoxia acts as a negative-feedback mechanism to modulate HIF-1alpha target gene expression.
- EGLN1 can be considered as a candidate tumor suppressor on chromosome 1q, and our observation could open the new aspect in exploring the machinery of senescence induction associated with hypoxia-inducible factor 1, alpha signal transduction
- Critical for normal regulation of hypoxia-inducible factor.
- PHD2 shows strongly elevated expression both at the mRNA and protein level in head and neck squamous cell carcinoma.
- Crystal structures of the catalytic domain of human PHD2 were described.
- a novel mechanism by which a growth factor controls hypoxia-inducible transcription factor-1 (HIF-1alpha)stability, and thereby drives the expression of specific genes, through the regulation of PHD2 levels
- A recombinant form of a human prolyl-4-hydroxylase (PHD2) was characterised and shown to have an unexpectedly high affinity for, and to copurify with endogenous levels of, its Fe(ii) cofactor and 2-oxoglutarate cosubstrate.
- PHD2 induction is an underlying mechanism of NO-induced degradation of HIF-1alpha
- Data suggest that the peptidyl prolyl cis/trans isomerase FKBP38 determines hypoxia-inducible transcription factor prolyl-4-hydroxylase PHD2 protein stability.
- PHD2 mutation is associated with abnormal erythrocytosis
- PHD inhibitors preferentially bind to the active site of PHD2 and stabilize HIF activity, induce angiogenesis and protect against cerebral ischemia.
- Genetic defects are first frameshift and nonsense mutations reported in PHD2 gene and suggest that a decreased prolyl hydroxylase activity disturbing the oxygen-sensing pathway might be the cause of erythrocytosis.
- PHD2 does not mediate the TCDD-mediated HIF-1 alpha destabilization nor control the interference of AhR and HIF-1 alpha pathways.
- Chronic hypoxia not only increases the pool of PHDs but also overactivates the three PHD isoforms.
- PHD2 has a role in modulating tumor-forming potential
- suggest a role for PHD2 as a decisive oxygen sensor of the hypoxia-inducible factor degradation pathway within the cell nucleus
- Biochemical characterization of PHD2 variants associated with polycythemia is reported.