PHD3 catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins, hydroxylates HIF-1 alpha at Pro-564, and also hydroxylates HIF-2 alpha.
| Inventor | Institute |
|---|---|
| Helen Turley | University of Oxford |
| Cat. #: | 151315 |
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| Tool sub type: | Primary antibody |
| Unit size: | 100 ug |
| Research Fields: | Cancer;Genetics;Metabolism;Tissue-specific biology |
| Application: | IHC ; WB |
| Target: | Prolyl Hydroxylase 3 (PHD3) |
| Reactivity: | Human |
| Clone: | EG188e/d5 |
| Host: | Mouse |
| Class: | Monoclonal |
| Product description: | PHD3 catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins, hydroxylates HIF-1 alpha at Pro-564, and also hydroxylates HIF-2 alpha. It functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitylation complex. It may play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissue. It promotes cell death through a caspase-dependent mechanism |
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| Conjugation: | Unconjugated |
| Isotype: | IgG1 |
| Molecular weight: | 27.3 kDa |
| Immunogen: | Residues 1-100 of human PHD3 |
| Myeloma used: | P3/NS1/1-Ag4.1 |
| Target background: | PHD3 catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins, hydroxylates HIF-1 alpha at Pro-564, and also hydroxylates HIF-2 alpha. It functions as a cellular oxygen sensor and, under normoxic conditions, targets HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitylation complex. It may play a role in cell growth regulation in muscle cells and in apoptosis in neuronal tissue. It promotes cell death through a caspase-dependent mechanism |
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| Format: | Liquid |
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| Concentration: | 1 mg/ml |
| Storage buffer: | PBS with 0.02% azide |
| Storage conditions: | -15° C to -25° C |
| Shipping conditions: | Dry ice |
| References: |
Fujita et al. 2012. J Biol Chem. 287(47):39942-53. PMID: 22948157. Prolyl hydroxylase 3 (PHD3) modulates catabolic effects of tumor necrosis factor-a (TNF-a) on cells of the nucleus pulposus through co-activation of nuclear factor B (NF-B)/p65 signaling. Soilleux et al. 2005. Histopathology. 47(6):602-10. PMID: 16324198. Use of novel monoclonal antibodies to determine the expression and distribution of the hypoxia regulatory factors PHD-1, PHD-2, PHD-3 and FIH in normal and neoplastic human tissues. Stolze et al. 2004. J Biol Chem. 279(41):42719-25. PMID: 15302861. Appelhoff et al. 2004. J Biol Chem. 279(37):38458-65. PMID: 15247232. Genetic analysis of the role of the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH) in regulating hypoxia-inducible factor (HIF) transcriptional target genes [corrected]. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. |
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