366G/76/3 recognises human prolyl hydroxylase 2 (PHD2), a 46kDa enzyme expressed abundantly in all tissues with the highest expression in testis
| Inventor | Institute |
|---|---|
| Helen Turley | University of Oxford |
| Cat. #: | 151314 |
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| Tool sub type: | Primary antibody |
| Unit size: | 100 ug |
| Research Fields: | Cancer;Genetics;Metabolism;Tissue-specific biology |
| Application: | FACS ; IHC ; WB |
| Target: | Prolyl Hydroxylase 2 (PHD2) |
| Reactivity: | Human |
| Clone: | 366G/76/3 |
| Host: | Mouse |
| Class: | Monoclonal |
| Product description: | 366G/76/3 recognises human prolyl hydroxylase 2 (PHD2), a 46kDa enzyme expressed abundantly in all tissues with the highest expression in testis |
|---|---|
| Conjugation: | Unconjugated |
| Isotype: | IgG1 |
| Molecular weight: | 46.1 kDa |
| Immunogen: | Residues 1-24 of PHD2 |
| Myeloma used: | P3/NS1/1-Ag4.1 |
| Target background: | Hypoxia inducible factor-1 (HIF-1) is a transcriptional complex, consisting of an alpha and beta subunit, which plays a key role in coordinating the cellular response to hypoxia. During normal oxygen conditions, the alpha subunit of HIF-1 is rapidly degraded, however when hypoxia occurs this degradation is suppressed and HIF-1 activates the transcription of various genes important for survival and adaptation to hypoxia. Prolyl hydroxylase 2 catalyses the hydroxylation of specific prolyl residues within the HIF-1 alpha subunit, thereby targeting this subunit for degradation. |
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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: |
Jubb et al. 2009. Br J Cancer. 101(10):1749-57. PMID: 19844231. Expression of delta-like ligand 4 (Dll4) and markers of hypoxia in colon cancer. 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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